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P9170

Sigma-Aldrich

Anti-Human IgG (γ-chain specific)−R-Phycoerythrin antibody produced in goat

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Goat Anti-Human IgG (γ-chain specific)−R-PE

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

goat

Quality Level

conjugate

phycoerythrin (R-PE) conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

technique(s)

direct immunofluorescence: 1:16

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

Related Categories

General description

Affinity isolated antigen specific antibody is obtained from goat anti-human IgG antiserum by immunospecific purification which removes essentially all goat serum proteins, including immunoglobulins, which do not specifically bind to the γ-chain of human IgG. Goat anti-human IgG is conjugated to Sigma R-Phycoerythrin (Product No. P8912) by a modification of the method of Kronick Unbound phycoerythrin is removed by gel filtration chromatography
Specificity for the γ-chain of human IgG is determined by Ouchterlony Double Diffusion (ODD). The antibody preparation is specific for human IgG when tested against purified human IgA, IgG, IgM, Bence Jones κ and Bence Jones Lambda myeloma proteins, prior to conjugation
Identity and purity of the antibody is established by immunoelectrophoresis (IEP), prior to conjugation Electrophoresis of the antibody preparation followed by diffusion versus anti-goat IgG and anti-goat whole serum results in single arcs of precipitation.
Human IgGs are glycoprotein antibodies that contain two equivalent light chains and a pair of identical heavy chains. IgGs have four distinct isoforms, ranging from IgG1 to IgG4. These antibodies regulate immunological responses to allergy and pathogenic infections. IgGs have also been implicated in complement fixation and autoimmune disorders
Anti-Human IgG (γ-chain specific)-R-Phycoerythrin antibody is specific for human IgG when tested against purified human IgA, IgG, IgM, and Bence Jones κ and λ myeloma proteins.
Immunoglobulin G (IgG) belongs to the immunoglobulin family and is a widely expressed serum antibody. It consists of a gamma (γ) heavy chain in the constant (C) region. The primary structure of the antibody contains disulfide bonds involved in linking the two heavy chains, linking the heavy and light chains and also resides inside the chains.

Immunogen

Developed in goat using purified human IgG as the immunogen.
Purified human IgG

Application

A minimum 1:16 dilution is required for direct immunofluorescent labelling of human peripheral blood lymphocytes. The antibody may be used in fluorescence-activated cell sorting applications.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.1 mM EDTA, 1 mM iodoacetamide, 1% bovine serum albumin and 15 mM sodium azide

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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WGK 1

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Not applicable

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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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We have previously shown that bivalent human gamma1 CD3 monoclonal antibody (mAb) is ineffective at mediating lysis of human T cells with human complement. In this paper we have used genetic engineering and sulfur chemistry to prepare 2 types of
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IgG has a long half-life through engagement of its Fc region with the neonatal Fc receptor (FcRn). The FcRn binding site on IgG1 has been shown to contain I253 and H310 in the CH2 domain and H435 in the CH3
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M N Kronick
Journal of immunological methods, 92(1), 1-13 (1986-08-21)

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