Category in women undergoing in vitro fertilisation.

Generation and characterization of a human-mouse chimeric high-affinity antibody that detects the DYKDDDDK FLAG peptide

DYKDDDDK peptide (FLAG) is a useful tool for investigating the function and localization of proteins whose antibodies (Abs) are not available. We recently established a high-affinity monoclonal antibody (mAb) for FLAG (clone 2H8).
The 2H8 Ab is highly sensitive for detecting FLAG-tagged proteins by flowcytometry and immunoprecipitation, but it can yield nonspecific signals in the immunohistochemistry of mouse tissues because it is of mouse origin. In this study, we reduced nonspecific signals by generating a chimeric 2H8 Ab with Fc fragments derived from human immunoglobulin.
We fused a 5′ terminal cDNA fragments for the Fab region of 2H8 mAb with 3′ terminal cDNA fragments for Fc region of human IgG1. We transfected both chimeric plasmids and purified the resulting human-mouse chimeric 2H8. The chimeric 2H8 Ab successfully detected FLAG-tagged proteins in flow cytometry with anti-human IgG secondary Ab with comparable sensitivity to 2H8 mAb.
Importantly, chimeric 2H8 detected specific FLAG peptide signals without nonspecific signals in immunohistochemical analysis with mouse tissues. This human-mouse chimeric high-affinity anti-FLAG Ab will prove useful for future immunohistochemical analysis of mouse tissues.

Thoracic Society of Australia and New Zealand Position Statement on Acute Oxygen Use in Adults: ‘Swimming between the flags

Oxygen is a life-saving therapy but, when given inappropriately, may also be hazardous. Therefore, in the acute medical setting, oxygen should only be given as treatment for hypoxaemia and requires appropriate prescription, monitoring and review.
This update to the Thoracic Society of Australia and New Zealand (TSANZ) guidance on acute oxygen therapy is a brief and practical resource for all healthcare workers involved with administering oxygen therapy to adults in the acute medical setting.
It does not apply to intubated or paediatric patients. Recommendations are made in the following six clinical areas: assessment of hypoxaemia (including use of arterial blood gases); prescription of oxygen; peripheral oxygen saturation targets; delivery, including non-invasive ventilation and humidified high-flow nasal cannulae; the significance of high oxygen requirements; and acute hypercapnic respiratory failure.
There are three sections which provide (1) a brief summary, (2) recommendations in detail with practice points and (3) a detailed explanation of the reasoning and evidence behind the recommendations. It is anticipated that these recommendations will be disseminated widely in structured programmes across Australia and New Zealand.

Decitabine and Vorinostat with FLAG Chemotherapy in Pediatric Relapsed/Refractory AML: Report from the Therapeutic Advances in Childhood Leukemia and Lymphoma (TACL) Consortium

Survival outcomes for relapsed/refractory pediatric acute myeloid leukemia (R/R AML) remain dismal. Epigenetic changes can result in gene expression alterations which are thought to contribute to both leukemogenesis and chemotherapy resistance.
We report results from a phase I trial with a dose expansion cohort investigating decitabine and vorinostat in combination with fludarabine, cytarabine, and G-CSF (FLAG) in pediatric patients with R/R AML [NCT02412475]. Thirty-seven patients enrolled with a median age at enrollment of 8.4 (range, 1-20) years. There were no dose limiting toxicities among the enrolled patients, including two patients with Down syndrome. The recommended phase 2 dose of decitabine in combination with vorinostat and FLAG was 10 mg/m2 .
The expanded cohort design allowed for an efficacy evaluation and the overall response rate among 35 evaluable patients was 54% (16 complete response (CR) and 3 complete response with incomplete hematologic recovery (CRi)). Ninety percent of responders achieved minimal residual disease (MRD) negativity (<0.1%) by centralized flow cytometry and 84% (n=16) successfully proceeded to hematopoietic stem cell transplant.
Two-year overall survival was 75.6% [95%CI: 47.3%, 90.1%] for MRD-negative patients vs. 17.9% [95%CI: 4.4%, 38.8%] for those with residual disease (p<0.001). Twelve subjects (34%) had known epigenetic alterations with 8 (67%) achieving a CR, 7 (88%) of whom were MRD negative.
Correlative pharmacodynamics demonstrated biologic activity of decitabine and vorinostat and identified specific gene enrichment signatures in non-responding patients.
Overall, this therapy was well-tolerated, biologically active, and effective in pediatric patients with R/R AML, particularly those with epigenetic alterations. This article is protected by copyright. All rights reserved.

Dento-facial infections in children – A potential red flag for child neglect?

Background: Healthcare professionals are often confronted with children presenting to the emergency department with dento-facial infections. These infections may be associated with dental neglect and as such could be a marker for general neglect. The aim of this retrospective study was to ascertain whether dento-facial infections can be used as an indicator for general neglect.
Method: All children aged 16 years and under, who were admitted for surgical incision and drainage of dento-facial infection between January 2017 and January 2019 at King’s College Hospital were examined retrospectively. All patients were discussed with the local safeguarding team/local authority to establish whether they were previously known to social services.
Results: This study showed that in our cohort, 48% of children admitted with dento-facial infection were already known to social services and one (2%) had been recently referred. The most commonly affected age group were 5-8-year-olds (50%) indicating that these children have an increased risk of neglect. An average of 5.6 teeth were extracted and four (10%) patients required extra-oral drainage. The average hospital stay was 2.26 days.
Conclusion: Our retrospective study revealed that social services were already aware of 48% of patients under the age of 16, who were admitted to hospital with a dento-facial infection.
This suggests a relationship between dental neglect and generalised neglect. Families of children presenting with dento-facial infection should be supported in accessing appropriate dental services for their children and clinicians should consider dento-facial infection a potential ‘red flag’ for generalised neglect.
Keywords: Child neglect; Dental neglect; Dento-facial infections; Maxillofacial.

Reduced Expression of Emotion: A Red Flag Signalling Conversion to Psychosis in Clinical High Risk for Psychosis (CHR-P) Populations

Objective: In this hypothesis-testing study, which is based on findings from a previous atheoretical machine-learning study, we test the predictive power of baseline “reduced expression of emotion” for psychosis.Method: Study participants (N = 96, mean age 16.55 years) were recruited from the Prevention of Psychosis Study in Rogaland, Norway. The Structured Interview for Prodromal Syndromes (SIPS) was conducted 13 times over two years. Reduced expression of emotion was added to positive symptoms at baseline (P1-P5) as a predictor of psychosis onset over a two-year period using logistic regression.
Results: Participants with a score above zero on expression of emotion had over eight times the odds of conversion (OR = 8.69, p < .001).
Data indicated a significant dose-response association. A model including reduced expression of emotion at baseline together with the positive symptoms of the SIPS rendered the latter statistically insignificant.

Recombinant Human APOA5 Protein, Flag Tag, E.coli-1mg

QP11046-FLAG-1mg EnQuireBio 1mg 5251 EUR

Recombinant Canine Clusterin Protein, Flag Tag, E.coli-1mg

QP11455-FLAG-1mg EnQuireBio 1mg 5251 EUR

Recombinant Canine Clusterin Protein, Flag Tag, E.coli-2ug

QP11455-FLAG-2ug EnQuireBio 2ug 155 EUR

Recombinant Human PEDF Protein, Flag Tag, E.coli-100ug

QP13005-FLAG-100ug EnQuireBio 100ug 1161 EUR

Recombinant Human PEDF Protein, Flag Tag, E.coli-10ug

QP13005-FLAG-10ug EnQuireBio 10ug 201 EUR

Recombinant Human PEDF Protein, Flag Tag, E.coli-2ug

QP13005-FLAG-2ug EnQuireBio 2ug 155 EUR

FLAG Octapeptide (FLAG) Antibody

20-abx132268 Abbexa
  • 439.00 EUR
  • 133.00 EUR
  • 1233.00 EUR
  • 592.00 EUR
  • 328.00 EUR
  • 100 ug
  • 10 ug
  • 1 mg
  • 200 ug
  • 50 ug

FLAG Octapeptide (FLAG) Antibody

20-abx130436 Abbexa
  • 398.00 EUR
  • 996.00 EUR
  • 495.00 EUR
  • 154.00 EUR
  • 286.00 EUR
  • 100 ug
  • 1 mg
  • 200 ug
  • 20 ug
  • 50 ug

FLAG Octapeptide (Flag) Antibody

20-abx118001 Abbexa
  • 551.00 EUR
  • 481.00 EUR
  • 100 ul
  • 50 ul

FLAG Octapeptide (Flag) Antibody

abx016078-100ul Abbexa 100 ul 411 EUR

FLAG Octapeptide (FLAG) Peptide

20-abx652293 Abbexa
  • 523.00 EUR
  • 244.00 EUR
  • 1497.00 EUR
  • 606.00 EUR
  • 384.00 EUR
  • 100 ug
  • 10 ug
  • 1 mg
  • 200 ug
  • 50 ug

Synthetic FLAG Octapeptide (FLAG)

4-SPX159Ge01 Cloud-Clone
  • 368.80 EUR
  • 202.00 EUR
  • 1108.00 EUR
  • 436.00 EUR
  • 772.00 EUR
  • 310.00 EUR
  • 2620.00 EUR
  • 100 ug
  • 10ug
  • 1 mg
  • 200 ug
  • 500 ug
  • 50ug
  • 5 mg

FLAG Octapeptide (FLAG) Peptide (OVA)

20-abx651286 Abbexa
  • 272.00 EUR
  • 189.00 EUR
  • 606.00 EUR
  • 300.00 EUR
  • 230.00 EUR
  • 100 ug
  • 10 ug
  • 1 mg
  • 200 ug
  • 50 ug
Conclusions: The study findings confirm findings from the previous machine-learning study, indicating that observing reduced expression of emotion may serve two purposes: first, it may add predictive value to psychosis conversion, and second, it is readily observable.
This may facilitate detection of those most at risk within the clinical high risk of psychosis population, as well as those at clinical high risk. A next step could be including this symptom within current high-risk criteria. Future research should consolidate these findings.

