Category On the fate of primordial germ cells injected into early mouse embryos.

Downregulated RRS1 inhibits invasion and metastasis of BT549 through RPL11‑c‑Myc‑SNAIL axis

Regulator of ribosome synthesis 1 (RRS1) is a key factor in ribosome biosynthesis and other cellular functions. High level of RRS1 in breast cancer cell lines is associated with increased cell proliferation, invasion and migration. RRS1 controls the assembly of the 60s subunit and maturation of 25S rRNA during ribosome biosynthesis.
In this study, lentiviral transfection of sh‑RNA was used to knock down the level of RRS1, to detect the effect of RRS1 on cell function and to explore the specific mechanism of RRS1 affecting cell invasion and metastasis by COIP and dual‑luciferase reporter gene assays.
The present study found that RRS1 knockdown reduced the accumulation of ribosome protein L11 (RPL11) in the nucleolus, which then migrated to the nucleoplasm and bound to c‑Myc. This inhibited trans‑activation of SNAIL by c‑Myc and eventually decreased the invasion and metastasis capacity of the human breast cancer cell line BT549.
Taken together, RRS1 regulates invasion and metastasis of human breast cancer cells through the RPL11‑c‑Myc‑SNAIL axis. The findings are of great significance for exploring the mechanism of breast cancer invasion and metastasis and the corresponding regulatory factors.

Jumonji-C domain-containing protein 5 suppresses proliferation and aerobic glycolysis in pancreatic cancer cells in a cMyc-dependent manner

Despite the importance of metabolic reprogramming in cancer cells, the molecular mechanism regulating the tumor metabolic shift is still poorly understood. Deregulation of Jumonji-C domain-containing protein 5 (JMJD5) has been associated with multiple facets of biological processes in cancer cells.
However, the role of JMJD5 in pancreatic cancer cells has seldom been discussed and requires further investigation. In the present study, by silencing or overexpressing JMJD5 in pancreatic cancer cells, we examined the impact of JMJD5 on cell proliferation and glucose metabolism. Using a dual luciferase assay, we assessed the effect of JMJD5 on the transcriptional activity of the c-Myc target gene.
Analyzing The Cancer Genome Atlas and the Gene Expression Omnibus datasets revealed that low JMJD5 expression was associated with poor prognosis in patients with pancreatic cancer.
JMJD5 loss promoted pancreatic cancer cell proliferation and induced a cellular metabolic shift from oxidative phosphorylation to glycolysis. In addition, in vivo experiments confirmed that ectopic JMJD5 expression inhibited cancer cell growth and the expression of glycolytic enzymes, such as lactate dehydrogenase and phosphoglycerate kinase 1.
Moreover, JMJD5 negatively regulated c-Myc expression, the main regulator of cancer metabolism, leading to decreased c-Myc-targeted gene expression. Overall, the present study indicated that decreased JMJD5 expression promoted cell proliferation and glycolytic metabolism in pancreatic cancer cells in a c-Myc-dependent manner.

Imaging-Based Screening of Deubiquitinating Proteases Identifies Otubain-1 as a Stabilizer of cMYC

The ubiquitin-proteasome pathway precisely controls the turnover of transcription factors in the nucleus, playing an important role in maintaining appropriate quantities of these regulatory proteins. The transcription factor c-MYC is essential for normal development and is a critical cancer driver. Despite being highly expressed in several tissues and malignancies, the c-MYC protein is also continuously targeted by the ubiquitin-proteasome pathway, which can either facilitate or inhibit c-MYC degradation. Deubiquitinating proteases can remove ubiquitin chains from target proteins and rescue them from proteasomal digestion.
This study sought to determine novel elements of the ubiquitin-proteasome pathway that regulate c-MYC levels. We performed an overexpression screen with 41 human proteases to identify which deubiquitinases stabilize c-MYC. We discovered that the highly expressed Otubain-1 (OTUB1) protease increases c-MYC protein levels.
Confirming its role in enhancing c-MYC activity, we found that elevated OTUB1 correlates with inferior clinical outcomes in the c-MYC-dependent cancer multiple myeloma, and overexpression of OTUB1 accelerates the growth of myeloma cells. In summary, our study identifies OTUB1 as a novel amplifier of the proto-oncogene c-MYC.

Rational design of small-molecules to recognize G-quadruplexes of cMYC promoter and telomere and the evaluation of their in vivo antitumor activity against breast cancer

DNA G4-structures from human c-MYC promoter and telomere are considered as important drug targets; however, the developing of small-molecule-based fluorescent binding ligands that are highly selective in targeting these G4-structures over other types of nucleic acids is challenging.
We herein report a new approach of designing small molecules based on a non-selective thiazole orange scaffold to provide two-directional and multi-site interactions with flanking residues and loops of the G4-motif for better selectivity.
The ligands are designed to establish multi-site interactions in the G4-binding pocket. This structural feature may render the molecules higher selectivity toward c-MYC G4s than other structures.
The ligand-G4 interaction studied with 1H NMR may suggest a stacking interaction with the terminal G-tetrad. Moreover, the intracellular co-localization study with BG4 and cellular competition experiments with BRACO-19 may suggest that the binding targets of the ligands in cells are most probably G4-structures.
Furthermore, the ligands that either preferentially bind to c-MYC promoter or telomeric G4s are able to downregulate markedly the c-MYC and hTERT gene expression in MCF-7 cells, and induce senescence and DNA damage to cancer cells. The in vivo antitumor activity of the ligands in MCF-7 tumor-bearing mice is also demonstrated.

cMyc Targets HDAC3 to Suppress NKG2DL Expression and Innate Immune Response in N-Type SCLC through Histone Deacetylation

SCLC is an aggressive malignancy with a very poor prognosis and limited effective therapeutic options. Despite the high tumor mutational burden, responses to immunotherapy are rare in SCLC patients, which may be due to the lack of immune surveillance.
Here, we aimed to examine the role and mechanism of oncogene MYC in the regulation of NKG2DL, the most relevant NK-activating ligand in SCLC-N.
Western Blotting, Immunofluorescence, flow cytometry, quantitative real-time PCR (qRT-PCR), Co-Immunoprecipitation (Co-IP), chromatin immunoprecipitation (ChIP), and Cytotoxicity assay were used on H2227 cells, H446 cells, and other SCLC cell lines, and we found that c-Myc negatively regulated NKG2DL expression in SCLC-N cells. Mechanistically, c-Myc recruited HDAC3 to deacetylate H3K9ac at the promoter regions of MICA and MICB, suppressing the MICA/B expression of SCLC-N cells and the cytotoxicity of NK cells.

