Product Name: ZAP70 (316-322) pY319
Product Number: PE-04ALM99
| Size: | 200 µg | Price: | 47.00 | |
| 1 mg | $US | 94.00 | ||
| 5 mg | 206.00 |
Peptide Name: ZAP70 (316-322) pY319
Product Use: Services as a blocking peptide for use with the ZAP70-pY319 rabbit polyclonal antibody (Cat. No.: AB-PK862) that is also available from Kinexus. This phosphopeptide may also be useful as a substrate for screening the phosphatase activity of protein phosphatases. The peptide sequence is located in the region between the SH2 and kinase catalytic domains. One of the major in vivo sites of phosphorylation in ZAP70. Y319 phosphorylation stimulates phosphotransferase activity and regulates intracellular location, transcription and molecular association, including inducing interaction with Lck and PLCG1.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: ESP-pY-SDP
Product Use: Services as a blocking peptide for use with the ZAP70-pY319 rabbit polyclonal antibody (Cat. No.: AB-PK862) that is also available from Kinexus. This phosphopeptide may also be useful as a substrate for screening the phosphatase activity of protein phosphatases. The peptide sequence is located in the region between the SH2 and kinase catalytic domains. One of the major in vivo sites of phosphorylation in ZAP70. Y319 phosphorylation stimulates phosphotransferase activity and regulates intracellular location, transcription and molecular association, including inducing interaction with Lck and PLCG1.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: ESP-pY-SDP
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: βAla-Cys
Peptide Modifications Other: Phosphorylated
Peptide Molecular Mass Calculated: 1047.96 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Related Product 1: ZAP70 - pY319 phosphosite-specific antibody (Cat. No.: AB-PK862)
Peptide Modifications C Terminus: βAla-Cys
Peptide Modifications Other: Phosphorylated
Peptide Molecular Mass Calculated: 1047.96 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Related Product 1: ZAP70 - pY319 phosphosite-specific antibody (Cat. No.: AB-PK862)
Scientific Background: ZAP70 (SRK) is a protein-tyrosine kinase of the TK group and Syk family. It is highly expressed in heart, lymph nodes, pancreas, parathyroid gland, spleen, stomach, thymus and tonsils. It plays an essential role in mediating the adaptive immune response. ZAP70 can control adhesion, motility, and cytokine production in T cells, and natural killer (NK) cell functions as well as the development of thymocytes and primary B-cells. ZAP70 is activated by phosphorylation at Y319, Y474 and Y493, and inhibited by phosphorylation at Y492, which functions as a docking site for Cbl. Phosphorylation of Y319 also increases PLC-g1+ and Ras activation, and it is an Lck binding site. Phosphorylation of Y315 of ZAP70 induces association with CrkII. Phosphorylation of S520 primes ZAP70 binding to the plasma membrane. ZAP70 mediates T-cell antigen receptor (TCR) signalling. ZAP70 is phosphorylated and activated by the doubly-phosphorylated TCR component CD247/CD3Z at the plasma membrane. Ligation of the TCR/CD3 receptor in Jurkat T-cells induces complexes which contain ZAP70. TCR zeta chains are initially phosphorylated by Lck, which leads to the recruitment of ZAP70 via its SH2 domain. ZAP70 in turn phosphorylates the zeta-chain dimer in the TCR/CD3-phosphoprotein complex. ZAP70 may be an oncoprotein (OP). Gain-of-function mutations in the ZAP70 gene have been observed in several human cancer types, including neck squamous cell carcinomas, Malt lymphomas, acute lymphoblastic leukemias (ALL) and in chronic lymphocytic leukemias (CLL). ZAP70 has also been linked with severe combined immunodeficiency, chronic arthritis, and selective T-cell defects.
© Kinexus Bioinformatics Corporation 2017