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A5403

Sigma-Aldrich

Anti-Human IgG (γ-chain specific), F(ab′)2 fragment−Alkaline Phosphatase antibody produced in goat

affinity isolated antibody, buffered aqueous solution

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About This Item

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

biological source

goat

conjugate

alkaline phosphatase conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

technique(s)

direct ELISA: 1:1,000

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

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General description

Human IgG antibodies are primarily responsible for the facilitation of humoral immune responses such as placental transport, complement fixation and phagocytosis among many others. The antigen binding is mediated by the variable Fab region of IgG antibodies, whereas the effector activities are stimulated by the Fc domain , . Anti-human IgG (γ-chain specific), F(ab′)2 fragment-alkaline phosphatase antibody can be used in ELISA for measuring anticardiolipin antibodies. Goat anti-human IgG (γ-chain specific), F(ab′)2 fragment-alkaline phosphatase antibody reacts specifically with human IgG.

Immunogen

Purified human IgG.

Application

Serum IgGs against HHV-6 or HHV-7 were detected by Elisa using alkaline phosphatase conjugated goat anti-human IgG F′ab specific at a concentration of 1:1000 diluted in PBS/0.05% skim milk. The antibody was incubated on plates for 2 hours at 37 degrees.
Transfected SN56 neuronal cell lysates were ran on a SDS page gel for western blot analysis using alkaline phosphatase conjugated goat anti-human IgG Fab specific as the secondary antibody.

Physical form

Solution in 0.05 M Tris, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2 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 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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K Underwood et al.
The Journal of infectious diseases, 168(6), 1436-1443 (1993-12-01)
Actinobacillus actinomycetemcomitans is frequently associated with severe periodontitis. Many periodontitis patients have elevated levels of serum IgG antibodies to A. actinomycetemcomitans, but the role of these antibodies is unknown. This study evaluated the functional capacity of anti-A. actinomycetemcomitans IgG antibody
G A Burghen et al.
Diabetes, 38 Suppl 1, 129-132 (1989-01-01)
More efficient methods of islet isolation must be developed for islet transplantation to become clinically routine. During collagenase dispersal of human pancreas, an amorphous, viscous, gellike material often develops and entraps large numbers of islets, thereby reducing the yield. When
Joshua D Ooi et al.
Nature communications, 10(1), 3392-3392 (2019-07-31)
Autoreactivity to myeloperoxidase (MPO) causes anti-neutrophil cytoplasmic antibody (ANCA)-associated vasculitis (AAV), with rapidly progressive glomerulonephritis. Here, we show that a Staphylococcus aureus peptide, homologous to an immunodominant MPO T-cell epitope (MPO409-428), can induce anti-MPO autoimmunity. The peptide (6PGD391-410) is part
Robert M Anthony et al.
Journal of clinical immunology, 30 Suppl 1, S9-14 (2010-05-19)
IgG antibodies have long been recognized as proinflammatory mediators of the humoral immune response. Antibodies bind and neutralize antigens to promote antibody-dependent cytotoxicity, opsonization of antigens, and the initiation of phagocytosis. Whereas the antigen specificity of antibodies is determined by
Ana Cristina Magalhães et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 25(21), 5207-5216 (2005-05-27)
Invasion of the nervous system and neuronal spread of infection are critical, but poorly understood, steps in the pathogenesis of transmissible spongiform encephalopathies or prion diseases. To characterize pathways for the uptake and intraneuronal trafficking of infectious, protease-resistant prion protein

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