|Calculated MW||95348 Da|
|Other Names||B-cell receptor CD22, B-lymphocyte cell adhesion molecule, BL-CAM, Sialic acid-binding Ig-like lectin 2, Siglec-2, T-cell surface antigen Leu-14, CD22, CD22, SIGLEC2|
|Target/Specificity||A synthetic phospho-peptide corresponding to residues surrounding Tyrosine 807 of human CD22 was used as immunogen. The antibody will detect CD22 phosphorylation on Tyrosine 807. This antibody is predicted to detect splice isoforms 2 based on sequence homology.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CD22 Antibody Phospho (pY807) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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.|
|Cellular Location||Cell membrane; Single-pass type I membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
CD22, a negative regulator of B cell signaling, belongs to the sialoadhesin family of receptors that preferentially binds to α2-6-linked sialic acid on glycoproteins (1-2). CD22 is known to interact with the B cell antigen receptor (BCR) (3) and the tyrosine phosphatase SHP1. Tyrosine phosphorylation of CD22 leads to the recruitment of multiple intracellular Src homology 2 (SH2) domain-containing effector molecules, including phospholipase C and Syk, which are important for triggering Ca2+ influx, as well as PI 3-kinase and Grb2 (4-5). Phosphorylation of Tyrosine 807 is involved in the binding of Syk.
1. Wilson, G. L.; Najfeld, V.; Kozlow, E.; Menniger, J.; Ward, D.; Kehrl, J. H.: J. Immun. 150: 5013-5024, 1993.
2. Nitschke, L., H. Floyd, P. R. Crocker. 2001. Scand. J. Immunol. 53:227
3. Tedder, T. F., J. Tuscano, S. Sato, J. H. Kehrl. 1997. Annu. Rev. Immunol. 15:481
4. Yohannan, J., J. Wienands, K. M. Coggeshall, L. B. Justement. 1999. J. Biol. Chem. 274:18769
5. Otipoby, K. L., K. E. Draves, E. A. Clark. 2001. J. Biol. Chem. 276:44315.
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