In-silico evidence for enhancement of avian influenza virus H9N2 virulence by modulation of its hemagglutinin (HA) antigen function and stability during co-infection with infectious bronchitis virus in chickens

In the last few decades, frequent incidences of avian influenza (AI) H9N2 outbreaks have caused high mortality in poultry farms resulting in colossal economic losses in several countries. In Egypt, the co-infection of H9N2 with the infectious bronchitis virus (IBV) has been observed extensively during these outbreaks. However, the pathogenicity of H9N2 in these outbreaks remained controversial.
The current study reports isolation and characterization of the H9N2 virus recovered from a concurrent IBV infected broiler chicken flock in Egypt during 2011. The genomic RNA was subjected to RT-PCR amplification followed by sequencing and analysis. The deduced amino acid sequences of the eight segments of the current study H9N2 isolate were compared with those of Egyptian H9N2 viruses isolated from healthy and diseased chicken flocks from 2011 to 2013.
In the phylogenetic analysis, the current study isolate was found to be closely related to the other Egyptian H9N2 viruses. Notably, no particular molecular characteristic difference was noticed among all the Egyptian H9N2 isolates from apparently healthy, diseased or co-infected with IBV chicken flocks.
Nevertheless, in-silico analysis, we noted modulation of stability and motifs structure of Hemagglutinin (HA) antigen among the co-infecting H9N2 AI and the IBV and isolates from the diseased flocks. The findings suggest that the putative factor for enhancement of the H9N2 pathogenicity could be co-infection with other respiratory pathogens such as IBV that might change the HA stability and function.

Recombinant bluetongue virus with hemagglutinin epitopes in VP2 has potential as a labeled vaccine

Bluetongue (BT) is an arbovirus-borne disease of ruminants caused by bluetongue virus (BTV) that has the potential to have a serious economic impact.
Currently available commercial vaccines include attenuated vaccines and inactivated vaccines, both of which have achieved great success in the prevention and control of BTV. However, these vaccines cannot distinguish between infected animals and immunized animals.
To control outbreaks of BTV, the development of labeled vaccines is urgently needed. In this study, we used the plasmid-based reverse genetics system (RGS) of BTV to rescue four recombinant viruses in which HA (influenza hemagglutinin) tags were inserted at different sites of VP2.
In vitro, the recombinant tagged viruses exhibited morphologies, plaque, and growth kinetics similar to the parental BTV-16, and expressed both VP2 and HA tag.
Subsequently, the selected recombinant tagged viruses were prepared as inactivated vaccines to immunize IFNAR(-/-) mice and sheep, and serological detection results of an anti-HA antibody provided discriminative detection. In summary, we used plasmid-based RGS to rescue BTV recombinant viruses with HA tags inserted into VP2, and detected several sites on VP2 that can accommodate HA tags.
Some of the recombinant tagged viruses have potential to be developed into distinctive inactivated vaccines.

Functional Analysis of Botulinum Hemagglutinin (HA).

Botulinum neurotoxin (BoNT), produced by Clostridium botulinum, is the most potent toxin and produced as a complex with non-toxic components. Food-borne botulism is caused by the ingestion of these BoNT complexes. Hemagglutinin (HA), one of the non-toxic components, is known to have lectin (carbohydrate binding) activity and E-cadherin-binding activity. These activities promote the intestinal absorption of BoNT.
To elucidate the mechanism of the onset of food-borne botulism, we focused on the role of HA in the intestinal absorption of BoNT. We describe the functional analysis methods for HA, including the expression of recombinant proteins, binding to glycoproteins and epithelial cells, and localization in mouse intestinal tissue.

Influenza Hemagglutinin Nanoparticle Vaccine Elicits Broadly Neutralizing Antibodies against Structurally Distinct Domains of H3N2 HA

Influenza vaccine effectiveness varies annually due to the fast evolving seasonal influenza A(H3N2) strain and egg-derived mutations-both of which can cause a mismatch between the vaccine and circulating strains.
To address these limitations, we have developed a hemagglutinin (HA)-based protein-detergent nanoparticle influenza vaccine (NIV) with a saponin-based Matrix-M™ adjuvant. In a phase 1 clinical trial of older adults, the vaccine demonstrated broadly cross-reactive A(H3N2) HA antibody responses.
Two broadly neutralizing monoclonal antibodies derived from NIV-immunized mice were characterized by transmission electron microscopy (TEM), antibody competition assays, fluorescence-activated cell sorting (FACS) analysis, and protein-protein docking. These antibodies recognize two conserved regions of the head domain, namely the receptor binding site and the vestigial esterase subdomain, thus demonstrating the potential for an HA subunit vaccine to elicit antibodies targeting structurally and antigenically distinct but conserved sites.
Antibody competition studies with sera from the phase 1 trial in older adults confirmed that humans also make antibodies to these two head domains and against the highly conserved stem domain. This data supports the potential of an adjuvanted recombinant HA nanoparticle vaccine to induce broadly protective immunity and improved vaccine efficacy.

Measuring influenza hemagglutinin (HA) stem-specific antibody-dependent cellular cytotoxicity (ADCC) in human sera using novel stabilized stem nanoparticle probes.

Generating vaccine that confers a complete protection is a major goal in designing a universal influenza vaccine. Currently, there is a considerable interest in the broadly neutralizing antibodies (bnAb) targeting the conserved HA stem region.
These antibodies have been shown to activate cellular immune responses, such as ADCC, in addition to their neutralization activity. We had previously demonstrated that immunization with H1-based stabilized stem (SS) nanoparticles (np) protects against heterosubtypic lethal H5N1 challenge, despite the absence of detectable neutralizing activity.
Utilizing these novel SS probes to develop an ADCC assay would help in understanding the mechanism of action of stem-specific antibodies, as well as evaluating future influenza vaccines.To develop a new protocol to assess the ADCC activity mediated by stem-directed antibodies in human sera using novel SS np probes. Human sera samples were screened for binding and ADCC activities to different influenza group 1 SS probes (H1, H2, and H5) using trimeric SS or multivalent SS-np (n = 8 trimers) formats.Initial screening revealed 63% (57/90) seroprevalence of anti-HA (H1) stem-epitope antibodies, as determined by the differential binding to HA SS and its corresponding epitope-mutant (Ile45Arg/Thr49Arg) probe.

Hemagglutinin (HA Tag) Antibody

20-abx132270 Abbexa
  • 425.00 EUR
  • 133.00 EUR
  • 1177.00 EUR
  • 565.00 EUR
  • 328.00 EUR
  • 100 ug
  • 10 ug
  • 1 mg
  • 200 ug
  • 50 ug

Hemagglutinin (HA Tag) Antibody

20-abx130437 Abbexa
  • 342.00 EUR
  • 885.00 EUR
  • 453.00 EUR
  • 154.00 EUR
  • 272.00 EUR
  • 100 ug
  • 1 mg
  • 200 ug
  • 20 ug
  • 50 ug

Influenza Hemagglutinin (HA) Peptide

A6004-25 ApexBio 25 mg 528 EUR

Influenza Hemagglutinin (HA) Peptide

A6004-5 ApexBio 5 mg 168 EUR

Influenza Hemagglutinin (HA) Peptide

A6004-5.1 ApexBio 10 mM (in 1mL DMSO) 467 EUR

OVA Conjugated Hemagglutinin (HA)

4-CPX160Ge21 Cloud-Clone
  • 193.18 EUR
  • 155.00 EUR
  • 449.44 EUR
  • 216.48 EUR
  • 332.96 EUR
  • 192.00 EUR
  • 973.60 EUR
  • 100 ug
  • 10ug
  • 1 mg
  • 200 ug
  • 500 ug
  • 50ug
  • 5 mg

Hemagglutinin (HA), human recombinant

4844-10 Biovision 566 EUR

Hemagglutinin (HA) Recombinant Protein

97-055 ProSci 0.1 mg 516.5 EUR

Hemagglutinin (HA) Recombinant Protein

97-056 ProSci 0.1 mg 516.5 EUR

Hemagglutinin (HA) Recombinant Protein

97-057 ProSci 0.1 mg 516.5 EUR

Human hemagglutinin(HA)ELISA Kit

GA-E1801HM-48T GenAsia Biotech 48T 289 EUR

Human hemagglutinin(HA)ELISA Kit

GA-E1801HM-96T GenAsia Biotech 96T 466 EUR

Human hemagglutinin,HA ELISA Kit

201-12-1785 SunredBio 96 tests 440 EUR

Influenza A virus Hemagglutinin (HA)

1-CSB-RP189374BA Cusabio
  • 611.00 EUR
  • 309.00 EUR
  • 1827.00 EUR
  • 939.00 EUR
  • 1218.00 EUR
  • 397.00 EUR
  • 100ug
  • 10ug
  • 1MG
  • 200ug
  • 500ug
  • 50ug

Influenza A virus Hemagglutinin (HA)