Human V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

RD-MYC-Hu-48Tests Reddot Biotech 48 Tests 500 EUR

Human V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

RD-MYC-Hu-96Tests Reddot Biotech 96 Tests 692 EUR

Mouse V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

RD-MYC-Mu-48Tests Reddot Biotech 48 Tests 511 EUR

Mouse V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

RD-MYC-Mu-96Tests Reddot Biotech 96 Tests 709 EUR

Rat V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

RD-MYC-Ra-48Tests Reddot Biotech 48 Tests 534 EUR

Rat V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

RD-MYC-Ra-96Tests Reddot Biotech 96 Tests 742 EUR

Human V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

DLR-MYC-Hu-48T DL Develop 48T 498 EUR

Human V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

DLR-MYC-Hu-96T DL Develop 96T 647 EUR

Mouse V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

DLR-MYC-Mu-48T DL Develop 48T 508 EUR

Mouse V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

DLR-MYC-Mu-96T DL Develop 96T 661 EUR

Rat V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

DLR-MYC-Ra-48T DL Develop 48T 528 EUR

Rat V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

DLR-MYC-Ra-96T DL Develop 96T 690 EUR

Human V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

RDR-MYC-Hu-48Tests Reddot Biotech 48 Tests 522 EUR

Human V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

RDR-MYC-Hu-96Tests Reddot Biotech 96 Tests 724 EUR

Mouse V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

RDR-MYC-Mu-48Tests Reddot Biotech 48 Tests 534 EUR

Mouse V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

RDR-MYC-Mu-96Tests Reddot Biotech 96 Tests 742 EUR

Rat V-Myc Myelocytomatosis Viral Oncogene Homolog (MYC) ELISA Kit

RDR-MYC-Ra-48Tests Reddot Biotech 48 Tests 558 EUR
Treatment with selective HDAC3 inhibitor up-regulated the expression of NKG2DL on SCLC-N cells and increased the cytotoxicity of NK cells. Furthermore, analysis of the CCLE and Kaplan-Meier plotter data performed the negative correlation between MYC and NKG2DL in SCLC-N cells and the correlation with the prognosis of lung cancer patients.
Collectively, the results provided the new insight into the role and mechanism of c-Myc/HDAC3 axis in NKG2DL expression and innate immune escape of SCLC-N, suggesting the potential target for SCLC-N immunotherapy.

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

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) 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) 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

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

abx016078-100ul Abbexa 100 ul 411 EUR

OVA Conjugated FLAG Octapeptide (FLAG)

4-CPX159Ge21 Cloud-Clone
  • 187.81 EUR
  • 153.00 EUR
  • 429.28 EUR
  • 209.76 EUR
  • 319.52 EUR
  • 188.00 EUR
  • 923.20 EUR
  • 100 ug
  • 10ug
  • 1 mg
  • 200 ug
  • 500 ug
  • 50ug
  • 5 mg
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.

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.

Complement Inhibitors Vitronectin and Clusterin Are Recruited from Human Serum to the Surface of Coronavirus OC43-Infected Lung Cells through Antibody-Dependent Mechanisms

Little is known about the role of complement (C’) in infections with highly prevalent circulating human coronaviruses such as OC43, a group of viruses of major public health concern. Treatment of OC43-infected human lung cells with human serum resulted in C3 deposition on their surfaces and generation of C5a, indicating robust C’ activation.
Real-time cell viability assays showed that in vitro C’-mediated lysis of OC43 infected cells requires C3, C5 and C6 but not C7, and was substantially delayed as compared to rapid C’-mediated killing of parainfluenza virus type 5 (PIV5)-infected cells.
In cells co-infected with OC43 and PIV5, C’-mediated lysis was delayed, similar to OC43 infected cells alone, suggesting that OC43 infection induced dominant inhibitory signals.
When OC43-infected cells were treated with human serum, their cell surfaces contained both Vitronectin (VN) and Clusterin (CLU), two host cell C’ inhibitors that can alter membrane attack complex (MAC) formation and C’-mediated killing.
VN and CLU were not bound to OC43-infected cells after treatment with antibody-depleted serum. Reconstitution experiments with purified IgG and VN showed that human antibodies are both necessary and sufficient for VN recruitment to OC43-infected lung cells-novel findings with implications for CoV pathogenesis.

Additivity in effects of vitronectin and monoclonal antibodies against alpha-helix F of plasminogen activator inhibitor-1 on its reactions with target proteinases.

The serpin plasminogen activator inhibitor-1 (PAI-1) is a potential therapeutic target in cardiovascular and cancerous diseases. PAI-1 circulates in blood as a complex with vitronectin. A PAI-1 variant (N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-3-diazole (NBD) P9 PAI-1) with a fluorescent tag at the reactive center loop (RCL) was used to study the effects of vitronectin and monoclonal antibodies (mAbs) directed against alpha-helix F (Mab-2 and MA-55F4C12) on the reactions of PAI-1 with tissue-type and urokinase-type plasminogen activators.
Both mAbs delay the RCL insertion and induce an increase in the stoichiometry of inhibition (SI) to 1.4-9.5.
Binding of vitronectin to NBD P9 PAI-1 does not affect SI but results in a 2.0-6.5-fold decrease in the limiting rate constant (klim) of RCL insertion for urokinase-type plasminogen activator at pH 6.2-8.0 and for tissue-type plasminogen activator at pH 6.2.
Binding of vitronectin to the complexes of NBD P9 PAI-1 with mAbs results in a decrease in klim and in a 1.5-22-fold increase in SI. Thus, vitronectin and mAbs demonstrated additivity in the effects on the reaction with target proteinases.
The same step in the reaction mechanism remains to limit for the rate of RCL insertion in the absence and presence of Vn and mAbs. We hypothesize that vitronectin, bound to alpha-helix F on the side opposite to the epitopes of the mAbs, potentiates the mAb-induced delay in RCL insertion and the associated substrate behavior by selectively decreasing the rate constant for the inhibitory branch of PAI-1 reaction (ki).
These results demonstrate that mAbs represent a valid approach for inactivation of vitronectin-bound PAI-1 in vivo.

Activated vitronectin as a target for anticancer therapy with human antibodies.

The formation of a provisional extracellular matrix represents an important step during tumor growth and angiogenesis. Proteins that participate in this process become activated and undergo conformational changes that expose biologically active cryptic sites.
Activated matrix proteins express epitopes not found on their native counterparts. We hypothesized that these epitopes may have a restricted tissue distribution, rendering them suitable targets for therapeutic human monoclonal antibodies (huMabs).
In this study, we exploited phage antibody display technology and subtractive phage selection to generate human monoclonal antibody fragments that discriminate between the activated and native conformation of the extracellular matrix protein vitronectin.
One of the selected antibody fragments, scFv VN18, was used to construct a fully human IgG/kappa monoclonal antibody with an affinity of 9.3 nM. In immunohistochemical analysis, scFv and huMab VN18 recognized activated vitronectin in tumor tissues, whereas hardly any activated vitronectin was detectable in normal tissues.
Iodine 123-radiolabeled huMabVN18 was shown to target to Rous sarcoma virus-induced tumors in chickens, an animal model in which the epitope for huMab VN18 is exposed during tumor development. Our results establish activated vitronectin as a potential target for tumor therapy in humans.

New insights into heparin binding to vitronectin: studies with monoclonal antibodies.

