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SAB3701173

Sigma-Aldrich

Anti-Mouse IgG1 (γ-chain specific)-Biotin antibody produced in rabbit

affinity isolated antibody, lyophilized powder

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

conjugate

biotin conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

lyophilized powder

species reactivity

mouse

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 and is a widely expressed serum antibody. It 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. 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. 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. IgG1 is induced due to antibody responses to membrane proteins and soluble protein antigens. It is the most abundant subclass of IgG.

Specificity

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.

Immunogen

Mouse IgG1 heavy chain

Physical properties

Antibody format: IgG

Physical form

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).

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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Danger

Hazard Classifications

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

supp_hazards

Storage Class

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

wgk_germany

WGK 3

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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Kirk J Wangensteen et al.
Hepatology (Baltimore, Md.), 68(2), 663-676 (2017-11-02)
Clustered regularly interspaced short palindromic repeats (CRISPR)/CRISPR-associated 9 activation (CRISPRa) systems have enabled genetic screens in cultured cell lines to discover and characterize drivers and inhibitors of cancer cell growth. We adapted this system for use in vivo to assess
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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