1-CSB-YP356048IBA Cusabio
  • 679.00 EUR
  • 335.00 EUR
  • 2172.00 EUR
  • 1051.00 EUR
  • 1442.00 EUR
  • 435.00 EUR
  • 100ug
  • 10ug
  • 1MG
  • 200ug
  • 500ug
  • 50ug

Influenza A virus Hemagglutinin (HA)

1-CSB-YP356317IDG Cusabio
  • 679.00 EUR
  • 335.00 EUR
  • 2172.00 EUR
  • 1051.00 EUR
  • 1442.00 EUR
  • 435.00 EUR
  • 100ug
  • 10ug
  • 1MG
  • 200ug
  • 500ug
  • 50ug

Influenza A virus Hemagglutinin (HA)

1-CSB-EP356317IDG Cusabio
  • 611.00 EUR
  • 309.00 EUR
  • 1827.00 EUR
  • 939.00 EUR
  • 1218.00 EUR
  • 397.00 EUR
  • 100ug
  • 10ug
  • 1MG
  • 200ug
  • 500ug
  • 50ug

Influenza A virus Hemagglutinin (HA)

1-CSB-EP607773IER Cusabio
  • 611.00 EUR
  • 309.00 EUR
  • 1827.00 EUR
  • 939.00 EUR
  • 1218.00 EUR
  • 397.00 EUR
  • 100ug
  • 10ug
  • 1MG
  • 200ug
  • 500ug
  • 50ug

Influenza A virus Hemagglutinin (HA)

1-CSB-EP714917IEX Cusabio
  • 611.00 EUR
  • 309.00 EUR
  • 1827.00 EUR
  • 939.00 EUR
  • 1218.00 EUR
  • 397.00 EUR
  • 100ug
  • 10ug
  • 1MG
  • 200ug
  • 500ug
  • 50ug

Influenza A virus Hemagglutinin (HA)

1-CSB-EP721113IFG Cusabio
  • 611.00 EUR
  • 309.00 EUR
  • 1827.00 EUR
  • 939.00 EUR
  • 1218.00 EUR
  • 397.00 EUR
  • 100ug
  • 10ug
  • 1MG
  • 200ug
  • 500ug
  • 50ug

Human hemagglutinin(HA)ELISA Kit

QY-E00658 Qayee Biotechnology 96T 400 EUR

Human hemagglutinin,HA ELISA Kit

CN-04295H1 ChemNorm 96T 434 EUR
Using equimolar amounts, the multivalent presentation of HA SS on np induced significantly higher ADCC activity compared to the monovalent (trimer) SS probes (2-6 fold increase).
Further, ADCC activity was similarly reported against different group 1 influenza subtypes: H1, H2, and H5. Importantly, ADCC was mediated mainly by antibodies targeting the bnAb-epitope on the HA stem.We report on an assay to measure stem-specific ADCC activity using SS np probes.
Our results indicate high prevalence of HA-stem antibodies with cross-reactive ADCC activity. Such assay could be utilized in the assessment of next generation influenza vaccines.

Modified uvsY by N-terminal hexahistidine tag addition enhances efficiency of recombinase polymerase amplification to detect SARS-CoV-2 DNA

Background: Recombinase (uvsY and uvsX) from bacteriophage T4 is a key enzyme for recombinase polymerase amplification (RPA) that amplifies a target DNA sequence at a constant temperature with a single-stranded DNA-binding protein and a strand-displacing polymerase. The present study was conducted to examine the effects of the N- and C-terminal tags of uvsY on its function in RPA to detect SARS-CoV-2 DNA.
Methods: Untagged uvsY (uvsY-Δhis), N-terminal tagged uvsY (uvsY-Nhis), C-terminal tagged uvsY (uvsY-Chis), and N- and C-terminal tagged uvsY (uvsY-NChis) were expressed in Escherichia coli and purified. RPA reaction was carried out with the in vitro synthesized standard DNA at 41 °C. The amplified products were separated on agarose gels.
Results: The minimal initial copy numbers of standard DNA from which the amplified products were observed were 6 × 105, 60, 600, and 600 copies for the RPA with uvsY-Δhis, uvsY-Nhis, uvsY-Chis, and uvsY-NChis, respectively. The minimal reaction time at which the amplified products were observed were 20, 20, 30, and 20 min for the RPA with uvsY-Δhis, uvsY-Nhis, uvsY-Chis, and uvsY-NChis, respectively. The RPA with uvsY-Nhis exhibited clearer bands than that with either of other three uvsYs.
Conclusions: The reaction efficiency of RPA with uvsY-Nhis was the highest, suggesting that uvsY-Nhis is suitable for use in RPA.
Keywords: Hexahistidine tag; Isothermal DNA amplification; Recombinase polymerase amplification (RPA); uvsY.

A Strategy to Fight against Triple-Negative Breast Cancer: pH-Responsive Hexahistidine-Metal Assemblies with High-Payload Drugs

Triple-negative breast cancer (TNBC), an aggressive subtype of breast cancer, is difficult to be targeted therapeutically due to negative expression of the bioreceptor, which leads to the poorest overall four-year survival rate among all cancer subtypes.
We proposed that the nanomedicine featuring high payload and pH-responsive release of the loaded drugs could assist the TNBC treatment. In the present study, the His6-metal assemblies (HmA) were employed to encapsulate the doxorubicin (Dox), and the effect of HmA loaded with Dox (HmA@Dox) on treating TNBC was evaluated in vitro and in vivo.
We found that the participation of Dox in the formation of HmA leads to high loading efficiency (99.4% for concentration ≤ 1 mg/mL) and the loading capacity (50.7% for concentration ≥ 10 mg/mL) of Dox encapsulated into HmA. HmA@Dox exhibited a narrow size distribution on the nanoscale, a pH-responsive release of loaded Dox, a quick endocytosis process, and fast lysosome escape. Most importantly, the HmA@Dox showed high efficacy in killing various breast cancer cells (MCF-7, MDA-MB-231, and MDA-MB-453) in vitro and depressing the development of TNBC in vivo.
Our results demonstrated that such a strategy for designing a nanomedicine with high payload and responsive release of drugs to the environment around the tumor was of great importance to treat TNBC.

Efficient Delivery of Antibodies Intracellularly by Co-Assembly with Hexahistidine-Metal Assemblies (HmA)

Purpose: There has been a substantial global market for antibodies, which are based on extracellular targets. Binding intracellular targets by antibodies will bring new chances in antibody therapeutics and a huge market increase. We aim to evaluate the efficiency of a novel delivery system of His6-metal assembly (HmA) in delivering intracellular antibodies and biofunctions of delivered antibodies.
Methods: In this study, the physicochemical properties of HmA@Antibodies generated through co-assembling with antibodies and HmA were well characterized by dynamic light scatter. The cytotoxicity of HmA@Antibodies was investigated by Cell Counting Kit-8 (CCK-8). The endocytic kinetics and lysosome escape process of HmA@Antibodies were studied by flow cytometry and fluorescent staining imaging, respectively. Compared to the commercialized positive control, the intracellular delivery efficiency by HmA@Antibodies and biofunctions of delivered antibodies were evaluated by fluorescent imaging and CCK-8.
Results: Various antibodies (IgG, anti-β-tubulin and anti-NPC) could co-assemble with HmA under a gentle condition, producing nano-sized (~150 nm) and positively charged (~+30 eV) HmA@Antibodies particles with narrow size distribution (PDI ~ 0.15). HmA displayed very low cytotoxicity to divers cells (DCs, HeLa, HCECs, and HRPE) even after 96 h for the feeding concentration ≤100 μg mL-1, and fast escape from endosomes. In the case of delivery IgG, the delivery efficiency into alive cells of HmA was better than a commercial protein delivery reagent (PULSin).
For cases of the anti-β-tubulin and anti-NPC, HmA showed comparable delivery efficiency to their positive controls, but HmA with ability to deliver these antibodies into alive cells was still superior to positive controls delivering antibodies into dead cells through punching holes.
Conclusion: Our results indicate that this strategy is a feasible way to deliver various antibodies intracellularly while preserving their functions, which has great potential in various applications and treating many refractory diseases by intracellular antibody delivery.
Keywords: antibody; coordination polymer; intracellular delivery; nanocarrier; peptide assembly.

Efficient delivery of cytosolic proteins by protein-hexahistidine-metal co-assemblies

Proteins play key roles in most biological processes, and protein dysfunction can cause various diseases. Over the past few decades, tremendous development has occurred in the protein therapeutic market due to the high specificity, low side effects, and low risk of proteins.
Currently, all protein drugs on the market are based on extracellular targeting; more than 70% of intracellular targets remain un-druggable. Efficient delivery of cytosolic proteins is of significance for protein drugs, advanced biotechnology and molecular cell biology. Herein, we developed a co-assembly strategy for protein-hexahistidine-metal for intracellular protein delivery.
Based on the coordinative interaction between His6 and metal ions, various proteins were encapsulated in situ into nanosized and positively charged protein encapsulation particles(Protein@HmA) through a co-assembly process with a high loading capacity and loading efficiency.
Protein@HmA was able to deliver proteins with diverse physicochemical properties through multiple endocytosis pathways, and the protein could quickly escape from endosomes.
In addition, the bioactivity of the loaded protein during co-assembly and the intracellular delivery processes were well preserved and could be properly exerted inside cells. Our results demonstrate that this strategy should be a valuable platform for protein delivery and has huge potential in protein-based theranostics,
 STATEMENT OF SIGNIFICANCE: : Intracellular targets with protein drugs may provide a new way for the treatment of many refractory disease. Herein, we developed a co-assembly strategy for protein-hexahistidine-metal for efficient intracellular protein delivery.