Vitronectin is a plasma glycoprotein that binds to a variety of ligands. There is considerable debate regarding the dependency of these binding interactions upon the conformational status of vitronectin, the role of multimerization and how the binding of different ligands can change vitronectin’s conformational state.
We have developed a method of capturing vitronectin directly from fresh plasma using solid-phase monoclonal antibodies. Various biotin-labelled secondary monoclonal antibodies were used to quantify the bound vitronectin and to measure its degree of denaturation.
Using these tools we demonstrated that one monoclonal antibody partially denatured vitronectin without direct multimerization.
Treatment of vitronectin in plasma with soluble heparin produced a similar degree of denaturation. These results led to a proposed adaptation of the unfolding/refolding pathways for chemically denatured vitronectin originally presented by Zhuang and co-workers in 1996 [Zhuang, Blackburn and Peterson (1996) J. Biol. Chem. 271, 14323-14332 and Zhuang, Li, Williams, Wagner, Seiffert and Peterson (1996) J. Biol. Chem. 271, 14333-14343]. The adapted version allows for the production of a more stable partially unfolded intermediate, resulting from the binding of particular ligands.
We also demonstrated that the avidity of heparin binding to vitronectin is governed by both the conformational state of the monomer and multimerization of the molecule.

Epitope mapping for four monoclonal antibodies against human plasminogen activator inhibitor type-1: implications for antibody-mediated PAI-1-neutralization and vitronectin-binding.

The inhibitory mechanism of serine proteinase inhibitors of the serpin family is based on their unique conformational flexibility. The formation of a stable proteinase-serpin complex implies insertion of the reactive centre loop of the serpin into the large central beta-sheet A and a shift in the relative positions of two groups of secondary structure elements, the smaller one including alpha-helix F.
In order to elucidate this mechanism,
we have used phage-display and alanine scanning mutagenesis to map the epitopes for four monoclonal antibodies against alpha-helix F and its flanking region in the serpin plasminogen activator inhibitor-1 (PAI-1).
One of these is known to inhibit the reaction between PAI-1 and its target proteinases, an effect that is potentiated by vitronectin, a physiological carrier protein for PAI-1.
When combined with the effects these antibodies have on PAI-1 activity, our epitope mapping points to the mobility of amino-acid residues in alpha-helix F and the loop connecting alpha-helix F and beta-strand 3A as being important for the inhibitory function of PAI-1.

Vitronectin Antibody

abx023996-200ug Abbexa 200 ug 578 EUR

Vitronectin Antibody

48876-100ul SAB 100ul 333 EUR

Vitronectin Antibody

48876-50ul SAB 50ul 239 EUR

Vitronectin antibody

10R-8488 Fitzgerald 100 ul 393 EUR

Vitronectin antibody

70R-10610 Fitzgerald 500 ug 492 EUR

Vitronectin antibody

10-1962 Fitzgerald 200 ul 543 EUR

Vitronectin antibody

10-1963 Fitzgerald 200 ul 543 EUR

Vitronectin antibody

10-1964 Fitzgerald 200 ul 769 EUR

Vitronectin antibody

10-1965 Fitzgerald 200 ul 543 EUR

Vitronectin antibody

20R-1396 Fitzgerald 10 mg 275 EUR

Vitronectin antibody

70R-14336 Fitzgerald 100 ug 322 EUR

Vitronectin antibody

70R-50548 Fitzgerald 100 ul 244 EUR

Vitronectin Polyclonal Antibody

ES8386-100ul ELK Biotech 100ul 279 EUR

Vitronectin Polyclonal Antibody

ES8386-50ul ELK Biotech 50ul 207 EUR

Vitronectin Polyclonal Antibody

ES7512-100ul ELK Biotech 100ul 279 EUR

Vitronectin Polyclonal Antibody

ES7512-50ul ELK Biotech 50ul 207 EUR

Anti-Vitronectin antibody

STJ16100270 St John's Laboratory 1 mL 720 EUR

Anti-Vitronectin antibody

STJ16100802 St John's Laboratory 100 µg 506 EUR

Human Vitronectin Antibody

48629-05011 AssayPro 150 ug 217 EUR

Vitronectin Polyclonal Antibody

ABP57393-003ml Abbkine 0.03ml 158 EUR

Vitronectin Polyclonal Antibody

ABP57393-01ml Abbkine 0.1ml 289 EUR
Although all antibodies reduced the affinity of PAI-1 for vitronectin, the potentiating effect of vitronectin on antibody-induced PAI-1 neutralization is based on formation of a ternary complex between antibody, PAI-1 and vitronectin, in which PAI-1 is maintained in a state behaving as a substrate for plasminogen activators.
These results thus provide new details about serpin conformational changes and the regulation of PAI-1 by vitronectin and contribute to the necessary basis for rational design of drugs neutralizing PAI-1 in cancer and cardiovascular diseases.

Short-Term Therapy with Anti-ICAM-1 Monoclonal Antibody Induced Long-Term Liver Allograft Survival in Non-Human Primates

Tolerance induction remains challenging following liver transplantation and the long-term use of immunosuppressants, especially calcineurin inhibitors, leads to serious complications.
We aimed to test an alternative immunosuppressant, a chimeric anti-ICAM-1 monoclonal antibody, MD-3, for improving outcomes of liver transplantation. We used a rhesus macaques liver transplantation model and monkeys were divided into three groups: no immunosuppression (n=2), conventional immunosuppression (n=4), and MD-3 (n=5).
Without immunosuppression, liver allografts failed within a week by acute rejection. Sixteen-week-long conventional immunosuppression that consisted of prednisolone, tacrolimus, and an mTOR inhibitor, prolonged liver allograft survival; however, recipients died of acute T cell-mediated rejection (day 52), chronic rejection (day 62, 66) or adverse effects of mTOR inhibitor (day 32).
In contrast, 12 weeks-long MD-3 therapy with transient conventional immunosuppression in the MD-3 group significantly prolonged the survival of liver allograft recipients (5, 96, 216, 412, 730 days; P = 0.0483). MD-3 effectively suppressed intragraft inflammatory cell infiltration, anti-donor T cell responses and donor-specific antibody with intact anti-cytomegalovirus antibody responses.
However, this regimen ended in chronic rejection. In conclusion, short-term therapy with MD-3 markedly improved liver allograft survival to 2 years without maintenance of immunosuppressant. MD-3 is therefore a promising immune-modulating agent for liver transplantation.

Fc-engineering significantly improves the recruitment of immune effector cells by anti-ICAM-1 antibody MSH-TP15 for myeloma therapy

Despite several therapeutic advances, patients with multiple myeloma (MM) require additional treatment options since no curative therapy exists yet.
In search of a novel therapeutic antibody, we previously applied phage display with myeloma cell screening and developed TP15, a scFv targeting intercellular adhesion molecule 1 (ICAM-1/CD54). To more precisely evaluate the antibody’s modes of action, fully human IgG1 antibody variants were generated bearing wild-type (MSH-TP15) or mutated Fc to either enhance (MSH-TP15 Fc-eng.) or prevent (MSH-TP15 Fc k.o.) Fc gamma receptor binding. Especially MSH-TP15 Fc-eng. induced potent antibody-dependent cell-mediated cytotoxicity (ADCC) against malignant plasma cells by efficiently recruiting NK cells and engaged macrophages for antibody-dependent cellular phagocytosis (ADCP) of tumor cells. Binding studies with truncated ICAM-1 demonstrated MSH-TP15 binding to ICAM-1 domain 1-2.
Importantly, MSH-TP15 and MSH-TP15 Fc-eng. both prevented myeloma cell engraftment and significantly prolonged survival of mice in an intraperitoneal xenograft model. In the subcutaneous model MSH-TP15 Fc-eng. was superior to MSH-TP15, whereas MSH-TP15 Fc k.o. was not effective in both models – reflecting the importance of Fc-dependent mechanisms of action also in vivo.
The efficient recruitment of immune cells and the potent anti-tumor activity of the Fc-engineered MSH-TP15 antibody hold significant potential for myeloma immunotherapy.

