Product Name: BARK1 (347-359) pS350+pT353+pY356
Product Number: PE-04ARY40
| Size: | 200 µg | Price: | 23.00 | |
| 1 mg | $US | 46.00 | ||
| 5 mg | 124.00 |
Peptide Name: BARK1 (347-359) pS350+pT353+pY356
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. Phosphorylation of the S350 site is predicted to be stimulatory, whereas the T353 and Y356 sites are predicted to be inhibitory.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: PHA-pS-VG-pT-HG-pY-MAP
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: βAla-Cys
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. Phosphorylation of the S350 site is predicted to be stimulatory, whereas the T353 and Y356 sites are predicted to be inhibitory.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: PHA-pS-VG-pT-HG-pY-MAP
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: βAla-Cys
Peptide Modifications Other: Phosphorylated
Peptide Molecular Mass Calculated: 1737.6 Da
Peptide Purity Percent after Synthesis and Purification: 43.2
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Molecular Mass Calculated: 1737.6 Da
Peptide Purity Percent after Synthesis and Purification: 43.2
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Scientific Background: BARK1 (GRK2, ADRBK1) is a protein-serine/threonine kinase of the AGC group and GRK family. It is activated by G-beta/gamma subunit complex. Phosphorylation of S29 increases phosphotransferase activity. Phosphorylation of S670 inhibits G-beta/gamma-mediated activation of GRK2. Phosphorylation of Y13, Y86, Y92 and S685 increases interaction with G-alpha(q) and may induce protein degradation.
© Kinexus Bioinformatics Corporation 2017