Anti-Hexahistidine (His6) tag Antibody

STJ60100 St John's Laboratory 100 µg 424 EUR

Recombinant Human MBL2 Protein-Hexahistidine tag

CTP-244 Creative Biolabs 100ug Ask for price
Based on the coordinative interaction between His6 and metal ions, various proteins were encapsulated in situ into nanosized and positively charged particles (Protein@HmA) with a high loading efficiency.
Protein@HmA was able to deliver different proteins through multiple endocytosis pathways, and the protein could quickly escape from endosomes. In addition, the bioactivity of the loaded protein during co-assembly and the intracellular delivery processes were well preserved and could be properly exerted inside cells.
This strategy should be a valuable platform for protein delivery and has huge potential in protein-based theranostics.

Rift Valley fever virus Gn V5-epitope tagged virus enables identification of UBR4 as a Gn interacting protein that facilitates Rift Valley fever virus production

Rift Valley fever virus (RVFV) is an arbovirus that was first reported in the Rift Valley of Kenya which causes significant disease in humans and livestock. RVFV is a tri-segmented, negative-sense RNA virus consisting of a L, M, and S segments with the M segment encoding the glycoproteins Gn and Gc. Host factors that interact with Gn are largely unknown.
To this end, two viruses containing an epitope tag (V5) on the Gn protein in position 105 or 229 (V5Gn105 and V5Gn229) were generated using the RVFV MP-12 vaccine strain as a backbone.
The V5-tag insertion minimally impacted Gn functionality as measured by replication kinetics, Gn localization, and antibody neutralization assays.
A proteomics-based approach was used to identify novel Gn-binding host proteins, including the E3 ubiquitin-protein ligase, UBR4. Depletion of UBR4 resulted in a significant decrease in RVFV titers and a reduction in viral RNA production.

The Dual Histone Deacetylase-Proteasome Inhibitor RTS-V5 Acts Synergistically With Ritonavir to Induce Endoplasmic Reticulum Stress in Bladder Cancer Cells

Background/aim: Simultaneous inhibition of histone deacetylase and proteasomes induces endoplasmic reticulum (ER) stress efficiently. RTS-V5 is the first dual histone deacetylase-proteasome inhibitor, and we anticipated that combining it with the cytochrome P450 family 3 subfamily A member 4 inhibitor ritonavir would enhance its activity in bladder cancer cells.
Materials and methods: Using bladder cancer cells (human T-24, J-82, murine MBT-2), we evaluated the ability and mechanism by which the combination of RTS-V5 and ritonavir induced ER stress and killed cancer cells.
Results: The combination of RTS-V5 and ritonavir triggered robust apoptosis and inhibited bladder cancer growth effectively in vitro and in vivo.
It caused ubiquitinated protein accumulation and induced ER stress synergistically. The combination inhibited the mammalian target of rapamycin pathway by increasing the expression of AMP-activated protein kinase. We also found that the combination caused histone and tubulin hyperacetylation.
Conclusion: Ritonavir enhances the ability of RTS-V5 to cause ER stress in bladder cancer cells.
Keywords: Histone deacetylase; endoplasmic reticulum stress; proteasome; ritonavir.

Ischemic ST-Segment Depression Maximal in V1-V4 (Versus V5-V6) of Any Amplitude Is Specific for Occlusion Myocardial Infarction (Versus Nonocclusive Ischemia)

Background Occlusion myocardial infarctions (OMIs) of the posterolateral walls are commonly missed by ST-segment-elevation myocardial infarction (STEMI) criteria, with >50% of patients with circumflex occlusion not receiving emergent reperfusion and experiencing increased mortality. ST-segment depression maximal in leads V1-V4 (STDmaxV1-4) has been suggested as an indicator of posterior OMI.
Methods and Results We retrospectively reviewed a high-risk population with acute coronary syndrome. OMI was defined from prior studies as a culprit lesion with TIMI (Thrombolysis in Myocardial Infarction) 0 to 2 flow or TIMI 3 flow plus peak troponin T >1.0 ng/mL or troponin I >10 ng/mL. STEMI was defined by the Fourth Universal Definition of Myocardial Infarction. ECGs were interpreted blinded to outcomes. Among 808 patients, there were 265 OMIs, 108 (41%) meeting STEMI criteria. A total of 118 (15%) patients had “suspected ischemic” STDmaxV1-4, of whom 106 (90%) had an acute culprit lesion, 99 (84%) had OMI, and 95 (81%) underwent percutaneous coronary intervention.
Suspected ischemic STDmaxV1-4 had 97% specificity and 37% sensitivity for OMI. Of the 99 OMIs detected by STDmaxV1-4, 34% had <1 mm ST-segment depression, and only 47 (47%) had accompanying STEMI criteria, of which 17 (36%) were identified a median 1.00 hour earlier by STDmaxV1-4 than STEMI criteria. Despite similar infarct size, TIMI flow, and coronary interventions, patients with STEMI(-) OMI and STDmaxV1-4 were less likely than STEMI(+) patients to undergo catheterization within 90 minutes (46% versus 68%; P=0.028).
Conclusions Among patients with high-risk acute coronary syndrome, the specificity of ischemic STDmaxV1-4 was 97% for OMI and 96% for OMI requiring emergent percutaneous coronary intervention. STEMI criteria missed half of OMIs detected by STDmaxV1-4. Ischemic STDmaxV1-V4 in acute coronary syndrome should be considered OMI until proven otherwise.

PhylomeDB V5: an expanding repository for genome-wide catalogues of annotated gene phylogenies

PhylomeDB is a unique knowledge base providing public access to minable and browsable catalogues of pre-computed genome-wide collections of annotated sequences, alignments and phylogenies (i.e. phylomes) of homologous genes, as well as to their corresponding phylogeny-based orthology and paralogy relationships.
In addition, PhylomeDB trees and alignments can be downloaded for further processing to detect and date gene duplication events, infer past events of inter-species hybridization and horizontal gene transfer, as well as to uncover footprints of selection, introgression, gene conversion, or other relevant evolutionary processes in the genes and organisms of interest. Here, we describe the latest evolution of PhylomeDB (version 5).
This new version includes a newly implemented web interface and several new functionalities such as optimized searching procedures, the possibility to create user-defined phylome collections, and a fully redesigned data structure.
This release also represents a significant core data expansion, with the database providing access to 534 phylomes, comprising over 8 million trees, and homology relationships for genes in over 6000 species.
This makes PhylomeDB the largest and most comprehensive public repository of gene phylogenies. PhylomeDB is available at http://www.phylomedb.org.
Application of local fully Convolutional Neural Network combined with YOLO v5 algorithm in small target detection of remote sensing image
This exploration primarily aims to jointly apply the local FCN (fully convolution neural network) and YOLO-v5 (You Only Look Once-v5) to the detection of small targets in remote sensing images.
Firstly, the application effects of R-CNN (Region-Convolutional Neural Network), FRCN (Fast Region-Convolutional Neural Network), and R-FCN (Region-Based-Fully Convolutional Network) in image feature extraction are analyzed after introducing the relevant region proposal network.
Secondly, YOLO-v5 algorithm is established on the basis of YOLO algorithm. Besides, the multi-scale anchor mechanism of Faster R-CNN is utilized to improve the detection ability of YOLO-v5 algorithm for small targets in the image in the process of image detection, and realize the high adaptability of YOLO-v5 algorithm to different sizes of images.
Finally, the proposed detection method YOLO-v5 algorithm + R-FCN is compared with other algorithms in NWPU VHR-10 data set and Vaihingen data set.
\The experimental results show that the YOLO-v5 + R-FCN detection method has the optimal detection ability among many algorithms, especially for small targets in remote sensing images such as tennis courts, vehicles, and storage tanks. Moreover, the YOLO-v5 + R-FCN detection method can achieve high recall rates for different types of small targets.

V5 Antibody

20-abx118003 Abbexa
  • 551.00 EUR
  • 481.00 EUR
  • 100 ul
  • 50 ul

V5 antibody

10R-10453 Fitzgerald 100 ug 435 EUR

V5 antibody

10R-10454 Fitzgerald 100 ug 435 EUR

V5 antibody

10R-10455 Fitzgerald 100 ug 435 EUR

V5-Tag Mouse Monoclonal Antibody, Clone V5.E10

Ab1008-100 GenDepot 100ug 381 EUR

V5-Tag Mouse Monoclonal Antibody, Clone V5.E10

Ab1008-101 GenDepot 1mg 2278 EUR

V5 agarose beads

AE029-100ul Abclonal 100 ul Ask for price

V5 agarose beads

AE029-50ul Abclonal 50 ul Ask for price

V5-Tag pAb

AE071 Abclonal 50 ul 176 EUR

V5 agarose beads

AE029-200ul Abclonal 200 ul 228 EUR

V5 agarose beads

AE029-20ul Abclonal 20 ul Ask for price

V5-tag Antibody

20-abx134695 Abbexa
  • 356.00 EUR
  • 565.00 EUR
  • 300.00 EUR
  • 100 ul
  • 200 ul
  • 50 ul

V5-tag Antibody

20-abx134696 Abbexa
  • 356.00 EUR
  • 565.00 EUR
  • 300.00 EUR
  • 100 ul
  • 200 ul
  • 50 ul

V5-tag Antibody

20-abx134697 Abbexa
  • 356.00 EUR
  • 537.00 EUR
  • 217.00 EUR
  • 100 ul
  • 200 ul
  • 30 ul
Furthermore, due to the deeper network architecture, the YOL v5 + R-FCN detection method has a stronger ability to extract the characteristics of image targets in the detection of remote sensing images.
Meanwhile, it can achieve more accurate feature recognition and detection performance for the densely arranged target images in remote sensing images. This research can provide reference for the application of remote sensing technology in China, and promote the application of satellites for target detection tasks in related fields.

