PKI (5-24)

Names

[ Name ]:
PKI (5-24)

[Synonym ]:
PROTEIN KINASE INHIBITOR RABBIT
ip20
TTYADFIASGRTGRRNAIHD
PROTEIN KINASE A INHIBITOR 5-24
protein kinase inhibitor from rabbit
H-TTYADFIASGRTGRRNAIHD

Biological Activity

[Description]:

PKI(5-24) is a potent, competitive, and synthetic peptide inhibitor of PKA (cAMP-dependent protein kinase), with a Ki of 2.3 nM. PKI(5-24) corresponds to residues 5-24 in the naturally occurring heat-stable protein kinase inhibitor[1][2].

[Related Catalog]:

Signaling Pathways >> Protein Tyrosine Kinase/RTK >> PKA

Research Areas >> Others

Signaling Pathways >> Stem Cell/Wnt >> PKA

[In Vitro]

PKI(5-24) is a 20-residue peptide has been synthesized that corresponds to the active site of the skeletal muscle inhibitor protein[1]. PKI(5-24) inhibits phosphotransferase activity of the mutant cGMP kinase with higher potency than that of wild type, with Ki values of 42 μΜ and 160 μΜ, respectively[2].

[References]

[1]. Cheng HC, et al. A potent synthetic peptide inhibitor of the cAMP-dependent protein kinase. J Biol Chem. 1986;261(3):989-992.

[2]. Ruth P, et al F. A cGMP kinase mutant with increased sensitivity to the protein kinase inhibitor peptide PKI(5-24). Biol Chem. 1996;377(7-8):513-520.

Chemical & Physical Properties

[ Molecular Formula ]:
C₉₄H₁₄₈N₃₂O₃₁

[ Molecular Weight ]:
2222.38000

[ Exact Mass ]:
2221.10000

[ PSA ]:
1049.44000

MSDS

Click to get detail MSDS

Safety Information

[ Personal Protective Equipment ]:
Eyeshields;Gloves;type N95 (US);type P1 (EN143) respirator filter

[ RIDADR ]:
NONH for all modes of transport

Articles

A potent synthetic peptide inhibitor of the cAMP-dependent protein kinase.

J. Biol. Chem. 261 , 989, (1986)

As an important new reagent for studying the cAMP-dependent protein kinase, a 20-residue peptide has been synthesized that corresponds to the active site of the skeletal muscle inhibitor protein. This...

Effects of endoplasmic reticulum stress on group VIA phospholipase A2 in beta cells include tyrosine phosphorylation and increased association with calnexin.

J. Thorac. Cardiovasc. Surg. 285 , 33843-57, (2010)

The Group VIA phospholipase A(2) (iPLA(2)β) hydrolyzes glycerophospholipids at the sn-2-position to yield a free fatty acid and a 2-lysophospholipid, and iPLA(2)β has been reported to participate in a...

Release of Ca2+ by inositol 1,4,5-trisphosphate in platelet membrane vesicles is not dependent on cyclic AMP-dependent protein kinase.

Biochem. J. 257(3) , 715-21, (1989)

In contrast with previous reports, it was found that membrane-protein phosphorylation by the catalytic subunit (CS) of cyclic AMP-dependent protein kinase had no effect on Ca2+ uptake into platelet me...