Effective targeted therapy for drug-resistant infection by ICAM-1 antibody-conjugated TPGS modified β-Ga2O3:Cr3+ nanoparticles.

The prevalence of antibiotic resistance and lack of alternative drugs have posed an increasing threat to public health. Here, we prepared β-Ga2O3:Cr3+ nanoparticles modified with ICAM1-antibody-conjugated TPGS (I-TPGS/Ga2O3) as a novel antibiotic carrier for the treatment of drug-resistant infections.
 Methods: I-TPGS/Ga2O3 were firstly characterized by measuring particle size, morphology, crystal structure, drug loading capacity, and in vitro drug release behaviors. The in vitro antibacterial activities of I-TPGS/Ga2O3/TIG were evaluated using standard and drug-resistant bacteria. The internalization of I-TPGS/Ga2O3 was observed by fluorescence confocal imaging, and the expression levels of the efflux pump genes of TRKP were analyzed by real-time RT-PCR.
In vitro cellular uptake and in vivo biodistribution study were performed to investigate the targeting specificity of I-TPGS/Ga2O3 using HUEVC and acute pneumonia mice, respectively. The in vivo anti-infective efficacy and biosafety of I-TPGS/Ga2O3/TIG were finally evaluated using acute pneumonia mice.
 Results: It was found that TPGS could down-regulate the over-expression of the efflux pump genes, thus decreasing the efflux pump activity of bacteria. I-TPGS/Ga2O3 with small particle size and uniform distribution facilitated their internalization in bacteria, and the TPGS modification resulted in a significant reduction in the efflux of loaded antibiotics.
These properties rendered the encapsulated tigecycline to exert a stronger antibacterial activity both in vitro and in vivo. Additionally, targeted delivery of I-TPGS/Ga2O3 mediated by ICAM1 antibodies contributed to a safe and effective therapy.
 Conclusion: It is of great value to apply I-TPGS/Ga2O3 as a novel and effective antibiotic delivery system for the treatment of drug-resistant infections.

Polyclonal and monoclonal antibodies against chicken gizzard 5‘-nucleotidase inhibit the spreading process of chicken embryonic fibroblasts on laminin substratum.

Polyclonal and monoclonal antibodies raised against chicken gizzard 5′-nucleotidase were tested in adhesion assays of embryonic chicken fibroblasts (CEF) for their ability to interfere with the adhesion process of these cells on either laminin or fibronectin substrata. The initial attachment process of CEF on fibronectin and laminin substrata was not influenced by preincubating these cells with antibodies against chicken gizzard 5′-nucleotidase.
However, the subsequent spreading process of these cells was found to be inhibited for at least 2 h on a laminin substratum. This effect was obtained with a polyclonal antibody as well as with one from 12 monoclonal antibodies raised against the native enzyme purified from chicken gizzard.
In vitro assays demonstrated a competition of laminin and this monoclonal antibody for the binding site on purified 5′-nucleotidase. Spreading-arrested and rounded CEF do not develop prominent intracellular stress-fibers like control cells, instead they seem to concentrate their available actin in areas of presumptive initial contact with the laminin substratum.

Clinical and immunological heterogeneity of canine subepidermal blistering dermatoses with anti-<em>laminin</em>-332 (<em>laminin</em>-<em>5</em>) auto-<em>antibodies</em>.

Laminin-332 (laminin-5) is a basement membrane heterotrimeric protein composed of alpha-3, beta-3 and gamma-2 laminin chains. Laminin-332 polypeptides are targeted by auto-antibodies in human patients with mucous membrane (cicatricial) pemphigoid or, more rarely, subepidermal vesicular diseases that resemble epidermolysis bullosa acquisita (EBA) or bullous pemphigoid (BP).
The objectives of this report were to characterize the clinical, histopathological and immunological characteristics of nine dogs with auto-antibodies targeting laminin-332. Immunological investigations consisted of direct immunofluorescence (IF), indirect IF with intact and salt-split canine gingival, and salt-split normal or laminin-332-deficient human skin, immunoblotting with purified human laminin-332 and immunoblotting with recombinant NC1 domain of human collagen VII.
All dogs exhibited varying degrees of skin blistering and ulceration associated with microscopic subepidermal vesiculation with or without inflammatory cells. Indirect IF established that circulating IgG auto-antibodies bound the dermal side of salt-split canine lip and human skin. In five dogs, IgG variably recognized the basement membrane of laminin-332-deficient human skin (three dogs negative, two dogs positive).
In all nine dogs, IgG auto-antibodies detected purified human laminin-332 by immunoblotting. In two dogs, additional targeting of collagen VII-NC1 was present.
These observations establish laminin-332 as a novel basement membrane antigen in dogs with autoimmune blistering diseases with variable clinical phenotypes. The names ‘acquired junctional epidermolysis bullosa’, ‘anti-laminin-332 mucous membrane pemphigoid (MMP)’ and ‘mixed auto-immune subepidermal blistering dermatosis’ are proposed for dogs with clinical signs reminiscent of EBA, MMP or BP respectively.

Bullous pemphigoid positive for anti-BP180 and anti-<em>laminin</em> <em>5</em> <em>antibodies</em> in a patient with graft-vs-host disease.

We report the case of a 55-year-old female with bullous pemphigoid (BP) who was positive for anti-BP180 and anti-laminin 5 antibodies after development of graft-vs-host disease (GVHD) caused by a bone marrow transplant. She had tense blisters on her trunk and extremities.
Histologic examination showed a subepidermal blister and marked lymphocytic infiltration, especially eosinophils. Direct immunofluorescence revealed a linear deposition of IgG on the base membrane zone. Indirect immunofluorescence on 1M NaCl split skin revealed a linear IgG deposition to both sides of the epidermal and the dermal layers.
Immunoblot assays using human epidermal extracts and BP180 NC16a domain recombinant protein confirmed the presence of IgG antibodies against BP180 and recombinant BP180 NC16a domain protein. Furthermore, immunoblotting using laminin 5 purified from human keratinocyte extract as the substrate demonstrated reactivity against the gamma2 and beta3 subunits but not the alpha3 subunit of laminin 5.
We diagnosed BP and treated her with prednisolone (40 mg/day). Both skin and oral lesions resolved without leaving scars on the bulla. Immune disturbance as well as destruction of basal epidermal cells and base membrane by GVHD may result in the induction of autoimmune blistering diseases with unusual clinical and laboratory manifestations.

Ocular ‘non-scarring’ mucous membrane pemphigoid associated with anti-<em>laminin</em>-<em>5</em> <em>antibodies</em>.