Expression of OsteoblastSpecific Factor 2 (OSF-2, Periostin) Is Associated with Drug Resistance in Ovarian Cancer Cell Lines.

One of the main obstacles to the effective treatment of ovarian cancer patients continues to be the drug resistance of cancer cells. Osteoblast-Specific Factor 2 (OSF-2, Periostin) is a secreted extracellular matrix protein (ECM) expressed in fibroblasts during bone and teeth development. Expression of OSF-2 has been also related to the progression and drug resistance of different tumors.
The present study investigated the role of OSF-2 by evaluating its expression in the primary serous ovarian cancer cell line, sensitive (W1) and resistant to doxorubicin (DOX) (W1DR) and methotrexate (MTX) (W1MR). The OSF-2 transcript (real-time PCR analysis), protein expression in cell lysates and cell culture medium (western blot), and expression of the OSF-2 protein in cell lines (immunofluorescence) were investigated in this study. Increased expression of OSF-2 mRNA was observed in drug-resistant cells and followed by increased protein expression in cell culture media of drug-resistant cell lines.
A subpopulation of ALDH1A1-positive cells was noted for W1DR and W1MR cell lines; however, no direct co-expression with OSF-2 was demonstrated. Both drugs induced OSF-2 expression after a short period of exposure of the drug-sensitive cell line to DOX and MTX.
The obtained results indicate that OSF-2 expression might be associated with the development of DOX and MTX resistance in the primary serous W1 ovarian cancer cell line.

Antibody-free detection of phosphoserine/threonine containing peptides by homogeneous time-resolved fluorescence.

Protein phosphorylation is a critical signaling mechanism in cellular regulation and stress response, and more than 95% of the phosphorylations are targeted toward Ser or Thr amino-acid residues. The classical techniques for analyzing phospho-amino acid residues use radioisotopes or sequence-specific antibodies.
However, both practical and economical limitations have prevented their development, and we here propose an original approach for the detection of phospho-Ser/Thr residues.
It requires no antibody and exploits the patented homogeneous time-resolved fluorescence (HTRF) technology, in association with a 3-step chemical transformation of phospho-amino acids into fluorescent derivatives.
The process involves: (i) alkaline β-elimination of the phosphorylated group, (ii) Michael addition of a bifunctional group, and then (iii) introduction of cyanin-5 as fluorescent acceptor for HTRF. The donor fluorescent moiety at the N-terminus of the phosphorylated peptide is a streptavidin europium cryptate conjugate.
After its development, the detection system has been validated on synthetic peptide substrates of Chk2, a key protein kinase activated in response to DNA damage and involved in cell cycle arrest.
The results showed a good correlation with known specificity profiles. Interestingly, the detection system is versatile, easy to implement, and suitable for multiple parallel analyses.

Characterization of agonist stimulation of cAMP-dependent protein kinase and G protein-coupled receptor kinase phosphorylation of the beta2-adrenergic receptor using phosphoserine-specific antibodies.

Agonist-stimulated desensitization of the beta2-adrenergic receptor (beta2AR) is caused by both a potent cAMP-dependent protein kinase (PKA)-mediated phosphorylation and a less potent, occupancy-dependent, G protein-coupled receptor kinase (GRK)-mediated phosphorylation that leads to beta-arrestin binding and internalization.
In this study the kinetics of phosphorylation of the third intracellular loop PKA site Ser262 and the putative C-tail GRK sites Ser355, Ser356 of the human beta2AR overexpressed in human embryonic kidney (HEK) 293 cells were characterized using phosphoserine-specific antibodies.
Specificity of the antibodies was shown by their lack of reactivity with mutant beta2ARs lacking the respective sites. In addition, overexpression of GRK2 and GRK5 increased basal levels of phosphorylation of the GRK sites Ser355, Ser356 in both COS-7 and HEK 293 cells. Epinephrine, prostaglandin E1, and forskolin at maximum concentrations stimulated phosphorylation of the beta2AR PKA site (Ser262) by 4-fold, whereas PMA stimulated it by 2-fold. Epinephrine stimulated PKA site phosphorylation with an EC50 of 20 to 40 pM. In contrast, epinephrine stimulated GRK site phosphorylation (Ser355,Ser356) with an EC50 of 200 nM (1-min treatments), which is more than 4000-fold higher relative to PKA site phosphorylation, consistent with an occupancy-driven process. After 10 to 30 min, the EC50 for epinephrine stimulation of GRK site phosphorylation was reduced to 10 to 20 nM but was still approximately 200-fold greater than for the PKA site.
The EC50 for internalization correlated with GRK site phosphorylation and showed a similar shift with time of epinephrine stimulation. The kinetics of epinephrine-stimulated GRK site phosphorylation were not altered in a mutant of the beta2AR lacking the PKA consensus sites.
The initial levels (2 min) of a range of agonist-stimulated GRK site phosphorylations were correlated with their efficacy for activation of adenylyl cyclase, namely epinephrine>> or = formoterol = fenoterol>> terbutaline = zinterol = albuterol>> salmeterol>> dobutamine>> or = ephedrine. However, after 20 to 30 min of treatment, agonists with intermediate strengths, such as albuterol and salmeterol, stimulate GRK site phosphorylations that are approximately equal to that produced by epinephrine, and the correlation breaks down.
The GRK and PKA site antibodies were also effective in detecting phosphorylation of the endogenous beta2AR expressed in A431 human epidermoid carcinoma cells.
To summarize, our results show a remarkable amplification of PKA site phosphorylation relative to the putative GRK site phosphorylation, heterologous stimulation of the PKA site phosphorylation, no dependence of GRK site phosphorylation on PKA sites, and a reasonable correlation of initial levels of GRK site phosphorylation with the strength of a range of agonists.

Changes in anti-phosphoserine and anti-phosphothreonine antibody binding during the sleep-waking cycle and after lesions of the locus coeruleus.

Cellular responses to many extracellular signals occur through phosphorylation or dephosphorylation of intracellular proteins.
To determine whether changes in protein phosphorylation accompany the electrophysiological changes occurring during the sleep-waking cycle, immunocytochemical mapping of cells labeled with anti-phosphoserine and anti-phosphothreonine antibodies was performed on brain sections of sleeping and waking rats.
Animals implanted for chronic polysomnographic recordings were sacrificed after either 3h of sleep or 3h of sleep deprivation by gentle handling.
Anti-phosphoserine and anti-phosphothreonine staining was mainly localized in neurons and was high in some brain regions, such as cerebral cortex and hypothalamus, and low in others, such as the thalamus. In all cases, the number of cells labeled with either antibody in the cerebral cortex was markedly higher in rats sacrificed after 3h of waking than in rats sacrificed after 3h of sleep.
Unilateral lesions of the locus coeruleus by local injection of 6-hydroxydopamine were performed in other animals to determine whether the increase in protein phosphorylation during waking was influenced by the activity of the noradrenergic system, which is higher in waking than in sleep.
In animals sacrificed after 3h of spontaneous or forced waking, the number of labeled neurons in the cerebral cortex was decreased on the side in which noradrenergic fibers had been lesioned.
These results suggest that 1) neurons exist physiologically in different states of phosphorylation, ranging from a state of very high phosphorylation (e.g., in the cerebral cortex) to a state of very low phosphorylation (e.g., in many thalamic nuclei); 2) the fraction of highly phosphorylated neurons in cerebral cortex is higher in waking than in sleep and 3) part of the immunoreactive phosphorylation present in highly labeled cortical neurons is controlled by the locus coeruleus.

Identification of a high-affinity anti-phosphoserineantibody for the development of a homogeneous fluorescence polarization assay of protein kinase C.

In the last few years, fluorescence polarization (FP) has been applied to the development of robust, homogeneous, high throughput assays in molecular recognition research, such as ligand-protein interactions.
Recently, this technology has been applied to the development of homogeneous tyrosine kinase assays, since there are high-affinity anti-phosphotyrosine antibodies available.
Unlike tyrosine kinases, application of FP to assay development for serine/threonine kinases has been impeded because of lack of high-affinity anti-phosphoserine/threonine antibodies. In the present study, we report the discovery of a high-affinity, monoclonal anti-phosphoserine antibody, 2B9, with a Kd of 250 +/- 34 pM for a phosphoserine-containing peptide tracer, fluorescein-RFARKGS(PO(4))LRQKNV. Our data suggest that 2B9 is selective for fluorescein-RFARKGS(PO(4))LRQKNV. The antibody and tracer have been used for the development of a competitive FP assay for protein kinase C (PKC) in 384-well plates.
Phosphatidylserine, which enhances the kinase activity of PKC in a Ca(2+)-dependent manner and has a structure similar to that of phosphoserine, did not interfere with binding of the peptide tracer to the antibody in the FP assay.
The data indicate that the FP assay is more sensitive and robust than the scintillation proximity assay for PKC. The FP assay developed here can be used for rapid screening of hundreds of thousands of compounds for discovery of therapeutic leads for PKC-related diseases.

Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody.

