Merck
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A6917

Sigma-Aldrich

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
MDL number:

biological source

rabbit

Quality Level

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

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General description

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.
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.

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.

Pictograms

Exclamation mark

Signal Word

Warning

Hazard 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

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

Enter Lot Number to search for Certificate of Origin (COO).

The Immunoglobulins: Structure and Function, 575-586 (1998)
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.
Margot Camoin et al.
BioMed research international, 2019, 2964639-2964639 (2019-12-31)
Surra, caused by Trypanosoma evansi, is a widely distributed animal trypanosomosis; it affects both domestic and wild mammals with high economic impact. Clinical picture is moderate in bovines but severe in equids. Surra is also an important constraint for international
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
Molecular Genetics of Immunoglobulin, 17, 575-586 (1987)

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