Skip to Content
Merck

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

Sign In to View Organizational & Contract Pricing.

Select a Size

Change View

About This Item

UNSPSC Code:
12352203
NACRES:
NA.46
MDL number:
Conjugate:
alkaline phosphatase conjugate
Clone:
polyclonal
Application:
ELISA (d)
Citations:
8
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist


biological source

goat

Quality Level

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

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).
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). Arnold, J. (2005) Human serum IgM glycosylation: identification of glycoforms that can bind to mannan-binding lectin. JBC, 280: 29080-29087.
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.


Still not finding the right product?

or

Try our Product Selector Tool to narrow your options


Storage Class

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable



Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library


Related Content

Instructions


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)
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
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