Human progesterone receptor (PR) is phosphorylated on multiple serine residues (at least seven sites) in a manner that involves distinct groups of sites coordinately regulated by hormone and different kinases. Progress on defining a functional role for PR phosphorylation has been hampered both by the complexity of phosphorylation and the lack of simple, nonradioactive methods to detect the influence of ligands and other signaling pathways on specific PR phosphorylation sites in vivo.
Toward this end, we have produced monoclonal antibodies (MAbs) that recognize specific phosphorylation sites within human PR including a basal site at Ser 190 (MAb P190) and a hormone-induced site at Ser 294 (MAb P294).
Biochemical experiments showed the differential reactivity of the P190 and P294 MAbs for phosphorylated and unphosphorylated forms of PR. Both MAbs recognize specific phosphorylated forms of PR under different experimental conditions including denatured PR protein by Western blots and PR in its native conformation in solution or complexed to specific target DNA.
As detected by Western blot of T47D cells treated with hormone for different times, hormone-dependent down-regulation of total PR and the Ser 190 phosphorylation site occurred in parallel, whereas the Ser 294 phosphorylation site was down-regulated more rapidly. This difference in kinetics suggests that the Ser 294 site is more labile than basal sites and is acted upon by distinct phosphatases.
A strong preferential hormone-dependent phosphorylation of Ser 294 was observed on PR-B as compared with the amino-terminal truncated A form of PR.
This was unexpected because Ser 294 and flanking sequences are identical on both proteins, suggesting that a distinct conformation of the N-terminal domain of PR-A inhibits phosphorylation of this site.
That Ser 294 lies within an inhibitory domain that mediates the unique repressive functions of PR-A raises the possibility that differential phosphorylation of Ser 294 is involved in the distinct functional properties of PR-A and PR-B.

Anti-phosphoserine and anti-phosphothreonine antibodies modulate autophosphorylation of the insulin receptor but not EGF receptor.

We examined the effect of anti-phosphothreonine and anti-phosphoserine antibodies on insulin receptor autophosphorylation. These antibodies did not affect insulin binding activity of the receptor. These antibodies, however, inhibited insulin-stimulated autophosphorylation of insulin receptor, while did not affect EGF-stimulated autophosphorylation of EGF receptor.

Phosphoserine Antibody

20-abx134715 Abbexa
  • 356.00 EUR
  • 537.00 EUR
  • 217.00 EUR
  • 100 ul
  • 200 ul
  • 30 ul

Phosphoserine Antibody

abx020673-100ug Abbexa 100 ug 1066 EUR

Phosphoserine Antibody

abx448438-400ul Abbexa 400 ul 537 EUR

Phosphoserine Antibody

20-abx159643 Abbexa
  • 272.00 EUR
  • 230.00 EUR
  • 100 ug
  • 50 ug

Phosphoserine antibody

10R-7895 Fitzgerald 100 ug 322 EUR

Phosphoserine antibody

10R-P125a Fitzgerald 250 ul 673 EUR

Phosphoserine antibody

20C-CR1332RP Fitzgerald 100 ug 133 EUR

Phosphoserine antibody

70R-PR015 Fitzgerald 50 ug 241 EUR

Phosphoserine Monoclonal Antibody

EM1189-100ul ELK Biotech 100ul 279 EUR

Phosphoserine Monoclonal Antibody

EM1189-50ul ELK Biotech 50ul 207 EUR

Phosphoserine Antibody (APC)

abx448359-400ul Abbexa 400 ul 592 EUR

Phosphoserine Antibody (Biotin)

abx448367-400ul Abbexa 400 ul 592 EUR

Phosphoserine Antibody (FITC)

abx448373-400ul Abbexa 400 ul 578 EUR

Phosphoserine Antibody (PerCP)

abx448393-400ul Abbexa 400 ul 592 EUR

Phosphoserine Antibody (RPE)

abx448401-400ul Abbexa 400 ul 592 EUR

Phosphoserine Antibody (Streptavidin)

abx448409-400ul Abbexa 400 ul 592 EUR

Phosphoserine Antibody (HRP)

abx448439-400ul Abbexa 400 ul 606 EUR

Phosphoserine (pSer) Antibody

abx415747-50ug Abbexa 50 ug 787 EUR

Phosphoserine Monoclonal Antibody

ABM40198-003ml Abbkine 0.03ml 158 EUR

Phosphoserine Monoclonal Antibody

ABM40198-01ml Abbkine 0.1ml 289 EUR

Phosphoserine Monoclonal Antibody

ABM40198-02ml Abbkine 0.2ml 414 EUR

Anti-Phosphoserine antibody

STJ97457 St John's Laboratory 200 µl 197 EUR

Antibody for Phosphoserine

SPC-149F Stressmarq 0.4ml 362 EUR

Antibody for Phosphoserine

SPC-149F-A390 Stressmarq 0.4ml 409 EUR

Antibody for Phosphoserine

SPC-149F-A488 Stressmarq 0.4ml 408 EUR

Antibody for Phosphoserine

SPC-149F-A565 Stressmarq 0.4ml 408 EUR

Antibody for Phosphoserine

SPC-149F-A594 Stressmarq 0.4ml 408 EUR
The inhibition was reversed by adding large amounts of phosphoserine or phosphothreonine. These data suggest that phosphoserine and phosphothreonine on insulin receptor play an important role in insulin-induced conformational change of the receptor.

Using a Syrian (Golden) Hamster Biological Model for the Evaluation of Recombinant Anthrax Vaccines

In this paper, we demonstrate that a Syrian hamster biological model can be applied to the study of recombinant anthrax vaccines. We show that double vaccination with recombinant proteins, such as protective antigen (PA) and fusion protein LF1PA4, consisting of lethal factor I domain (LF) and PA domain IV, leads to the production of high titers of specific antibodies and to protection from infection with the toxicogenic encapsulated attenuated strain B. anthracis 71/12.
In terms of antibody production and protection, Syrian hamsters were much more comparable to guinea pigs than mice. We believe that Syrian hamsters are still underestimated as a biological model for anthrax research, and, in some cases, they can be used as a replacement or at least as a complement to the traditionally used mouse model.

Vaccination with a Brucella ghost developed through a double inactivation strategy provides protection in Guinea pigs and cattle

Vaccination can prevent and control animal brucellosis. Currently, live attenuated vaccines are extensively used to prevent Brucella infection. However, traditional vaccines such as live attenuated vaccines are associated with biological safety risks for both humans and animals. The bacterial ghost (BG) is a new form of vaccine with great prospects. However, bacterial cells cannot be completely inactivated by biological lysis https://www.joplink.net/guinea-pig-antibodies/, conferring a safety risk associated with the vaccine.
In this study, we developed a Brucella abortus A19 bacterial ghost (A19BG) through a double inactivation strategy with sequential biological lysis and hydrogen peroxide treatment. This strategy resulted in 100% inactivation of Brucella, such that viable bacterial cells were not detected even at an ultrahigh concentration of 1010 colony-forming units/mL. Furthermore, A19BG had a typical BG morphology and good genetic stability. Moreover, it did not induce adverse reactions in guinea pigs.
The levels of antibodies, interferon-γ, interleukin-4, and CD4+ T cells in guinea pigs inoculated with the A19BG vaccine were similar to those inoculated with the existing A19 vaccine. Immunization with A19BG conferred a similar level of protection with that of A19 against Brucella melitensis M28 in both guinea pigs and cattle. In conclusion, the combination of biological lysis and H2O2-mediated inactivation is a safe and effective strategy that can serve as a reference for the preparation of BG vaccines.

Infection and protection responses of deletion mutants of non-structural proteins of foot-and-mouth disease virus serotype Asia1 in guinea pigs

The development of a negative marker vaccine against the foot-and-mouth disease virus (FMDV) will enhance the capabilities to differentiate vaccinated from infected animals and move forward in the progressive control pathway for the control of FMD. Here, we report the development of mutant FMDV of Asia1 with partial deletion of non-structural proteins 3A and 3B and characterization of their infectivity and protection response in the guinea pig model. The deleted FMDV Asia1/IND/63/1972 mutants, pAsiaΔ3A and pAsiaΔ3A3B1 were constructed from the full-length infectious clone pAsiaWT, the viable virus was rescued, and the genetic stability of the mutants was confirmed by 20 monolayer passages in BHK21 cells.
The mutant Asia1 viruses showed comparable growth pattern and infectivity with that of AsiaWT in the cell culture. However, the AsiaΔ3A3B1 virus showed smaller plaque and lower virus titer with reduced infectivity in the suckling mice. In guinea pigs, the AsiaΔ3A3B1 virus failed to induce the disease, whereas the AsiaΔ3A virus induced typical secondary lesions of FMD. Vaccination with inactivated Asia1 mutant viruses induced neutralizing antibody response that was significantly lower than that of the parent virus on day 28 post-vaccination (dpv) in guinea pigs (P < 0.05).
Furthermore, challenging the vaccinated guinea pigs with the homologous vaccine strain of FMDV Asia1 conferred complete protection. It is concluded that the mutant AsiaΔ3A3B1 virus has the potential to replace the wild-type virus for use as a negative marker vaccine after assessing the vaccine worth attributes in suspension cell and protective efficacy study in cattle.Key points• Deletion mutant viruses of FMDV Asia1, developed by PCR-mediated mutagenesis of NSP 3A and 3B1, were genetically stable.• The growth kinetics and antigenic relatedness of the mutant viruses were comparable with that of the wild-type virus.• Vaccination of guinea pigs with the deletion mutant viruses conferred complete protection upon challenge with the homologous virus.

