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SAB3701275

Sigma-Aldrich

Anti-Human IgG (Fc specific) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinónimos:

Anti-Human IgG

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.46

origen biológico

rabbit

conjugado

unconjugated

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

secondary antibodies

clon

polyclonal

Formulario

buffered aqueous solution

reactividad de especies

human

concentración

3.0 mg/mL

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

Descripción general

Immunoglobulin G (IgG) belongs to the immunoglobulin family. It is widely expressed and consists of a gamma (γ) heavy chain in the constant (C) region. IgG is a monomer with a molecular weight of about 150 kDa. The structure of IgG constitutes two identical heavy chains and two identical light chains with molecular weight of 50 kDa and 25 kDa respectively. The primary structure of this antibody also contains disulfide bonds involved in linking the two heavy chains, linking the heavy and light chains and resides inside the chains. IgG is further subdivided into four classes namely, IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, respectively. Limited digestion using papain cleaves the antibody into three fragments, two of which are identical and contain the antigen-binding activity. The third fragment does not possess antigen-binding activity and is known as fragment crystallizable (Fc). It interacts with cells and effector molecules. The Fc fragment contains the CH2 and CH3 domains of the antibody molecule. Maternal IgG is the only antibody transported across the placenta to the fetus. It passively immunizes the infants.

Especificidad

This product was prepared from monospecific antiserum by immunoaffinity chromatography using Human IgG 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-Rabbit Serum, Human IgG, Human IgG F(c) and Human Serum. No reaction was observed against Human IgG F(ab′)2.

Inmunógeno

Human IgG F(c) fragment

Aplicación

Anti-Human IgG (Fc specific) antibody produced in rabbit has been used as a control in cysteine-rich angiogenic inducer 61 (CYR61) blocking experiment.

Propiedades físicas

Antibody format: IgG

Forma física

Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2

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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Código de clase de almacenamiento

10 - Combustible liquids

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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The structure of a typical antibody molecule
Immunobiology: The Immune System in Health and Disease (2001)
The matricellular protein CYR61 promotes breast cancer lung metastasis by facilitating tumor cell extravasation and suppressing anoikis
Yu-Ting H et al.
Oncotarget, 8(6), 9200-9200 (2017)
Yu-Ting Huang et al.
Oncotarget, 8(6), 9200-9215 (2016-12-03)
Matricellular proteins play multiple roles in primary tumor growth, local invasion and tumor angiogenesis. However, their contribution to metastasis and the putative mechanisms involved are less well characterized. In ER-negative human breast cancer, elevated expression levels of the matricellular protein
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)
Antibody structure, instability, and formulation.
Wang W
Journal of Pharmaceutical Sciences, 96(1), 1-26 (2007)

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