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Key Documents

B1140

Sigma-Aldrich

Anti-Human IgG (γ-chain specific)-Biotin antibody produced in goat

affinity isolated antibody, buffered aqueous solution

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About This Item

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

biological source

goat

Quality Level

conjugate

biotin conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

technique(s)

direct ELISA: 1:20,000

storage temp.

2-8°C

target post-translational modification

unmodified

General description

Human IgG antibodies are primarily responsible for the facilitation of humoral immune responses such as complement fixation, placental transport, and phagocytosis among many others. Anti-human IgG (γ-chain specific)-biotin antibody can be used in preparation of the double-codified gold nanoparticle label. Goat anti- human IgG (γ-chain specific)-biotin antibody reacts specifically with human IgG but not with other immunoglobulins.
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)-Biotin antibody is specific for human IgG and does not bind other human immunoglobulins.

Immunogen

Purified human IgG.

Application

Anti-Human IgG (γ-chain specific)-Biotin antibody is suitable for use in ELISA (1:2000) and double-codified gold nanolabel-based immunoanalysis.
Anti-human IgG (γ-chain specific)-biotin antibody can be used in direct ELISA

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 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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Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Eliana Ferreira Monteiro et al.
Pathogens (Basel, Switzerland), 10(9) (2021-09-29)
Plasmodium malariae has a wide geographic distribution, but mainly at very low parasitemias and in co-infections, leading to an underestimated prevalence of this species. Studies for the detection of antibodies against Plasmodium recombinant proteins are increasingly used to map geographical
Alina Sultanova et al.
Microbiology spectrum, 10(3), e0236921-e0236921 (2022-05-24)
Human herpesvirus-6 (HHV-6) contains two genes (U12 and U51) that encode putative homologues of human G-protein-coupled receptors like CCR1, CCR3, and CCR5. It has been shown that these viral proteins can be expressed on the surface of epithelial and some
Adriano Ambrosi et al.
Analytical chemistry, 79(14), 5232-5240 (2007-06-21)
A novel double-codified nanolabel (DC-AuNP) based on gold nanoparticle (AuNP) modified with anti-human IgG peroxidase (HRP)-conjugated antibody is reported. It represents a simple assay that allows enhanced spectrophotometric and electrochemical detection of antigen human IgG as a model protein. The
Robert S Matson et al.
Methods in molecular biology (Clifton, N.J.), 382, 273-286 (2008-01-29)
The ability to perform microarray-based immunoassays without the need for wells or other fluid barriers were demonstrated. Both contact and noncontact microarray printing technology is used to prepare spotted arrays of analyte binding sites, as well as, to deliver samples
Wanwisa Dejnirattisai et al.
Nature immunology, 16(2), 170-177 (2014-12-17)
Dengue is a rapidly emerging, mosquito-borne viral infection, with an estimated 400 million infections occurring annually. To gain insight into dengue immunity, we characterized 145 human monoclonal antibodies (mAbs) and identified a previously unknown epitope, the envelope dimer epitope (EDE)

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