Mucous membrane pemphigoid is a rare, chronic autoimmune disease characterized by subepidermal blistering and scarring, predominantly affecting mucous membranes. Ocular involvement frequently occurs and often represents the only manifestation of the disease.
We describe a 62-year-old woman with a bilateral 18-month duration of conjunctival hyperaemia, associated with erythema and oedema of the eyelids, lacking any typical ocular signs of mucous membrane pemphigoid such as sub-conjuctival fibrosis and scarring. Histology was not significant.
Direct immunofluorescence of the conjunctiva showed IgG, IgA and complement deposition along the basement membrane zone. Immunoprecipitation analysis of affinity purified laminin-5 revealed a band consistent with the beta3 chain of laminin-5. This represents the first case of pure ocular mucous membrane pemphigoid associated with anti-laminin-5 antibodies.

Detection of <em>laminin</em> <em>5</em>-specific auto-<em>antibodies</em> in mucous membrane and bullous pemphigoid sera by ELISA.

Mucous membrane pemphigoid (MMP) is an autoimmune bullous disease that primarily affects mucous membranes leading to a scarring phenotype. MMP patients produce auto-antibodies (auto-ab) that preferentially recognize two components of the dermoepidermal basement membrane zone (BMZ): bullous pemphigoid (BP)180 and laminin 5 (LN5). Since detection of disease-specific auto-ab may be critical for the diagnosis of MMP, we developed an ELISA with affinity-purified native human LN5. A total of 24 MMP, 72 BP, and 51 control sera were analyzed for LN5-specific auto-ab: 18/24 (75.0%) MMP and 29/72 (40.3%) BP sera were LN5 reactive.
Sensitivity and specificity of the LN5 ELISA for MMP were 75% and 84.3%, respectively, and 40.3% and 88.2% for BP, respectively.
The LN5 ELISA was more sensitive than a dot blot assay with native LN5, which detected LN5-reactive IgG in 14/24 (58.3%) MMP and 16/72 (22.2%) BP sera. In MMP, but not BP, levels of LN5-reactive IgG correlated with disease severity. Furthermore, IgG reactivity to LN5 of the MMP and BP sera was not significantly associated with IgG reactivity against other autoantigens of the BMZ, such as BP180 or BP230. Thus, the established LN5 ELISA holds great promise as a novel diagnostic and prognostic parameter for MMP.

<em>Antibody</em>-induced activation of beta1 integrin receptors stimulates cAMP-dependent migration of breast cells on <em>laminin</em>-<em>5</em>.

The beta1 integrin-stimulating antibody TS2/16 induces cAMP-dependent migration of MCF-10A breast cells on the extracellular matrix protein laminin-5. TS2/16 stimulates a rise in intracellular cAMP within 20 min after plating. Pertussis toxin, which inhibits both antibody-induced migration and cAMP accumulation, targets the Galphai3 subunit of heterotrimeric G proteins in these cells, suggesting that Galphai3 may link integrin activation and migration via a cAMP signaling pathway.

Anti-epiligrin cicatricial pemphigoid with <em>antibodies</em> against the gamma2 subunit of <em>laminin</em> <em>5</em>.

BACKGROUND
Cicatricial pemphigoid (CP) is a scarring subepithelial mucocutaneous blistering disease characterized by anti-basement membrane zone autoantibodies. Anti-epiligrin CP is an uncommon variant that has been recently characterized. Severe laryngeal involvement is infrequently observed in all forms of CP and has been documented in only 2 patients with anti-epiligrin CP.

Laminin 5 Antibody

abx020892-100ug Abbexa 100 ug 1358 EUR

Laminin ?-5 Polyclonal Antibody

ES6077-100ul ELK Biotech 100ul 279 EUR

Laminin ?-5 Polyclonal Antibody

ES6077-50ul ELK Biotech 50ul 207 EUR

Laminin alpha 5 antibody

70R-49989 Fitzgerald 100 ul 244 EUR

Laminin 5 Protein

abx069877-10ug Abbexa 10 ug 1156 EUR

anti-Laminin 5

YF-PA24065 Abfrontier 50 ul 334 EUR

anti-Laminin 5

YF-PA24067 Abfrontier 50 ul 334 EUR

Laminin Alpha-5 Polyclonal Antibody

ABP55078-003ml Abbkine 0.03ml 158 EUR

Laminin Alpha-5 Polyclonal Antibody

ABP55078-01ml Abbkine 0.1ml 289 EUR

Laminin Alpha-5 Polyclonal Antibody

ABP55078-02ml Abbkine 0.2ml 414 EUR

Laminin, Alpha 5 (LAMA5) Antibody

20-abx304327 Abbexa
  • 411.00 EUR
  • 1845.00 EUR
  • 599.00 EUR
  • 182.00 EUR
  • 300.00 EUR
  • 100 ug
  • 1 mg
  • 200 ug
  • 20 ug
  • 50 ug

Laminin Alpha 5 (LAMA5) Antibody

20-abx339132 Abbexa
  • 411.00 EUR
  • 300.00 EUR
  • 100 ul
  • 50 ul

Laminin Alpha 5 (LAMa5) Antibody

20-abx101531 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

Laminin Alpha 5 (LAMA5) Antibody

20-abx009049 Abbexa
  • 300.00 EUR
  • 439.00 EUR
  • 189.00 EUR
  • 100 ul
  • 200 ul
  • 30 ul

Laminin, Alpha 5 (LAMA5) Antibody

20-abx014033 Abbexa
  • 314.00 EUR
  • 98.00 EUR
  • 398.00 EUR
  • 495.00 EUR
  • 100 ug
  • 10 ug
  • 200 ug
  • 300 µg

Laminin, Alpha 5 (LAMA5) Antibody

abx432909-200ul Abbexa 200 ul 286 EUR

Laminin Alpha 5 (LAMa5) Antibody

20-abx177308 Abbexa
  • 1205.00 EUR
  • 578.00 EUR
  • 1 mg
  • 200 ug

Laminin Alpha 5 (LAMa5) Antibody

20-abx173303 Abbexa
  • 857.00 EUR
  • 439.00 EUR
  • 1 mg
  • 200 ug

Laminin, Alpha 5 (LAMA5) Antibody

abx216513-100ug Abbexa 100 ug 439 EUR

Laminin Alpha 5 (LAMA5) Antibody

20-abx325869 Abbexa
  • 314.00 EUR
  • 244.00 EUR
  • 100 ug
  • 50 ug

Anti-Laminin alpha-5 antibody

STJ93892 St John's Laboratory 200 µl 197 EUR

Laminin (925-933)

5-01438 CHI Scientific 4 x 5mg Ask for price

Laminin (929-933)

5-01439 CHI Scientific 4 x 5mg Ask for price

Laminin Nonapeptide, Amide

5-01441 CHI Scientific 4 x 5mg Ask for price

Laminin (925-933)

A1023-5 ApexBio 5 mg 189 EUR

anti-Laminin 5 (2G10)

LF-MA10171 Abfrontier 100 ug 363 EUR

anti-laminin alpha 5

YF-PA12922 Abfrontier 100 ug 403 EUR
METHODS
We report a case of CP exhibiting extensive laryngeal and ocular involvement. Histological, immunofluorescence, and immunoprecipitation studies confirmed the diagnosis of anti-epiligrin CP. Immunoblotting studies demonstrated the presence of antibodies against the alpha3 and the gamma2 subunit of laminin 5.
CONCLUSIONS
This article expands the diversity of the clinical and immunopathologic features of this newly characterized variant of CP.
On the fate of primordial germ cells injected into early mouse embryos.

