| Identification | Back Directory | [Name]
H-ARG-PHE-ALA-ARG-LYS-GLY-SER-LEU-ARG-GLN-LYS-ASN-VAL-OH | [CAS]
136795-05-6 | [Synonyms]
RFARKGSLRQKNV
[SER25]-PKC (19-31)
[SER25]-PROTEIN KINASE C (19-31)
PROTEIN KINASE C [SER-25] (19-31)
[SER 25]-PROTEIN KINASE C FRAGMENT 19-31
7:PN:JP2006076967 SEQID:7 unclaimed protein
ARG-PHE-ALA-ARG-LYS-GLY-SER-LEU-ARG-GLN-LYS-ASN-VAL
H-ARG-PHE-ALA-ARG-LYS-GLY-SER-LEU-ARG-GLN-LYS-ASN-VAL-OH
L-Valine, L-arginyl-L-phenylalanyl-L-alanyl-L-arginyl-L-lysylglycyl-L-seryl-L-leucyl-L-arginyl-L-glutaminyl-L-lysyl-L-asparaginyl- | [Molecular Formula]
C67H118N26O17 | [MDL Number]
MFCD00076724 | [MOL File]
136795-05-6.mol | [Molecular Weight]
1559.82 |
| Hazard Information | Back Directory | [Uses]
[Ser25] Protein Kinase C (19-31) is a substrate of protein kinase C (PKC) (Km: 0.3 μM). [Ser25] Protein Kinase C (19-31) is derived from the pseudo-substrate regulatory domain of PKCα (19-31) with a Serine at position 25 replacing the wild-type Alanine[1]. | [Biological Activity]
protein kinase c (19-31), (c67h118n26o17), a peptide with the sequence h-arg-phe-ala-arg-lys-gly-ser-leu-arg-gln-lys-asn-val-oh, mw= 1559.82. this peptide derived from the pseudo-substrate regulatory domain of pkca (residues 19-31) with a serine at position 25 replacing the wild-type alanine, it was used as protein kinase c substrate peptide for testing the protein kinase c activity.protein kinase c also known as pkc, is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins. pkca has been reported to play roles in many different cellular processes, such as cell adhesion, cell transformation, cell cycle checkpoint, and cell volume control. knockout studies in mice suggest that this kinase may be a fundamental regulator of cardiac contractility and ca2+ handling in myocytes.figure1 formula of [ser25] protein kinase c (19-31)figure2 signaling pathway of protein kinase c1. mellor h, parker pj (1998). "the extended protein kinase c superfamily". biochem. j.. 332 ( pt 2): 281–922. nishizuka y (1995). "protein kinase c and lipid signaling for sustained cellular responses" (abstract). faseb j. 9 (7): 484–96.3. vicente micol. correlation between protein kinase c an activity and membrane phase behavior. departamento de bioqu?′mica y biolog?′a molecular | [References]
[1] Wilder PT, et al. S100B(betabeta) inhibits the protein kinase C-dependent phosphorylation of a peptide derived from p53 in a Ca2+-dependent manner. Protein Sci. 1998 Mar;7(3):794-8. DOI:10.1002/pro.5560070330 |
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