Anti-Human IgM (μ-chain specific)−Alkaline Phosphatase antibody produced in goat

affinity isolated antibody, buffered aqueous glycerol solution

MDL number:

Quality Level

biological source


antibody form

affinity isolated antibody

antibody product type

secondary antibodies




buffered aqueous glycerol solution

species reactivity



direct ELISA: 1:7,000-1:21,000


alkaline phosphatase conjugate

shipped in

wet ice

storage temp.


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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.


Human IgM.


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


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.


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

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)
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...
H A Cubie et al.
Journal of clinical pathology, 46(9), 840-845 (1993-09-01)
AIMS--To compare the sensitivity, specificity, and practicality of recombinant proteins in serological tests for the detection of human parvovirus B19 IgG and IgM. METHODS--Indirect enzyme linked immunosorbent assays using B19 structural proteins expressed in Escherichia coli were developed for the...
Francesca Gori et al.
Journal of neuroimmunology, 233(1-2), 216-220 (2011-01-11)
Antibodies to MOG in serum have a dubious prognostic value in multiple sclerosis. The MOG recombinant protein conformational properties relevant to the antigenic activity are unknown. We employed a solid-phase ELISA based on a product (rMOG(ED)(His)(6)) expressed in E. coli...
Songwang Hou et al.
Journal of immunological methods, 440, 27-34 (2016-10-30)
The presence of circulating autoantibodies against phosphatidylethanolamine (PE) has been shown to be positively associated with symptoms of antiphospholipid syndromes (APS). However, the current ELISA-based tests for antiphosphatidylethanolamine (aPE) antibodies remain inconsistent and controversial. The term PE refers to a...

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