On the fate of primordial germ cells injected into early mouse embryos.

Primordial germ cells (PGCs) are the founder cells of the germline. Via gametogenesis and fertilisation this lineage generates a brand new embryo in the subsequent technology. PGCs are additionally the cell of origin of multilineage teratocarcinomas.

In vitro, mouse PGCs can provide rise to embryonic germ (EG) cells – pluripotent stem cells that may contribute to main chimaeras when launched into pre-implantation embryos. Thus, PGCs can provide rise to pluripotent cells in the course of the developmental cycle, throughout teratocarcinogenesis and by in vitro tradition. However, there isn’t any proof that PGCs can differentiate instantly into somatic cell varieties.

Furthermore, it’s typically assumed that PGCs don’t contribute to chimaeras following injection into the early mouse embryo. However, these knowledge have by no means been formally revealed. Here, we current the main knowledge from the unique PGC-injection experiments carried out 40 years in the past, alongside outcomes from newer research in three separate laboratories.

These outcomes have knowledgeable and influenced present fashions of the relationship between pluripotency and the germline cycle. Current applied sciences enable additional experiments to substantiate and develop upon these findings and permit definitive conclusions as to the developmental efficiency of PGCs.

On the fate of primordial germ cells injected into early mouse embryos.

On the fate of primordial germ cells injected into early mouse embryos.

MC Chang–Reproductive biologist of distinction 1908-1991.

This article evaluations the outstanding life and main scientific achievements of the reproductive biologist M.C. Chang. His scholarly profession progressed from college in Peking, through Edinburgh, Scotland, and Cambridge, England, to the newly based Worcester Foundation for Experimental Biology in Massachusetts. At every stage, the hand of fate is famous as are the help and encouragement of key professors.

Chang’s personal contributions on capacitation of spermatozoa, in vitro fertilisation of mammalian eggs, and transplantation of oocytes and embryos are all introduced out, as is his important enter to the creation and improvement of a steroid contraceptive capsule.

alpha beta TcR antibody

10R-6708 100 ug
EUR 192
Description: Mouse monoclonal alpha beta TcR antibody

TCR alpha / beta Antibody (PerCP)

abx139896-100tests 100 tests
EUR 481

TCR alpha / beta Antibody (PE)

abx139897-100tests 100 tests
EUR 481

TCR alpha / beta Antibody (APC)

abx139898-100tests 100 tests
EUR 481

TCR alpha / beta Antibody (Biotin)

abx139899-01mg 0.1 mg
EUR 425

TCR alpha / beta Antibody (FITC)

abx139900-100tests 100 tests
EUR 425

TCR alpha / beta Antibody (FITC)

abx140307-01mg 0.1 mg
EUR 398

TCR alpha / beta Antibody (PE)

abx140308-01mg 0.1 mg
EUR 425

alpha beta TcR antibody (biotin)

61R-1695 100 ug
EUR 316
Description: Mouse monoclonal alpha beta TcR antibody (biotin)

T-Cell Receptor Alpha Beta (TCR Alpha/Beta) Antibody

abx413042-025mg 0.25 mg
EUR 565

T-Cell Receptor Alpha Beta (TCR Alpha/Beta) Antibody

abx414734-05mg 0.5 mg
EUR 829

T-Cell Receptor Alpha Beta (TCR Alpha/Beta) Antibody

abx414736-025mg 0.25 mg
EUR 565

T-Cell Receptor Alpha Beta (TCR Alpha/Beta) Antibody

abx414737-01mg 0.1 mg
EUR 439

Anti-Hu TCR alpha/beta PerCP

PC-607-T025 25 tests
EUR 140

Anti-Hu TCR alpha/beta PerCP

PC-607-T100 100 tests
EUR 240

Anti-Hu TCR alpha/beta Purified

11-607-C025 0.025 mg
EUR 99

Anti-Hu TCR alpha/beta Purified

11-607-C100 0.1 mg
EUR 158

Anti-Rt TCR alpha/beta Purified

11-653-C100 0.1 mg
EUR 131

Anti-Hu TCR alpha/beta APC

1A-607-T025 25 tests
EUR 140

Anti-Hu TCR alpha/beta APC

1A-607-T100 100 tests
EUR 240

Anti-Hu TCR alpha/beta Biotin

1B-607-C025 0.025 mg
EUR 122

Anti-Hu TCR alpha/beta Biotin

1B-607-C100 0.1 mg
EUR 204

Anti-Hu TCR alpha/beta FITC

1F-607-T025 25 tests
EUR 122

Anti-Hu TCR alpha/beta FITC

1F-607-T100 100 tests
EUR 204

Anti-Rt TCR alpha/beta FITC

1F-653-C025 0.025 mg
EUR 113

Anti-Rt TCR alpha/beta FITC

1F-653-C100 0.1 mg
EUR 186

Anti-Hu TCR alpha/beta PE

1P-607-T025 25 tests
EUR 140

Anti-Hu TCR alpha/beta PE

1P-607-T100 100 tests
EUR 240

Anti-Rt TCR alpha/beta PE

1P-653-C025 0.025 mg
EUR 122

Anti-Rt TCR alpha/beta PE

1P-653-C100 0.1 mg
EUR 204

T-Cell Receptor Alpha Beta (TCR Alpha/Beta) Antibody (FITC)

abx413043-01mg 0.1 mg
EUR 509

T-Cell Receptor Alpha Beta (TCR Alpha/Beta) Antibody (FITC)

abx413044-05mg 0.5 mg
EUR 718

T-Cell Receptor Alpha Beta (TCR Alpha/Beta) Antibody (FITC)

abx414735-01mg 0.1 mg
EUR 509

TCR beta Antibody

20-abx201040
  • EUR 272.00
  • EUR 411.00
  • 100 ug
  • 500 ug

TCR beta Antibody

20-abx218918
  • EUR 425.00
  • EUR 342.00
  • 100 ug
  • 50 ug

TCR beta Antibody

DF8621 200ul
EUR 304
Description: TCR β Antibody detects endogenous levels of total TCR β.

