A6917
Anti-Horse IgG (whole molecule)−Peroxidase antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Rabbit Anti-Horse IgG (whole molecule)−HRP
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
biological source
rabbit
conjugate
peroxidase conjugate
antibody form
affinity isolated antibody
antibody product type
secondary antibodies
clone
polyclonal
form
buffered aqueous solution
technique(s)
direct ELISA: 1:10,000
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Looking for similar products? Visit Product Comparison Guide
Related Categories
General description
An immunoglobulin has two heavy chain and two light chain connected by disulfide bond. It mainly helps in immune defense. It is a glycoprotein. IgG is a major class of immunoglobulin. Horse IgG has different subclasses, IgG2a, IgG2b, IgG2c, IgG1 and IgG(T). Compared to other IgG molecules, IgG(T) has more carbohydrate content. In healthy individuals, total IgG is dispersed equally between circulating plasma and interstitial fluids.
Horse IgG is a plasma B cell derived antibody isotype defined by its heavy chain. IgG is the most abundant antibody isotype found in horse serum. IgG crosses the placental barrier, is a complement activator and binds to the Fc-receptors on phagocytic cells. The level of IgG may vary with the status of disease or infection.
Immunogen
Purified horse IgG
Application
Anti-Horse IgG (whole molecule)-Peroxidase antibody produced in rabbit has been used in:
- enzyme-linked immunosorbent assay (ELISA)
- HeV soluble G
- indirect ELISA (HeVsG iELISA)
Biochem/physiol Actions
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 .
Immunoglobulin G (IgG) participates in hypersensitivity type II and type III.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4 containing 1% bovine serum albumin and 0.05% MIT
Preparation Note
Prepared using the periodate method described by Wilson, M.B., and Nakane, P.K., in Immunofluorescence and Related Staining Techniques, Elsevier/North Holland Biomedical Press, Amsterdam, p215 (1978).
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.
Not finding the right product?
Try our Product Selector Tool.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Skin Sens. 1
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Natacha Ferreira de Oliveira et al.
Toxins, 14(10) (2022-10-27)
Viperidae snakes are the most important agents of snakebites in Brazil. The protein composition of snake venoms has been frequently analyzed by means of electrophoretic techniques, but the interaction of proteins in venoms has barely been addressed. An electrophoretic technique
Eliane Cristina de Freitas et al.
Microbiology (Reading, England), 165(3), 355-365 (2019-01-29)
Upstream open reading frames (ORFs) are frequently found in the 5'-flanking regions of genes and may have a regulatory role in gene expression. A small ORF (named cohL here) was identified upstream from the copAB copper operon in Xanthomonascitri subsp.
Caio B Abreu et al.
Frontiers in immunology, 11, 2011-2011 (2020-09-26)
Scorpionism is responsible for most accidents involving venomous animals in Brazil, which leads to severe symptoms that can evolve to death. Scorpion venoms consist of complexes cocktails, including peptides, proteins, and non-protein compounds, making separation and purification procedures extremely difficult
Isadora Sousa de Oliveira et al.
The journal of venomous animals and toxins including tropical diseases, 24, 34-34 (2018-12-12)
Our group has previously performed a proteomic study verifying that individual variations can occur among Crotalus durissus collilineatus venoms. These variations may lead to differences in venom toxicity and may result in lack of neutralization of some components by antivenom.
Giordanni C Dantas et al.
Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 47(2), 518-526 (2016-03-19)
Citrus canker, caused by the Gram-negative bacterium Xanthomonas citri subsp. citri (Xac), is one of the most devastating diseases to affect citrus crops. There is no treatment for citrus canker; effective control against the spread of Xac is usually achieved
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service