IgD Heavy Chain Antibody

Immunohistochemistry (FFPE): 1-2ug/ml for 30 minutes at RT

Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through interchain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin D (IgD) exists as a monomer with delta heavy chains and either kappa or lambda light chains. It plays a biological role as a transmembrane receptor molecule, co-expressed with IgM on the surface of mature/naive B cells. In particular, it is found on spleen B cell surfaces. Compared to IgM, IgD exists in much lower numbers and is not expressed on immature B cells. IgD surface expression on B cells is regulated in part by IL-27. In mice, the inhibition of this immunoglobulin isotype does not cause a significant change to the immune system.

Purified

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide

A recombinant partial protein sequence (within amino acids 1-200) from the human protein was used as the immunogen for the IgD antibody.

This IgD antibody is available for research use only.

Cytoplasm

Protein A/G affinity

P01880