TCR beta antibody

10R-6585 100 ug
EUR 181
Description: Armenian Hamster monoclonal TCR beta antibody

TCR beta antibody

20R-1838 100 ug
EUR 673
Description: Rabbit polyclonal TCR beta antibody

TCR beta antibody

70R-12401 100 ug
EUR 418
Description: Rabbit polyclonal TCR beta antibody

TCR beta Antibody

5651-100
EUR 327

TCR beta Antibody

5651-30T
EUR 146

TCR alpha antibody

20R-1837 100 ug
EUR 673
Description: Rabbit polyclonal TCR alpha antibody

TCR alpha antibody

70R-12400 100 ug
EUR 460
Description: Rabbit polyclonal TCR alpha antibody

anti-TCR alpha

YF-PA14966 50 ug
EUR 363
Description: Mouse polyclonal to TCR alpha

anti-TCR alpha

YF-PA14967 50 ul
EUR 363
Description: Mouse polyclonal to TCR alpha

TCR alpha Antibody

5648-100
EUR 354

TCR alpha Antibody

5648-30T
EUR 146

T-Cell Receptor Alpha Beta V Beta 1 (TCR Alpha/Beta Vb1) Antibody

abx415177-025mg 0.25 mg
EUR 592

T-Cell Receptor Alpha Beta V Beta 2 (TCR Alpha/Beta Vb2) Antibody

abx415178-025mg 0.25 mg
EUR 592

Polyclonal TCR beta Antibody

APR00309G 0.1mg
EUR 484
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human TCR beta . This antibody is tested and proven to work in the following applications:

TCR Beta Polyclonal Antibody

ABP52577-003ml 0.03ml
EUR 158
Description: A polyclonal antibody for detection of TCR Beta from Human. This TCR Beta antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human TCR ?

TCR Beta Polyclonal Antibody

ABP52577-01ml 0.1ml
EUR 289
Description: A polyclonal antibody for detection of TCR Beta from Human. This TCR Beta antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human TCR ?

TCR Beta Polyclonal Antibody

ABP52577-02ml 0.2ml
EUR 414
Description: A polyclonal antibody for detection of TCR Beta from Human. This TCR Beta antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human TCR ?

Anti-TCR beta Antibody

A15765 100ul
EUR 397
Description: Rabbit Polyclonal Antibody for TCR beta Antibody (TRBC1) detection. Tested with WB in Human.

TCR beta Antibody (APC)

20-abx201033
  • EUR 370.00
  • EUR 272.00
  • 100 ug
  • 25 ug

TCR beta Antibody (Biotin)

20-abx201034
  • EUR 314.00
  • EUR 258.00
  • 100 ug
  • 25 ug

TCR beta Antibody (FITC)

20-abx201036
  • EUR 286.00
  • EUR 244.00
  • EUR 398.00
  • 100 ug
  • 25 ug
  • 500 ug

TCR beta Antibody (PE)

20-abx201037
  • EUR 370.00
  • EUR 272.00
  • 100 ug
  • 25 ug

TCR beta Antibody (PerCP)

20-abx201038
  • EUR 481.00
  • EUR 286.00
  • 100 ug
  • 25 ug

Anti-TCR beta antibody

STJ95953 200 µl
EUR 197
Description: Rabbit polyclonal to TCR beta.

TCR beta Blocking Peptide

DF8621-BP 1mg
EUR 195

TCR beta Blocking Peptide

33R-11054 50 ug
EUR 191
Description: A synthetic peptide for use as a blocking control in assays to test for specificity of TCR beta antibody, catalog no. 70R-12401

TCR beta antibody (FITC)

61R-1156 100 ug
EUR 181
Description: Armenian Hamster monoclonal TCR beta antibody (FITC)

TCR beta antibody (PE)

61R-1386 100 ug
EUR 219
Description: Armenian Hamster monoclonal TCR beta antibody (PE)

TCR beta antibody (biotin)

61R-1632 100 ug
EUR 165
Description: Armenian Hamster monoclonal TCR beta antibody (biotin)

TCR beta antibody (allophycocyanin)

61R-1895 100 ug
EUR 349
Description: Armenian Hamster monoclonal TCR beta antibody (allophycocyanin)

TCR beta Blocking Peptide

33R-10581 50 ug
EUR 349
Description: A synthetic peptide for use as a blocking control in assays to test for specificity of TCR beta antibody, catalog no. 20R-1838

TCR beta Blocking Peptide

5651BP-50
EUR 153

Polyclonal TCR alpha Antibody

AMM08788G 0.1mg
EUR 484
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human TCR alpha . This antibody is tested and proven to work in the following applications:

TCR alpha Blocking Peptide

33R-11053 50 ug
EUR 191
Description: A synthetic peptide for use as a blocking control in assays to test for specificity of TCR alpha antibody, catalog no. 70R-12400

TCR alpha Blocking Peptide

33R-10580 50 ug
EUR 349
Description: A synthetic peptide for use as a blocking control in assays to test for specificity of TCR alpha antibody, catalog no. 20R-1837

Anti-TCR alpha (4H8)

YF-MA15787 100 ug
EUR 363
Description: Mouse monoclonal to TCR alpha

TCR alpha Blocking Peptide

5648BP-50
EUR 153

Anti-Ms TCR beta Purified

11-571-C100 0.1 mg
EUR 113

TCR beta Antibody (CF-Blue)

20-abx201035
  • EUR 453.00
  • EUR 300.00
  • 100 ug
  • 25 ug

TCR beta Antibody (PerCP-Cy5.5)

20-abx201039
  • EUR 495.00
  • EUR 272.00
  • 100 ug
  • 25 ug

TCR beta (V beta 5.3-related) Antibody

abx140251-01mg 0.1 mg
EUR 398

TCR beta (V beta 5.3-related) Antibody

abx140264-01mg 0.1 mg
EUR 398

Anti-TCR alpha/TRAC Antibody

A05315 100ug/vial
EUR 334

V beta 13.1 TCR antibody (FITC)

61R-1141 25 tests
EUR 235
Description: Mouse monoclonal V beta 13.1 TCR antibody (FITC)

V beta 13.2 TCR antibody (PE)

61R-1349 100 tests
EUR 435
Description: Mouse monoclonal V beta 13.2 TCR antibody (PE)

V beta 10b TCR antibody (PE)

61R-1352 100 ug
EUR 316
Description: Rat monoclonal V beta 10b TCR antibody (PE)

TCR

ABD8621 100 ug
EUR 438

V alpha 2 TCR antibody (FITC)

61R-1145 100 ug
EUR 284
Description: Rat monoclonal V alpha 2 TCR antibody (FITC)

V alpha 2 TCR antibody (PE)

61R-1356 100 ug
EUR 316
Description: Rat monoclonal V alpha 2 TCR antibody (PE)

V alpha 2 TCR antibody (biotin)

61R-1598 100 ug
EUR 208
Description: Rat monoclonal V alpha 2 TCR antibody (biotin)

V alpha 2 TCR antibody (allophycocyanin)

61R-1776 100 ug
EUR 478
Description: Rat monoclonal V alpha 2 TCR antibody (allophycocyanin)

V alpha 24 J alpha 18 TCR antibody

10R-6544 100 ug
EUR 257
Description: Mouse monoclonal V alpha 24 J alpha 18 TCR antibody

TCR beta (V beta 5.3-related) Antibody (Azide free)

abx140265-01mg 0.1 mg
EUR 398

Anti-Ms TCR beta Purified Low Endotoxin

12-571-C100 0.1 mg
EUR 113

V alpha 24 J alpha 18 TCR antibody (PE)

61R-1353 100 tests
EUR 554
Description: Mouse monoclonal V alpha 24 J alpha 18 TCR antibody (PE)

