Human CD8B recombinant protein (C-cleavage)

Human CD8B recombinant protein (C-cleavage)

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CD8B (CD8b molecule), also known as P37 and LEU2, contains 1 Ig-like V-type (immunoglobulin-like) domain. The CD8 antigen is a cell surface glycoprotein found on most cytotoxic T lymphocytes that mediates efficient cell-cell interactions within the immune system. The CD8 antigen, acting as a coreceptor, and the T-cell receptor on the T lymphocyte recognize antigens displayed by an antigen presenting cell (APC) in the context of class I MHC molecules. The functional coreceptor is either a homodimer composed of two alpha chains, or a heterodimer composed of one alpha and one beta chain. Both alpha and beta chains share significant homology to immunoglobulin variable light chains. P37 gene encodes the CD8 beta chain isoforms. Multiple alternatively spliced transcript variants encoding distinct membrane associated or secreted isoforms have been described. A pseudogene, also located on chromosome 2, has been identified. CD8 is thought to play a role in the process of T-cell mediated killing.

T-cell surface glycoprotein CD8 beta chain

CD8B1,LEU2,LY3,LYT3,P37

P10966-1

T-cell surface glycoprotein CD8 beta chain; CD antigen CD8b

Human Cells

A DNA sequence encoding the extracellular domain of human CD8B (P10966-1) (Met1-Pro170) was expressed with six amino acids (LEVLFQ) at the C- terminus. The purified protein was biotinylated in vitro.

Human

The recombinant human CD8B comprises 156 amino acids and has a predicted molecular mass of 17.6 kDa.

> 95 % as determined by SDS-PAGE