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Immunoglobulin M (IgM) has a high molecular weight and belongs to the immunoglobulin family. It exists as a pentamer in the serum. Monomeric IgM has a molecular weight of 190kDa. The pentameric IgM consists of ten µ-heavy chains, ten light chains and a single J-chain which are 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 present between Fab and Fc. IgM is the first antibody to be produced during an immune response and is the major isotype secreted in T-cell independent immune responses.
Rat IgM mu heavy chain
Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 10 mg/mL Bovine Serum Albumin (BSA) - Immunoglobulin and Protease free
Antibody format: IgG
Reconstitute with 1.0 mL deionized water (or equivalent).
This product was prepared from monospecific antiserum by immunoaffinity chromatography using antigens coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Peroxidase, Anti-Rabbit Serum, Rat IgM and Rat Serum. No reaction was observed against Rat IgA or Rat IgG. ELISA was used to confirm specificity at less than 1% cross reactivity against other rat heavy or light chain isotypes.