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SAB3701275

Sigma-Aldrich

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

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Human IgG

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

concentration

3.0 mg/mL

technique(s)

immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

General description

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.

Specificity

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.

Immunogen

Human IgG F(c) fragment

Application

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

Physical properties

Antibody format: IgG

Physical form

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

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.

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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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