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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

Código UNSPSC:
12352203
NACRES:
NA.46

origen biológico

rabbit

conjugado

biotin conjugate

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

secondary antibodies

clon

polyclonal

formulario

lyophilized powder

reactividad de especies

mouse

técnicas

immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable

Condiciones de envío

wet ice

temp. de almacenamiento

2-8°C

modificación del objetivo postraduccional

unmodified

Categorías relacionadas

Descripción general

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.

Especificidad

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.

Inmunógeno

Mouse IgG2a heavy chain

Propiedades físicas

Antibody format: IgG

Forma física

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

Reconstitución

Reconstitute with 1.0 mL deionized water (or equivalent).

Cláusula de descargo de responsabilidad

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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Pictogramas

Skull and crossbonesEnvironment

Palabra de señalización

Danger

Frases de peligro

Clasificaciones de peligro

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

Riesgos supl.

Código de clase de almacenamiento

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

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

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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