A6063
Anti-Horse IgG (whole molecule)−Alkaline Phosphatase antibody produced in rabbit
affinity isolated antibody, buffered aqueous glycerol solution
Synonyme(s) :
Rabbit Anti-Horse IgG (whole molecule)−AP
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About This Item
Produits recommandés
Source biologique
rabbit
Conjugué
alkaline phosphatase conjugate
Forme d'anticorps
affinity isolated antibody
Type de produit anticorps
secondary antibodies
Clone
polyclonal
Forme
buffered aqueous glycerol solution
Technique(s)
direct ELISA: 1:30,000
western blot: 1:30,000
Conditions d'expédition
wet ice
Température de stockage
2-8°C
Modification post-traductionnelle de la cible
unmodified
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Catégories apparentées
Description générale
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.
Immunogène
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.
Actions biochimiques/physiologiques
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.
Forme physique
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
Clause de non-responsabilité
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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Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Les clients ont également consulté
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)
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
Noah D Cohen et al.
PloS one, 15(10), e0240479-e0240479 (2020-10-16)
Strangles is a common disease of horses with worldwide distribution caused by the bacterium Streptococcus equi subspecies equi (SEE). Although vaccines against strangles are available commercially, these products have limitations in safety and efficacy. The microbial surface antigen β 1→6
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
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