Affinity isolated antibody is obtained from rabbit antiserum by immunospecific purification, which removes essentially all rabbit serum proteins, including immunoglobulins, which do not specifically bind to horse IgG. The horse IgG is present majorly in the serum, mucoasal surface, urinary tract, lungs and colostrum.
Horse IgGs have seven subclasses ranging from IgG1 to IgG7. Equine IgG antibodies mainly regulate mucosal and systemic immunological responses and thereby, provide protection against disease-causing pathogens such as Streptococcus equi., and the horse flu virus. Horse IgG may also function to control the advancement of EHV-1 infection . Anti-Horse IgG (whole molecule)-Alkaline Phosphatase antibody is specific for IgG in horses.
Immunogen
Horse IgG
Application
Anti-Horse IgG (whole molecule)-Alkaline Phosphatase antibody is suitable for use in direct ELISA (1:30,000) and western blot (1:30,000).
Anti-Horse IgG (whole molecule)-Alkaline Phosphatase antibody produced in rabbit has been used in indirect enzyme-linked immunosorbent assay (ELISA).
Binding of horse anti-diphtheria toxin IgG was analyzed by ELISA using alkaline phosphatase-conjugated rabbit anti-horse IgG.
Biochem/physiol Actions
The equine IgG subclasses elicit a strong respiratory burst by interacting with the interact with FcγR receptor peripheral blood leukocytes and with the Fc receptors on effector cells. It is useful as a monoclonal antibody in treating non-human primates (NHPs) infected with Ebola virus. It is used as a component in commercial equine IgG test called the SNAP Foal IgG test kit, for the diagnosis of failure of transfer of passive immunity (FTPI) in foals.
Physical form
Solution in 0.05 M Tris buffer, pH 8.0, containing 1 mM MgCl2, 10 mM glycine, 1% bovine serum albumin, 50% glycerol and 15 mM sodium azide
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
A toxicovenomic analysis of the venom of the forest cobra, N. melanoleuca, was performed, revealing the presence of a total of 52 proteins by proteomics analysis. The most abundant proteins belong to the three-finger toxins (3FTx) (57.1wt%), which includes post-synaptically
Seroprevalence of Toxoplasma gondii and Trichinella spiralis in Horses in Xinjiang, Northwestern China
Xing H, et al.
Journal of equine veterinary science, 60, 11-15 (2018)
Successful post-exposure prophylaxis of Ebola infected non-human primates using Ebola glycoprotein-specific equine IgG
A toxicovenomic study was performed on the venom of the green mamba, Dendroaspis angusticeps. Forty-two different proteins were identified in the venom of D. angusticeps, in addition to the nucleoside adenosine. The most abundant proteins belong to the three-finger toxin
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