Anti-TCR beta Antibody [H57-597], Unconjugated-100ug

QAB79-100ug 100ug
EUR 141

Anti-TCR beta Antibody [H57-597], APC-100ug

QAB79-APC-100ug 100ug
EUR 216

Anti-TCR beta Antibody [H57-597], APC-25ug

QAB79-APC-25ug 25ug
EUR 131

Anti-TCR beta Antibody [H57-597], FITC-100ug

QAB79-F-100ug 100ug
EUR 131

Anti-TCR beta Antibody [H57-597], FITC-25ug

QAB79-F-25ug 25ug
EUR 115

Anti-TCR beta Antibody [H57-597], FITC-500ug

QAB79-F-500ug 500ug
EUR 225

Anti-TCR beta Antibody [H57-597], PE-100ug

QAB79-PE-100ug 100ug
EUR 216

Anti-TCR beta Antibody [H57-597], PE-25ug

QAB79-PE-25ug 25ug
EUR 123

Anti-TCR beta Antibody [H57-597], V450-100ug

QAB79-V450-100ug 100ug
EUR 284

Anti-TCR beta Antibody [H57-597], V450-25ug

QAB79-V450-25ug 25ug
EUR 166

T-Cell Receptor V Beta 8.5 (TCR V Beta 8.5) Antibody

abx415659-025mg 0.25 mg
EUR 565

T-Cell Receptor V Beta 10 (TCR V Beta 10) Antibody

abx415660-025mg 0.25 mg
EUR 565

Human p73 alpha/beta Control/blocking peptide #1

P73A11-P 100 ug
EUR 164

Rabbit Anti-Human p73 alpha/beta antiserum # 1

P73A11-S 100 ul
EUR 457

Actin (Pan, alpha, beta, gamma) Control/blocking peptide

ACTB22-P 100 ug
EUR 164

Alpha V Beta 5 Integrin, Peptide Aptamer, Biotinylated

AP-301-B 1 mg Ask for price

Alpha V Beta 5 Integrin, Peptide Aptamer, unlabeled

AP-301-U 5 mg Ask for price

Anti-TCR beta Antibody [H57-597], PerCP-Cy5.5-100ug

QAB79-PCP55-100ug 100ug
EUR 276

Anti-TCR beta Antibody [H57-597], PerCP-Cy5.5-25ug

QAB79-PCP55-25ug 25ug
EUR 149

Anti-TCR beta Antibody [H57-597], PE-Cy7-100ug

QAB79-PE7-100ug 100ug
EUR 318

Anti-TCR beta Antibody [H57-597], PE-Cy7-25ug

QAB79-PE7-25ug 25ug
EUR 166

Anti-TCR beta Antibody [H57-597], Qfluor 630-100ug

QAB79-QF630-100ug 100ug
EUR 216

TCR ? Polyclonal Antibody

ES3576-50ul 50ul
EUR 207
Description: A Rabbit Polyclonal antibody against TCR ? from Human. This antibody is tested and validated for WB, ELISA, WB, ELISA

TCR ? Polyclonal Antibody

ES3576-100ul 100ul
EUR 279
Description: A Rabbit Polyclonal antibody against TCR ? from Human. This antibody is tested and validated for WB, ELISA, WB, ELISA

Anti-TCR antibody

STJ16100214 100 µg
EUR 524

TCR β Antibody

45399-100ul 100ul
EUR 252

TCR β Antibody

45399-50ul 50ul
EUR 187

TCR α/β

TCRBABA-100T 100 test
EUR 635

mouse TCR β

MOTCRBA(V100) 100 ug
EUR 50

mouse TCR β

MOTCRBA(V25) 25 ug
EUR 50

mouse TCR β

MOTCRBB(V100) 100 ug
EUR 50

mouse TCR β

MOTCRBB(V25) 25 ug
EUR 50

mouse TCR β

MOTCRBCFB(V100) 100 ug
EUR 50

mouse TCR β

MOTCRBCFB(V25) 25 ug
EUR 50

mouse TCR β

MOTCRBF(V100) 100 ug
EUR 50

mouse TCR β

MOTCRBF(V25) 25 ug
EUR 50

mouse TCR β

MOTCRBF(V500) 500 ug
EUR 50

mouse TCR β

MOTCRBPE(V100) 100 ug
EUR 50

mouse TCR β

MOTCRBPE(V25) 25 ug
EUR 50

mouse TCR β

MOTCRBPP(V100) 100 ug
EUR 50

mouse TCR β

MOTCRBPP(V25) 25 ug
EUR 50

mouse TCR β

MOTCRBPP5.5(V100) 100 ug
EUR 50

mouse TCR β

MOTCRBPP5.5(V25) 25 ug
EUR 50

mouse TCR β

MOTCRBPU(V100) 100 ug
EUR 50

mouse TCR β

MOTCRBPU(V500) 500 ug
EUR 50

TCR antibody (allophycocyanin)

61R-1775 25 ug
EUR 192
Description: Mouse monoclonal TCR antibody (allophycocyanin)

Mouse Monoclonal Anti-Actin (Pan, alpha, beta, gamma)-biotinylated

ACTB24-BTN 50 ul
EUR 408

Alpha V Beta 5 Integrin, Peptide Aptamer, FITC labelled

AP-301-F 1 mg Ask for price

Rabbit Anti-Human p73 alpha/beta IgG # 1, aff pure

P73A11-A 100 ug
EUR 482

Rabbit Anti-Actin (Pan, alpha, beta, gamma) IgG, aff pure

ACTB22-A 100 ug
EUR 482

Anti-Mouse TCR beta Monoclonal Antibody FITC Conjugated, Flow Validated

FC09166-FITC 25 ug, 100ug, 500ug
EUR 91
Description: Hamster Monoclonal Mouse TCR beta Antibody FITC Conjugated, Flow Validated. Validated in Flow Cytometry and tested in Mouse.

Monoclonal Anti-Human/mouse/rat HSP90 alpha/beta IgG, aff pure

HSP901-M 100 ul
EUR 482

Mouse Monoclonal Anti-Actin (Pan, alpha, beta, gamma) IgG-Cy3 conjugate

ACTB24-Cy3 100 ul
EUR 408

Mouse Monoclonal Anti-Actin (Pan, alpha, beta, gamma) IgG-FITC conjugate

ACTB24-FITC 100 ul
EUR 408

Mouse Monoclonal Anti-Actin (Pan, alpha, beta, gamma) IgG, aff pure

ACTB24-M 100 ug
EUR 482

Endothelial intergerin Alpha-V Beta-3 (Clone 17.16), RNA Aptamer, unlabeled

AR-287-U Custom Ask for price

TCR gamma / delta Antibody

abx139895-01mg 0.1 mg
EUR 314

TCR gamma / delta Antibody

abx140353-01mg 0.1 mg
EUR 356

He strongly inspired younger reproductive biologists who labored in his laboratory, and applauded the world-wide distinction of his scholar and affiliate, R. Yanagimachi, as a specialist in mammalian fertilisation. Finally, Chang’s continued emotions in the direction of his homeland are contrasted with the actuality of his American life after 1945, itself a examine in poignancy.