Product Name: PKG1 (518-527) pT521+pY524
Product Number: PE-04AXA95
| Size: | 200 µg | Price: | 47.00 | |
| 1 mg | $US | 95.00 |
Peptide Name: PKG1 (518-527) pT521+pY524
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. T521 and Y524 phosphorylation are predicted to be inhibitory for phosphotransferase activity.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: FCG-pT-PE-pY-VAP
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. T521 and Y524 phosphorylation are predicted to be inhibitory for phosphotransferase activity.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: FCG-pT-PE-pY-VAP
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: βAla-Cys
Peptide Modifications Other: Phosphorylated
Peptide Molecular Mass Calculated: 1458.4 Da
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Storage Stability: Stable as powder; solution tends to dimerize
Peptide Purity Percent after Synthesis and Purification: >95
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Storage Stability: Stable as powder; solution tends to dimerize
Scientific Background: PKG1 (PRKG1) is a protein-serine/threonine kinase of the AGC group and PKG family. It is activated by cGMP, which is generated in response to nitric oxide. Phosphorylation at T59 increases phosphotransferase activity and its affinity for cGMP Phosphorylation at T517 increases phosphotransferase activity. An R177Q mutation in AAT8 results in a constitutively active form of PKG1, which also has reduced cGMP binding.
© Kinexus Bioinformatics Corporation 2017