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Key Documents

SAB3701180

Sigma-Aldrich

Anti-Mouse IgG2a (γ-chain specific)-Biotin antibody produced in rabbit

affinity isolated antibody, lyophilized powder

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

rabbit

Conjugué

biotin conjugate

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

secondary antibodies

Clone

polyclonal

Forme

lyophilized powder

Espèces réactives

mouse

Technique(s)

immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

Catégories apparentées

Description générale

Immunoglobulin G (IgG) consists of a γ heavy chain in the constant (C) region. The monomeric 150kDa structure of IgG constitutes two identical heavy chains and two identical light chains with molecular weight of 50kDa and 25kDa, respectively. It belongs to the immunoglobulin family and is a widely expressed serum antibody. Disulfide bonds link the two heavy chains, the heavy and light chains and also links residues inside the chains. Maternal IgG is the only antibody transported across the placenta to the fetus. It passively immunizes the infants. IgG is further subdivided into four classes namely, IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, respectively. IgG2 is involved in immune responses to bacterial capsular polysaccharide antigens. Its deficiency has been linked to an increased susceptibility to bacterial infections.

Spécificité

This product was prepared from monospecific antiserum by immunoaffinity chromatography using Mouse antigens coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Biotin, Anti-Rabbit Serum, Mouse IgG and Mouse Serum. Specificity was confirmed by ELISA. Typically less than 1% cross reactivity was observed against other Mouse heavy chain isotypes.

Immunogène

Mouse IgG2a heavy chain

Propriétés physiques

Antibody format: IgG

Forme physique

Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 10 mg/mL Bovine Serum Albumin (BSA) - Immunoglobulin and Protease free

Reconstitution

Reconstitute with 1.0 mL deionized water (or equivalent).

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

Skull and crossbonesEnvironment

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

Acute Tox. 3 Dermal - Acute Tox. 4 Oral - Aquatic Chronic 2

Risques supp

Code de la classe de stockage

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

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)

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

Human placental Fc receptors and the transmission of antibodies from mother to fetus.
Simister NE and Story CM
Journal of Reproductive Immunology, 37(1), 1-23 (1997)
Gestur Vidarsson et al.
Frontiers in immunology, 5, 520-520 (2014-11-05)
Of the five immunoglobulin isotypes, immunoglobulin G (IgG) is most abundant in human serum. The four subclasses, IgG1, IgG2, IgG3, and IgG4, which are highly conserved, differ in their constant region, particularly in their hinges and upper CH2 domains. These
Antibody structure, instability, and formulation.
Wang W
Journal of Pharmaceutical Sciences, 96(1), 1-26 (2007)

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