Product Name: PKACa (201-208) pT202+pY205
Product Number: PE-04AWY99
| Size: | 200 µg | Price: | 16.00 | |
| 1 mg | $US | 31.00 |
Peptide Name: PKACa (201-208) pT202+pY205
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. T202 and Y205 phosphorylation are predicted to be inhibitory for phosphotransferase activity.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: G-pT-PE-pY-LAP
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. T202 and Y205 phosphorylation are predicted to be inhibitory for phosphotransferase activity.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: G-pT-PE-pY-LAP
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: βAla-Cys
Peptide Modifications Other: Phosphorylated
Peptide Molecular Mass Calculated: 1222.1 Da
Peptide Purity Percent after Synthesis and Purification: >50
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Peptide Molecular Mass Calculated: 1222.1 Da
Peptide Purity Percent after Synthesis and Purification: >50
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Scientific Background: PKACa (PRKACA) is a protein-serine/threonine kinase of the AGC group and PKA family. It serves as the alpha catalytic subunit of the cAMP-dependent protein kinase holoenzyme PKA, and it phosphorylates and regulates a very large number of cytoplasmic and nuclear substrate proteins. Phosphorylates hundreds of substrates in the cytoplasm and the nucleus. These include CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, TRPC1 and VASP. It is activated by binding of two cAMP molecules to each of the two associated regulatory subunits in the PKA holoenzyme. Binding of cAMP induces dissociation of the two active catalytic subunits. Phosphorylation of T198 increases phosphotransferase activity. Phosphorylation of S338 plays a key role in stabilizing PKACa. PKACa may be an oncoprotein (OP), although this kinase has also been implicated in inhibiting normal cell proliferation. Gain-of-function mutations in the PRKACA catalytic domain are associated with elevated catalytic activity of the kinase, and have been observed in several cancer types. In particular, a L206R subsitution mutation is observed in cancer and in Cushing's syndrome patients. The gain-of-function mutation is predicted to result in the interruption of the interaction between the catalytic and regulatory subunits of protein kinase A, resulting in a constitutively active PKA. Gain-of-function mutations in the PRKACA gene that lead to consitutive activity of the PKA holoenzyme have been proposed to play an important role in the development of several types of cancer.
© Kinexus Bioinformatics Corporation 2017