Product Name: JNK3 (220-226) pY223
Product Number: PE-04AWD00
| Size: | 200 µg | Price: | 29.00 | |
| 1 mg | $US | 59.00 |
Peptide Name: JNK3 (220-226) pY223
Product Use: This phosphopeptide may be useful as a substrate for screening the phosphatase activity of protein phosphatases. The peptide sequence is located in the protein kinase catalytic domain activation T loop region between subdomains VII and VIII. Y223 phosphorylation stimulates phosphotransferase activity.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: MTP-pY-VVT
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: βAla-Cys
Peptide Modifications Other: Phosphorylated
Product Use: This phosphopeptide may be useful as a substrate for screening the phosphatase activity of protein phosphatases. The peptide sequence is located in the protein kinase catalytic domain activation T loop region between subdomains VII and VIII. Y223 phosphorylation stimulates phosphotransferase activity.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: MTP-pY-VVT
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: βAla-Cys
Peptide Modifications Other: Phosphorylated
Peptide Purity Percent after Synthesis and Purification: ~70
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Storage Stability: solution tends to dimerize
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Storage Stability: solution tends to dimerize
Scientific Background: JNK3 (MAPK10) is a protein-serine/threonine kinase of the CMGC group and MAPK family. Phosphorylation at T221 and Y223, by MAP2K4 and MAP2K7. MAP2K7, increases phosphotransferase activity. MAP2K7 phosphorylates JNK3 on T221 causing a conformational change and a large increase in Vmax. MAP2K4 then phosphorylates Y223 resulting in a further increase in Vmax. Phosphorylation at T131 inhibits phosphotransferase activity. It is inhibited by dual specificity phosphatases, such as DUSP1 and by HDAC9. The near absence of reported somatic mutations in this protein indicates that it may function as a tumour requiring protein (TRP) in many human tumours.
© Kinexus Bioinformatics Corporation 2017