Tick immunity using mRNA, DNA and protein-based Salp14 delivery strategies

Guinea pigs exposed to multiple infestations with Ixodes scapularis ticks develop acquired resistance to ticks, which is also known as tick immunity. The I. scapularis salivary components that contribute to tick immunity are likely multifactorial. An anticoagulant that inhibits factor Xa, named Salp14, is present in tick saliva and is associated with partial tick immunity. A tick bite naturally releases tick saliva proteins into the vertebrate host for several days, which suggests that the mode of antigen delivery may influence the genesis of tick immunity. We therefore utilized Salp14 as a model antigen to examine tick immunity using mRNA lipid nanoparticles (LNPs), plasmid DNA, or recombinant protein platforms.
salp14 containing mRNA-LNPs vaccination elicited erythema at the tick bite site after tick challenge that occurred earlier, and that was more pronounced, compared with DNA or protein immunizations. Humoral and cellular responses associated with tick immunity were directed towards a 25 amino acid region of Salp14 at the carboxy terminus of the protein, as determined by antibody responses and skin-testing assays.
This study demonstrates that the model of antigen delivery, also known as the vaccine platform, can influence the genesis of tick immunity in guinea pigs. mRNA-LNPs may be useful in helping to elicit erythema at the tick bite site, one of the most important early hallmarks of acquired tick resistance. mRNA-LNPs containing tick genes is a useful platform for the development of vaccines that can potentially prevent selected tick-borne diseases.

Characterization of Canine Influenza Virus A (H3N2) Circulating in Dogs in China from 2016 to 2018

Avian H3N2 influenza virus follows cross-host transmission and has spread among dogs in Asia since 2005. After 2015-2016, a new H3N2 subtype canine influenza epidemic occurred in dogs in North America and Asia. The disease prevalence was assessed by virological and serological surveillance in dogs in China.
Herein, five H3N2 canine influenza virus (CIV) strains were isolated from 1185 Chinese canine respiratory disease samples in 2017-2018; these strains were on the evolutionary branch of the North American CIVs after 2016 and genetically far from the classical canine H3N2 strain discovered in China before 2016. Serological surveillance showed an HI antibody positive rate of 6.68%. H3N2 was prevalent in the coastal areas and northeastern regions of China. In 2018, it became the primary epidemic strain in the country.
The QK01 strain of H3N2 showed high efficiency in transmission among dogs through respiratory droplets. Nevertheless, the virus only replicated in the upper respiratory tract and exhibited low pathogenicity in mice. Furthermore, highly efficient transmission by direct contact other than respiratory droplet transmission was found in a guinea pig model.
The low-level replication in avian species other than ducks could not facilitate contact and airborne transmission in chickens. The current results indicated that a novel H3N2 virus has become a predominant epidemic strain in dogs in China since 2016 and acquired highly efficient transmissibility but could not be replicated in avian species. Thus, further monitoring is required for designing optimal immunoprophylactic tools for dogs and estimating the zoonotic risk of CIV in China.

Hemoglobin Antibody

1 mg 537 EUR

Hemoglobin Antibody

1 mg 537 EUR

Hemoglobin Antibody

  • 317.00 EUR
  • 335.00 EUR
  • 100ug
  • 50ug

Hemoglobin Antibody

  • 317.00 EUR
  • 335.00 EUR
  • 100ug
  • 50ug

Hemoglobin Antibody

  • 317.00 EUR
  • 335.00 EUR
  • 100ug
  • 50ug

Hemoglobin Antibody

  • 317.00 EUR
  • 335.00 EUR
  • 100ug
  • 50ug

Hemoglobin Antibody

  • 317.00 EUR
  • 335.00 EUR
  • 100ug
  • 50ug

Hemoglobin antibody

100 ug 327 EUR

Hemoglobin antibody

100 ug 327 EUR

Hemoglobin antibody

1 mg 181 EUR
Study protocol: E-freeze - freezing of embryos in assisted conception: a randomised controlled trial evaluating the clinical and cost effectiveness of a policy of freezing embryos followed by thawed frozen embryo transfer compared with a policy of fresh embryo transfer, in women undergoing in vitro fertilisation.

Study protocol: E-freeze – freezing of embryos in assisted conception: a randomised controlled trial evaluating the clinical and cost effectiveness of a policy of freezing embryos followed by thawed frozen embryo transfer compared with a policy of fresh embryo transfer, in women undergoing in vitro fertilisation.

Infertility impacts one in seven {{couples}}; many of these need in vitro fertilisation (IVF). IVF entails exterior hormones to stimulate a girl’s ovaries to produce eggs which might be harvested surgically. Embryos, created in the laboratory by mixing eggs with sperm, are grown in custom for a few days sooner than being modified inside the uterus (fresh embryo transfer).

Spare embryos are sometimes frozen with a view to transfer at a later degree in time – significantly if the preliminary fresh transfer does not consequence in a being pregnant. Despite enhancements in know-how, IVF success costs keep low with an complete reside starting value of 25-30% per remedy. Additionally, there are issues about nicely being outcomes for mothers and infants conceived by IVF, notably after fresh embryo transfer, collectively with maternal ovarian hyperstimulation syndrome (OHSS) and preterm provide.

It is believed that prime ranges of hormones all through ovarian stimulation could create a comparatively hostile setting for embryo implantation whereas rising the menace of OHSS. It has been steered that freezing all embryos with the intention of thawing and altering them inside the uterus at a later stage (thawed frozen embryo transfer) as a substitute of fresh embryo transfer, would possibly outcome in improved being pregnant costs and fewer issues. We goal to examine the clinical and cost effectiveness of fresh and thawed frozen embryo transfer, with the main goal of determining any distinction in the likelihood of having a healthful baby.

E-Freeze is a pragmatic, multicentre two-arm parallel group randomised controlled trial the place women aged ≥18 and < 42 years, with not lower than three good prime quality embryos are randomly allotted to acquire each a fresh or thawed frozen embryo transfer.

The main remaining result’s a healthful baby, outlined as a time interval, singleton, reside starting with relevant weight for gestation. Cost effectiveness may be calculated from a healthcare and societal perspective.E-Freeze will determine the relative benefits of fresh and thawed frozen embryo transfer in phrases of enhancing the likelihood of having a healthful baby. The outcomes of this pragmatic study have the potential to be straight transferred to clinical observe.ISRCTN registry

 Study protocol: E-freeze - freezing of embryos in assisted conception: a randomised controlled trial evaluating the clinical and cost effectiveness of a policy of freezing embryos followed by thawed frozen embryo transfer compared with a policy of fresh embryo transfer, in women undergoing in vitro fertilisation.

Study protocol: E-freeze – freezing of embryos in assisted conception: a randomised controlled trial evaluating the clinical and cost effectiveness of a policy of freezing embryos followed by thawed frozen embryo transfer compared with a policy of fresh embryo transfer, in women undergoing in vitro fertilisation.

In vitro fertilisation/intracytoplasmic sperm injection previous 2020.

Over eight million infants have been born following IVF (in vitro fertilisation) and completely different artificial reproductive know-how (ART) procedures since Louise Brown’s starting 40 years in the previous. New enhancements have added a lot complexity to every clinical and laboratory procedures over the remaining four a few years. Translation of novel approaches from major science into clinical observe continues unabated, widening the applicability of ART to new groups of people and serving to boost every chances of healthful reside starting and affected particular person acceptability.

PI Staining Kit

abx097208-1Kit 1 Kit
EUR 230

ALP Antibody

DF12525 200ul
EUR 304
Description: ALP Antibody detects endogenous levels of ALP.

anti-ALP

YF-PA18460 50 ug
EUR 363
Description: Mouse polyclonal to ALP

anti-ALP

YF-PA18461 50 ul
EUR 363
Description: Mouse polyclonal to ALP

ALP-B/ Rat ALP- B ELISA Kit

ELA-E0473r 96 Tests
EUR 886

PI / RNase Staining Buffer

20-abx090619
  • EUR 272.00
  • EUR 230.00
  • 100 tests
  • 50 tests

Hoechst 33342 Staining Kit

abx097207-1Kit 1 Kit
EUR 230

Human Histochemistry Staining Kit

20-abx299039
  • EUR 871.00
  • EUR 1219.00
  • EUR 565.00
  • 150 tests
  • 500 tests
  • 50 tests

Ponceau S Staining Solution

PW005 100ml
EUR 69.14

CometAssay Silver Staining Kit

4254-200-K 200 Tests
EUR 325.8

Ponceau S Staining Solution

B7778-100000 100 g
EUR 163

Ponceau S Staining Solution

B7778-50000 50 g
EUR 126

ProsiBlue Gel Staining Solution

P7300-050 500ml
EUR 174

Beta-Galactosidase Staining Kit

K2182-250 250 assays
EUR 293

EasyDip Slide Staining System

M900-12AS-ASSORTED 1 Case(s)
EUR 176

Alkaline Phosphatase Staining Kit

K2035-50 50 assays
EUR 379

Beta-Galactosidase Staining Kit

K802-250
EUR 294

Beta Galactosidase Staining Kit

55R-1541 250 assays
EUR 370
Description: Assay Kit for detection of Beta Galactosidase in the research laboratory

