Anti-CD22

The B lymphocyte specific CD22 antigen, also designated B-lymphocyte cell adhesion molecule (BLCAM), sialic acid-binding Ig-like lectin 2 (Siglec-2) and Leu-14, is a type I integral membrane glycoprotein, structurally similar to other cell adhesion molecules (CAMs), which acts as a regulator of B cell signaling. CD22 is expressed as both a cytoplasmic and membrane protein during discrete stages of B cell lymphocyte differentiation. The cytoplasmic form of CD22, expressed early in B cell development, is a useful marker for acute lymphocytic leukemia. The membrane form of CD22 is expressed in mature B cells prior to their differentiation into plasma cells. Protein function: Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins, one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. [The UniProt Consortium]