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Key Documents

I1886

Sigma-Aldrich

Anti-Human IgG (whole molecule) antibody produced in goat

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-Human IgG, Goat Anti-Human IgG

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About This Item

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

biological source

goat

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

technique(s)

indirect ELISA: 1:10,000
quantitative precipitin assay: 3.0 mg/mL

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 . Anti-human IgG (whole molecule) antibody is specific for human IgG when tested against normal human serum and IgG by immunoelectrophoresis. The antibody also reacts with light chains. Immunoglobulin G (IgG) is part of the immunoglobulin family and is a widely expressed serum antibody. It consists of a γ heavy chain in the constant (C) region. The primary structure of this antibody contains disulfide bonds involved in linking the two heavy chains, linking the heavy and light chains and also resides inside the chains.

Immunogen

Human IgG

Application

Anti-Human IgG (whole molecule) antibody is suitable for use in quantitative precipitin assay (3.0 mg/mL).
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide as preservative

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

nwg

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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Tuerhongjiang Tuxun et al.
Scientific reports, 8(1), 4417-4417 (2018-03-15)
Fluorodeoxyglucose (FDG) uptake by alveolar echinococcosis (AE) liver lesions is a signal of their metabolic activity and of disease progression. In order to find a surrogate marker for this status, we investigated whether parameters of the peripheral and/or periparasitic immune
Laura E M Dunn et al.
Journal of virology, 97(2), e0189422-e0189422 (2023-02-07)
The ability of Epstein-Barr virus (EBV) to switch between latent and lytic infection is key to its long-term persistence, yet the molecular mechanisms behind this switch remain unclear. To investigate transcriptional events during the latent-to-lytic switch, we utilized Precision nuclear
Steffen Preissler et al.
eLife, 4, e08961-e08961 (2015-10-17)
DnaK/Hsp70 chaperones form oligomers of poorly understood structure and functional significance. Site-specific proteolysis and crosslinking were used to probe the architecture of oligomers formed by the endoplasmic reticulum (ER) Hsp70, BiP. These were found to consist of adjacent protomers engaging
Lorenzo Russo et al.
Nanoscale, 11(22), 10819-10827 (2019-05-29)
Myxovirus protein A (MxA) is a biomarker that can be used to distinguish between viral and bacterial infections. While MxA lateral flow assays (LFAs) have been successfully used for viral vs. bacterial differential diagnosis for children, the clinically relevant level
Yakov A Lomakin et al.
Communications biology, 7(1), 842-842 (2024-07-11)
Identifying high-affinity antibodies in human serum is challenging due to extremely low number of circulating B cells specific to the desired antigens. Delays caused by a lack of information on the immunogenic proteins of viral origin hamper the development of

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