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A8419

Sigma-Aldrich

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

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Goat Anti-Human IgG (gamma-chain specific) HRP

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.77

biological source

goat

Quality Level

conjugate

peroxidase conjugate

antibody form

IgG fraction of antiserum

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

technique(s)

direct ELISA: 1:40,000
dot blot: 1:100,000 (chemiluminescent)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:100

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

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General description

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 . The specificity of Anti-Human IgG (γ-chain specific)-Peroxidase antibody is determined by immunoelectrophoresis and Ouchterlony Double Diffusion techniques. This antibody is specific for for human IgG when tested against purified human IgA, IgG, IgM, Bence Jones κ and Bence Jones lambda myeloma proteins.
Immunoglobulin G (IgG) belongs to the immunoglobulin family and is a widely expressed serum antibody. IgG is usually found as a monomer. IgG antibody subtype is the most abundant of serum immunoglobulins of the immune system. About 70 % of the total immunoglobulin consists of IgG.

Specificity

This antibody is specific for for human IgG when tested against purified human IgA, IgG, IgM, Bence Jones κ and Bence Jones lambda myeloma proteins.

Immunogen

Human IgG

Application

Anti-Human IgG (γ-chain specific) Peroxidase antibody produced in goat has been used in enzyme-linked immunosorbent assay (ELISA) and western blot.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
IgM concentration in sera from patients with chronic CA syndrome was determined by ELISA using HRP-conjugated goat anti-human (mu chain specific) as the secondary antibody.

Biochem/physiol Actions

Immunoglobulin G (IgG) mainly participates in hypersensitivity type II and type III.

Physical form

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 0.05% MIT

Preparation Note

Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).

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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Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

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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Qingbo Liu et al.
Journal of virology, 95(12) (2021-04-09)
Broadly neutralizing antibodies (bNAbs) are the focus of increasing interest for human immunodeficiency virus type 1 (HIV-1) prevention and treatment. Although several bNAbs are already under clinical evaluation, the development of antibodies with even greater potency and breadth remains a
Qingbo Liu et al.
Nature communications, 10(1), 721-721 (2019-02-15)
Broadly neutralizing antibodies (bNAbs) represent a promising alternative to antiretroviral drugs for HIV-1 prevention and treatment. Selected antibodies to the CD4-binding site bolster envelope trimer binding via quaternary contacts. Here, we rationally engraft a new paratope, i.e., the extended heavy-chain
An accessory protease inhibitor to increase the yield and quality of a tumour-targeting mAb in Nicotiana benthamiana leaves
Jutras PV, et al.
Testing, 11(11), e0167086-e0167086 (2016)
Heriberto Caballero-Ortega et al.
Journal of infection in developing countries, 8(5), 642-647 (2014-05-14)
There are few articles on evaluation of Toxoplasma gondii serological tests. Besides, commercially available tests are not always useful and are expensive for studies in open population. The aim of this study was to evaluate in-house ELISA and western blot
Philippe V Jutras et al.
PloS one, 11(11), e0167086-e0167086 (2016-11-29)
The overall quality of recombinant IgG antibodies in plants is dramatically compromised by host endogenous proteases. Different approaches have been developed to reduce the impact of endogenous proteolysis on IgGs, notably involving site-directed mutagenesis to eliminate protease-susceptible sites or the

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