Skip to Content
Merck
All Photos(1)

Key Documents

I8260

Sigma-Aldrich

IgM from human serum

reagent grade, ~95% (HPLC), buffered aqueous solution

Synonym(s):

Human IgM

Sign Into View Organizational & Contract Pricing


About This Item

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

conjugate

unconjugated

Quality Level

grade

reagent grade

Assay

~95% (HPLC)

form

buffered aqueous solution

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

General description

There are five immunoglobulin classes in humans. Out of these, immunoglobulin M (IgM) is a high molecular weight protein that has five or six subunits. IgM monomers are made of two heavy chains and two light chains connected by a disulfide bond. Human serum shows low concentration of IgM monomers. It has a high carbohydrate content of about 12%. It is the first immunoglobulin produced by neonates.
IgM antibodies are present as pentamers in the serum and are produced in response to antigens.
IgM from human serum is purified from normal human serum by precipitation and gel filtration techniques. The immunoglobulin is determined to be atleast 95% pure by HPLC procedures.

Application

Purified human IgM may be used as a reference antigen, standard, blocking agent, or coating protein in a variety of immunoassays including ELISA, dot immunobinding, Western immunoblotting, immunodiffusion, and immunoelectrophoresis. Other applications include starting materials for the preparation of immunogens and solid phase immunoadsorbents. IgM from human serum was used as standard in ELISA (100 μg/ml) and dot blot assay. Antibody concentration range of 200 μg/ml to 1 mg/ml was used in IgM binding assays.
IgM from human serum has been used
  • in ELISA inhibition assay
  • in immunoblotting
  • as MW (molecular weight) standards
  • in IgM binding assay
  • to confirm the depletion of immunoglobulins

Biochem/physiol Actions

Immunoglobulin M (IgM) acts as an antigen specific part of the B cell antigen receptor on the surface of B lymphocytes that are not stimulated, in its monomeric form. Polymeric IgM molecules also serve as important activators of the classical complement cascade. IgM is essential in agglutination and cytolytic reactions.

Physical form

Solution in 0.05 M Tris-HCl, 0.2 M sodium chloride, pH 8.0, containing 15 mM sodium azide.

Storage and Stability

Store at 2-8 °C. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.

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.

Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

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

Visit the Document Library

H R Amini et al.
FEMS immunology and medical microbiology, 16(3-4), 163-172 (1996-12-31)
Western blot analysis (immunoblotting) of cell surface-associated proteins from Helicobacter pylori confirmed our previous findings that binding of human IgG is a common property (among H. pylori strains). Purification of the IgG-binding proteins (IGBP) was achieved by two purification steps
Killing of dsrA mutants of Haemophilus ducreyi by normal human serum occurs via the classical complement pathway and is initiated by immunoglobulin M binding.
Abdullah M, et al.
Infection and Immunity, 73(6), 3431-3439 (2005)
Localization of the domains of the Haemophilus ducreyi trimeric autotransporter DsrA involved in serum resistance and binding to the extracellular matrix proteins fibronectin and vitronectin.
Leduc I, et al.
Infection and Immunity, 77(2), 657-666 (2009)
Selection of mimotopes of the cell surface adhesion molecule Mel-CAM from a random pVIII-28aa phage peptide library.
Hafner C, et al.
The Journal of Investigative Dermatology, 119(4), 865-869 (2002)
Isabelle Leduc et al.
Infection and immunity, 77(2), 657-666 (2008-11-19)
Resisting the bactericidal activity of naturally occurring antibodies and complement of normal human serum is an important element in the evasion of innate immunity by bacteria. In the gram-negative mucosal pathogen Haemophilus ducreyi, serum resistance is mediated primarily by the

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service