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SAB4700346

Sigma-Aldrich

Monoclonal Anti-IgM antibody produced in mouse

clone CH2, purified immunoglobulin, buffered aqueous solution

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

CH2, monoclonal

form

buffered aqueous solution

species reactivity

human

concentration

1 mg/mL

technique(s)

flow cytometry: suitable

isotype

IgG1

NCBI accession no.

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

Gene Information

human ... IGH@(3492)

Related Categories

General description

Immunoglobulin M (IgM) is a member of immunoglobulin family. It exists as a pentamer in the serum and has a high molecular weight. Monomeric IgM has a molecular weight of 190 kDa. The pentameric IgM is characterized with ten μ heavy chains, ten light chains and a single J-chain which is linked by disulphide bonds. The μ chain consists of five domains- VH, Cμ1, Cμ2, Cμ3 and Cμ4. Limited digestion using papain cleaves the antibody into three fragments, two of which are identical and contain the antigen-binding activity. They are known as fragment antigen binding (Fab) fragments. The third fragment does not possess antigen-binding activity and is known as fragment crystallizable (Fc). It interacts with cells and effector molecules. The heavy chains of IgM contain an extra C domain that replaces the hinge region. IgM is the first antibody to be produced during an immune response and is the major isotype secreted in T-cell independent immune responses.
The antibody CH2 reacts with Fc fragment of human IgM.

Immunogen

Purified human IgM

Application

The reagent is designed for Flow Cytometry analysis. Suggested working dilution for Flow Cytometry is 1 μg/mL of sample. Indicated dilution is recommended starting point for use of this product. Working concentrations should be determined by the investigator.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

Solution in Tris buffered saline, pH 8.0, with 15 mM sodium azide.

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 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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The structure of a typical antibody molecule
Immunobiology: The Immune System in Health and Disease (2001)
Structural variation in immunoglobulin constant regions
Immunobiology: The Immune System in Health and Disease (2001)
D Martins de Medeiros et al.
Lupus, 23(13), 1412-1416 (2014-06-26)
The objective of this report is to conduct short- and long-term evaluation of a large panel of antiphospholipid (aPL) autoantibodies following pandemic influenza A/H1N1 non-adjuvant vaccine in primary antiphospholipid syndrome (PAPS) patients and healthy controls. Forty-five PAPS and 33 healthy
Andi Krumbholz et al.
Medical microbiology and immunology, 203(4), 273-282 (2014-04-20)
An increase in acute autochthonous hepatitis E virus (HEV) infections has been recorded in Germany. These are suspected to be zoonotically transmitted from wild boar, deer and domestic pig. The latter may represent a major reservoir for HEV. In this
Rosane Oliveira et al.
Journal of medical microbiology, 63(Pt 9), 1119-1130 (2014-06-15)
Leptospirosis, a worldwide zoonotic infection, is an important human and veterinary health problem. We have previously identified a leptospiral multipurpose adhesin, Lsa66, capable of binding extracellular matrix (ECM) components and plasminogen (PLG). In this work, we report the cloning, expression

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