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.

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

  • 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

1 mg 537 EUR

Hemoglobin Antibody

1 mg 537 EUR

Hemoglobin antibody

100 ul 393 EUR

Hemoglobin antibody

1 mg 343 EUR

Hemoglobin antibody

1 mg 30 EUR