|Calculated MW||23147 Da|
|Other Names||T-cell surface glycoprotein CD3 epsilon chain, T-cell surface antigen T3/Leu-4 epsilon chain, CD3e, CD3E, T3E|
|Target/Specificity||A synthetic peptide corresponding to residues in cytoplasmic domain of human CD3 epsilon was used as immunogen. The antibody does not cross-react with other subunits of CD3.|
|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||CD3 epsilon Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||The CD3 complex mediates signal transduction, resulting in T-cell activation and proliferation. Required for normal immune responses (PubMed:15546002, PubMed:8490660).|
|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.
CD3 (Cluster of Differentiation 3) is a complex of proteins that associates directly with the T cell antigen receptor (TCR) (1). Antigen binding to the TCR leads to IL-2 secretion via activation of a tyrosine phosphorylation pathway and a phospholipase C (PLC) pathway, in turn activating protein kinase C (1,2). CD3 is composed of five invariant polypeptide chains that associate to form three dimers. The five invariant chains of CD3 are labeled gamma, delta, epsilon, zeta, and eta. The gamma, epsilon and delta chains each contain a single copy of a conserved immunoreceptor tyrosine-based activation motif (ITAM). Phosphorylated ITAMs act as docking sites for protein kinases such as ZAP-70 and Syk (3).
1. Weiss, A., et al. Signal transduction by the T cell antigen receptor. Sem. Immunol. 3: 313
2. Siegel, J.N., et al. Multiple signal transduction pathways activated through the T cell receptor for antigen. Semin Immunol. 3: 325
3. Futterer, K., et al. Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide. J Mol Biol. 281: 523
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