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A3688

Sigma-Aldrich

Anti-Mouse IgG (whole molecule)−Alkaline Phosphatase antibody produced in goat

affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Goat Anti-Mouse IgG (whole molecule)−AP

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About This Item

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

biological source

goat

conjugate

alkaline phosphatase conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

mouse

should not react with

human

technique(s)

direct ELISA: 1:30,000
dot blot: 1:30,000
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50
western blot: 1:30,000

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

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General description

Immunoglobulin G (IgG) is a glycoprotein antibody that regulates immune responses such as phagocytosis and is also involved in the development of autoimmune diseases. Mouse IgGs have four distinct isotypes, namely, IgG1, IgG2a, IgG2b, and IgG3. IgG1 regulates complement fixation in mice.
Goat Anti-Mouse IgG (whole molecule)-Alkaline Phosphatase antibody react with normal mouse serum and mouse IgG using IEP. By ODD, the antiserum is reacts with mouse IgG1, IgG2a, IgG2b, IgG3, IgA and IgM. The conjugate shows no reactivity with human serum proteins by ELISA.

Immunogen

purified mouse IgG

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Goat Anti-Mouse IgG (whole molecule)-Alkaline Phosphatase antibody for immunocytochemistry assays and ELISA.
Human and Murine tumor cell lysate were analyzed for various protein expression by western blot using alkaline phosphatase conjugated goat anti-mouse IgG as the secondary for 1 hour at 37 degrees.
Surfactant Protein A was detected in bronchoalveolar fluid using alkaline phosphatase conjugated goat anti-mouse IgG as the secondary at μg/ml in TBS/Tween containing final concentration of 0.5M NaCl.

Other Notes

Antibody adsorbed with human serum proteins.

Physical form

Solution in 0.05 M Tris, pH 8.0, containing 1% bovine serum albumin, 10 mM glycine, 1 mM MgCl2, 50% glycerol and 15 mM sodium azide.

Preparation Note

Adsorbed to reduce background with human samples.

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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Catharina E Dam et al.
Scandinavian journal of clinical and laboratory investigation, 74(6), 506-514 (2014-05-06)
Knowledge about antibody-antigen interactions is important for the understanding of the immune system mechanisms and for supporting development of drugs and biomarkers. A tool for identification of these antigenic epitopes of specific antibodies is epitope mapping. In this study, a
Alberta Bergamo et al.
The Journal of pharmacology and experimental therapeutics, 305(2), 725-732 (2003-02-28)
We have examined the biological and antitumor activity of a series of dinuclear ruthenium complexes. The aim of this study was to compare the in vitro effects of these new compounds on cell proliferation, cell distribution among cell cycle phases
Zahir Ali et al.
ACS synthetic biology, 11(1), 406-419 (2021-12-24)
Simple, rapid, specific, and sensitive point-of-care detection methods are needed to contain the spread of SARS-CoV-2. CRISPR/Cas9-based lateral flow assays are emerging as a powerful alternative for COVID-19 diagnostics. Here, we developed Bio-SCAN (biotin-coupled specific CRISPR-based assay for nucleic acid
J P Donahue et al.
Proceedings of the National Academy of Sciences of the United States of America, 91(25), 12178-12182 (1994-12-06)
We have developed a method for crystallizing small functional protein segments so that their three-dimensional structure can be determined by x-ray diffraction analysis. This method consists of linking a small protein segment of unknown tertiary structure to either the amino
Sandra Alejandra Serna-Salas et al.
BioMed research international, 2018, 4706976-4706976 (2019-01-16)
Regulation of the mechanisms of fibrosis is an important goal in the treatment of liver cirrhosis. One mechanism is the participation of hepatic stellate cells in fibrogenesis when activated by catecholamines. Consequently, α/β adrenoblockers are proposed as an alternative treatment

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