Streptavidin Protein (ALP)

abx061009-2ml 2 ml
EUR 704

ALP Blocking Peptide

20-abx161265
  • EUR 272.00
  • EUR 411.00
  • 1 mg
  • 5 mg

ALP Blocking Peptide

DF12525-BP 1mg
EUR 195

7-AAD Viability Staining Solution

EXB0026 400 tests
EUR 76

Coomassie Blue Staining Destaining Solution

AR0140 1kit (for 10 assays to stain gels of 5 x 8.5cm)
EUR 70

Coomassie Blue Fast Staining Solution

AR0170 100mL(for 10 assays to stain gels of 5 x 8.5cm)
EUR 80

7-AAD Viability Staining Buffer

abx090617-100tests 100 tests
EUR 217

SafePinky DNA Gel Staining Solution

S1000-050 500ml
EUR 131

SafePinky DNA Gel Staining Solution

S1000-100 2X500ml
EUR 188

SafePinky DNA Gel Staining Solution

S1000-200 4X500ml
EUR 280

Nerve Terminal Staining Kit V

70034 1SET
EUR 509
Description: Minimum order quantity: 1 unit of 1SET

Manual Staining System (12 Wells)

IMS001 1 ea.
EUR 356

Fluorescein Active Caspase Staining Kit

K2047-25 25 assays
EUR 238

Red Active Caspase Staining Kit

K2052-100 100 assays
EUR 572

Red Active Caspase Staining Kit

K2052-25 25 assays
EUR 238

Live-Dead Cell Staining Kit

K2081-100 100 staining
EUR 460

Stain Tray Slide Staining System

M920-1 1 Clear
EUR 428

Stain Tray Slide Staining System

M920-2 1 Black
EUR 445

Blue-Color AP Staining Kit

AP100B-1 50 Assays
EUR 262

Dual- Color AP Staining Kit

AP100D-1 100 Assays
EUR 412

Red-Color AP Staining Kit

AP100R-1 50 Assays
EUR 262

DNA Ploidy Analysis Staining Kit

K1439-1
EUR 588

DNA Ploidy Analysis Staining Kit

K1439-5
EUR 2002

Live-Dead Cell Staining Kit

K501-100
EUR 468

CaspGLOW Active Caspase Staining Kit

55R-1292 25 assays
EUR 296
Description: Caspase Staining Kit for use activity in the research laboratory

Live/Dead Cell Staining Kit

55R-1434 100 tests
EUR 638
Description: Live/Dead Cell Staining Kit for use in the research laboratory

Sheep ALP ELISA Kit

ESA0038 96Tests
EUR 521

Mouse ALP ELISA Kit

EMA0038 96Tests
EUR 521

Monkey ALP ELISA Kit

EMKA0038 96Tests
EUR 521

Porcine ALP ELISA Kit

EPA0038 96Tests
EUR 521

Rat ALP ELISA Kit

ERA0038 96Tests
EUR 521

Rabbit ALP ELISA Kit

ERTA0038 96Tests
EUR 521

Anserini ALP ELISA Kit

EAA0038 96Tests
EUR 521

Goat ALP ELISA Kit

EGTA0038 96Tests
EUR 521

Canine ALP ELISA Kit

ECA0038 96Tests
EUR 521

Chicken ALP ELISA Kit

ECKA0038 96Tests
EUR 521

Human ALP ELISA Kit

EHA0038 96Tests
EUR 521

Bovine ALP ELISA Kit

EBA0038 96Tests
EUR 521

Alkaline Phosphatase (ALP) Antibody

20-abx121265
  • EUR 300.00
  • EUR 439.00
  • EUR 189.00
  • 100 ul
  • 200 ul
  • 30 ul

Alkaline Phosphatase (ALP) Antibody

abx038456-100ug 100 ug
EUR 391

Protein A Antibody (ALP)

abx023329-2ml 2 ml
EUR 843

Endoplasmin (GRP94) Antibody (ALP)

abx442250-200ug 200 ug
EUR 578

GRP75 (Grp75) Antibody (ALP)

abx442270-100ug 100 ug
EUR 565

ubiquitin (Ubiquitin) Antibody (ALP)

abx442291-200ug 200 ug
EUR 620

ubiquitin (Ubiquitin) Antibody (ALP)

abx442300-200ug 200 ug
EUR 620

Rhodopsin (RHO) Antibody (ALP)

abx442303-100ug 100 ug
EUR 578

Rhodopsin (RHO) Antibody (ALP)

abx442304-100ug 100 ug
EUR 578

Synaptophysin (SYP) Antibody (ALP)

abx442305-100ug 100 ug
EUR 509

Syntaxin (STX) Antibody (ALP)

abx442308-100ug 100 ug
EUR 537

Piccolo (Pclo) Antibody (ALP)

abx442314-100ug 100 ug
EUR 565

Kir2.1 (Kir2.1) Antibody (ALP)

abx442362-100ug 100 ug
EUR 578

Kir2.2 (Kir2.2) Antibody (ALP)

abx442363-100ug 100 ug
EUR 578

VGLUT1 (VGLUT1) Antibody (ALP)

abx442402-100ug 100 ug
EUR 578

VGLUT2 (VGLUT2) Antibody (ALP)

abx442403-100ug 100 ug
EUR 578

Versican (VCAN) Antibody (ALP)

abx442447-100ug 100 ug
EUR 578

Malin (NHLRC1) Antibody (ALP)

abx442452-100ug 100 ug
EUR 578

Laforin (EPM2A) Antibody (ALP)

abx442472-100ug 100 ug
EUR 578

Kir6.1 (Kir6.1) Antibody (ALP)

abx442497-100ug 100 ug
EUR 578

Citrulline (CIT) Antibody (ALP)

abx442502-100ug 100 ug
EUR 662

Citrulline (CIT) Antibody (ALP)

abx442503-100ug 100 ug
EUR 662

Endoplasmin (GRP94) Antibody (ALP)

abx447036-100ug 100 ug
EUR 537

Piccolo (Pclo) Antibody (ALP)

abx447495-100ug 100 ug
EUR 578

ubiquitin (Ubiquitin) Antibody (ALP)

abx447954-200ul 200 ul
EUR 620

Metallothionein (mymT) Antibody (ALP)

abx448218-100ug 100 ug
EUR 578

ubiquitin (Ubiquitin) Antibody (ALP)

abx444810-100ug 100 ug
EUR 398

Calreticulin (CALR) Antibody (ALP)

abx445319-200ul 200 ul
EUR 551

Bassoon (BSN) Antibody (ALP)

abx446594-100ug 100 ug
EUR 578

Rubicon (Rubicon) Antibody (ALP)

abx446730-100ug 100 ug
EUR 578

Alkaline Phosphatase (ALP) Antibody

20-abx175316
  • EUR 1177.00
  • EUR 578.00
  • 1 mg
  • 200 ug

Alkaline Phosphatase (ALP) Antibody

20-abx175317
  • EUR 1247.00
  • EUR 592.00
  • 1 mg
  • 200 ug

Anti-ASRGL1 / ALP antibody

STJ71356 100 µg
EUR 359

Recombinant Alkaline Phosphatase (ALP)

4-RPB472Bo01
  • EUR 503.20
  • EUR 238.00
  • EUR 1612.00
  • EUR 604.00
  • EUR 1108.00
  • EUR 400.00
  • EUR 3880.00
  • 100 ug
  • 10ug
  • 1 mg
  • 200 ug
  • 500 ug
  • 50ug
  • 5 mg
Description: Recombinant Bovine Alkaline Phosphatase expressed in: E.coli

ALP ELISA KIT|Human

EF009206 96 Tests
EUR 689

QuantiFluo ALP Detection Reagent

QFALP-6mL 600
EUR 156
Description: A stable 4-methylumbelliferyl phosphate (MUP) liquid substrate reagent formulated for detecting alkaline phosphatase ALP, e.g. in ELISA. This single reagent produces a highly fluorescent product (360/450 nm) when dephosphorylated by ALP. The fluorescent p

STAT Double Staining ragent for Double staining Mouse and Sheep antibodies, 450 Plus slides

NB330DB 25 ml
EUR 740

StemTAG Alkaline Phosphatase Staining Kit (Red)

CBA-300 100 assays
EUR 461
Description: Alkaline Phosphatase (AP) is a widely used marker for both mouse and human embryonic stem cells (ES) and embryonic germ cells (EG). Our StemTAG Alkaline Phosphatase kits provide an efficient system for monitoring cell differentiation or undifferentiation using the AP marker. The StemTAG Alkaline Phosphatase Staining Kits provide reagents for monitoring alkaline phosphatase activity via immunocytochemistry staining.

StemTAG Alkaline Phosphatase Staining Kit (Purple)

CBA-306 100 assays
EUR 461
Description: Alkaline Phosphatase (AP) is a widely used marker for both mouse and human embryonic stem cells (ES) and embryonic germ cells (EG). Our StemTAG Alkaline Phosphatase kits provide an efficient system for monitoring cell differentiation or undifferentiation using the AP marker. The StemTAG Alkaline Phosphatase Staining Kits provide reagents for monitoring alkaline phosphatase activity via immunocytochemistry staining.

Human Type I Collagen Staining Kit

9044 1 kit
EUR 338.55
Description: Human Type I Collagen Staining Kit

Coomassie Brilliant Blue Fast Staining Solution

abx090652-200ml 200 ml
EUR 203

Coomassie Brilliant Blue Gel Staining Kit

abx090653-1Kit 1 Kit
EUR 189

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What is apparent is that there may be a sustained world growth in utilisation of ART and that reproductive tourism will allow many people to entry the remedy they want nevertheless nationwide legal guidelines that may forbid some approaches. The greatest drawback is to broaden entry to ART to those residing in the a lot much less wealthy nations who’re equally deserving of its benefits.