Anti-CD22/B-cells, clone MEM-01 (Monoclonal) [Mouse]

MON1067 reacts with CD22, a 130 kDa type Itransmembrane glycoprotein (immunoglobulin superfamily) expressed in the cytoplasm of pro-B and pre-B lymphocytes, and on the surface of mature and activated B lymphocytes. Intracellular domain of CD22 recruits protein tyrosine phosphatase SHP1 through the immunoreceptor tyrosine-based inhibitory motifs (ITIMs), thus setting a threshold for B cell receptor-mediated activation. CD22 also regulates B-cell response by involvement in controlling the CD19/CD21-Src-family protein tyrosine kinase amplification pathway and CD40 signaling. CD22 exhibits hallmarks of clathrin-mediated endocytic pathway. 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]