T-cell surface glycoprotein CD8 beta chain (CD8B)

The T-cell surface glycoprotein CD8 beta chain (CD8B) is a type I transmembrane glycoprotein that, together with the CD8 alpha chain, forms the CD8 co-receptor on the surface of cytotoxic T lymphocytes. The CD8 co-receptor exists either as an alpha-beta heterodimer (most common in peripheral T cells) or less commonly as an alpha-alpha homodimer, and binds specifically to the non-polymorphic α3 domain of MHC class I molecules. This interaction increases the affinity of the T cell receptor (TCR) for antigen-MHC complexes, stabilizes the T cell-target cell interaction, and is critical for T cell activation, signaling, and cytotoxic function. The CD8 beta chain plays a complementary role to the alpha chain, with distinct patterns of palmitoylation affecting its cell surface localization and signaling efficiency. CD8 expression is a hallmark of cytotoxic T cells, making it a key immune marker and a potential therapeutic target in immunomodulation, cancer immunotherapy, and immune depletion strategies.

Other names

CD8 beta chainCD8BT-cell surface antigen CD8 beta chain

Monoclonal antibodies: Depletion, blocking, or modulation of CD8+ T cells by binding to the CD8 beta chain