A6063
Anti-Horse IgG (whole molecule)−Alkaline Phosphatase antibody produced in rabbit
affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Rabbit Anti-Horse IgG (whole molecule)−AP
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About This Item
Recommended Products
biological source
rabbit
conjugate
alkaline phosphatase conjugate
antibody form
affinity isolated antibody
antibody product type
secondary antibodies
clone
polyclonal
form
buffered aqueous glycerol solution
technique(s)
direct ELISA: 1:30,000
western blot: 1:30,000
shipped in
wet ice
storage temp.
2-8°C
target post-translational modification
unmodified
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General description
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.
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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
Pyankov OV, et al.
Scientific Reports, 7(3), 41537-41537 (2017)
Line P Lauridsen et al.
Journal of proteomics, 136, 248-261 (2016-02-16)
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
D Tortorella et al.
The Journal of biological chemistry, 270(46), 27439-27445 (1995-11-17)
Diphtheria toxin is a bacterial protein that undergoes a physiologically critical conformational change at low pH. This change involves a partial unfolding event forming a molten globule-like structure, which exposes hydrophobic regions and which allows the toxin to insert into
Andreas H Laustsen et al.
Toxicon : official journal of the International Society on Toxinology, 107(Pt B), 187-196 (2015-07-15)
Four specimens of the olive sea snake, Aipysurus laevis, were collected off the coast of Western Australia, and the venom proteome was characterized and quantitatively estimated by RP-HPLC, SDS-PAGE, and MALDI-TOF-TOF analyses. A. laevis venom is remarkably simple and consists
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