A3275
Anti-Human IgM (μ-chain specific)−Alkaline Phosphatase antibody produced in goat
affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Goat Anti-Human IgM (μ-chain specific)−AP
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About This Item
Recommended Products
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
human
technique(s)
direct ELISA: 1:7,000-1:21,000
shipped in
wet ice
storage temp.
2-8°C
target post-translational modification
unmodified
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General description
IgM antibody is produced by B cells and has pentamer structure which helps the antibody in polyreactivity and can also remove apoptotic cells. Anti-human IgM (μ-chain specific) -alkaline phosphatase antibody can be used in solid phase ELISA for determination of anti-sp75 antibodies. Goat anti human IgM-alkaline phosphatase antibody reacts specifically with human IgM.
Immunogen
Human IgM.
Application
IgM is a glycoprotein with 5 n-linked glycosylation sites on the heavy chain. An ELISA assay was performed to identify glycosylated forms of IgM that bind to lectin. Alkaline phosphatase conjugated goat anti-human IgM was used as the secondary at 1:2000 and developed using p-nitrophenyl substrate (Sigma).
It may be used for immunoblotting.
Physical form
Solution in 0.05 M Tris, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2, 15 mM sodium azide and 50% glycerol
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 Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Mandar Patgaonkar et al.
Parasite immunology, 40(10), e12580-e12580 (2018-08-14)
B cell-mediated humoral responses are essential for controlling malarial infection. Studies have addressed the effects of Plasmodium falciparum infection on peripheral B-cell subsets but not much is known for P. vivax infection. Furthermore, majority of the studies investigate changes during acute
Immunoglobulin M Reactivity Towards the Immunologicdly Active Region sp75 of the Core Protein of Hepatitis C Virus (HCV) in Chronic HCV Infection.
U.B. Hellstrorn, S.P.E. Sylvan
Journal of Medical Virology, 39(4), 39325-39332 (1993)
Equatorial Assembly of the Cell-Division Actomyosin Ring in the Absence of Cytokinetic Spatial Cues.
Tzer Chyn Lim et al.
Current biology : CB, 28(6), 955-962 (2018-03-06)
The position of the division site dictates the size and fate of daughter cells in many organisms. In animal cells, division-site placement involves overlapping mechanisms, including signaling from the central spindle microtubules, astral microtubules, and spindle poles and through polar
Young Chan Kim et al.
Viruses, 11(5) (2019-05-06)
Chikungunya fever is a debilitating disease caused by Chikungunya virus (CHIKV) that can result in long-lasting arthralgias. The early diagnosis of CHIKV relies on PCR during the acute infection phase to allow differential diagnosis with other co-circulating arboviruses such as
Henrik Chart et al.
FEMS immunology and medical microbiology, 47(3), 391-397 (2006-07-29)
The techniques of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting were evaluated for the serodiagnosis of human infections with Yersinia enterocolitica and Yersinia pseudotuberculosis. Lipopolysaccharide (LPS) was prepared from strains comprising four serogroups of Y. enterocolitica and five
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