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Key Documents

A6917

Sigma-Aldrich

Anti-Horse IgG (whole molecule)−Peroxidase antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Rabbit Anti-Horse IgG (whole molecule)−HRP

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

rabbit

Niveau de qualité

Conjugué

peroxidase conjugate

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

secondary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Technique(s)

direct ELISA: 1:10,000

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

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Description générale

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.

Immunogène

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)

Actions biochimiques/physiologiques

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.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4 containing 1% bovine serum albumin and 0.05% MIT

Notes préparatoires

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).

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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Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Skin Sens. 1

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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.
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.
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
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

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