PKI (5-24) structure
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Common Name | PKI (5-24) | ||
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CAS Number | 99534-03-9 | Molecular Weight | 2222.38000 | |
Density | N/A | Boiling Point | N/A | |
Molecular Formula | C94H148N32O31 | Melting Point | N/A | |
MSDS | USA | Flash Point | N/A |
Use of PKI (5-24)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]. |
Name | h-thr-thr-tyr-ala-asp-phe-ile-ala-ser-gly-arg-thr-gly-arg-arg-asn-ala-ile-his-asp-oh |
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Synonym | More Synonyms |
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]. |
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Related Catalog | |
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 |
Molecular Formula | C94H148N32O31 |
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Molecular Weight | 2222.38000 |
Exact Mass | 2221.10000 |
PSA | 1049.44000 |
Personal Protective Equipment | Eyeshields;Gloves;type N95 (US);type P1 (EN143) respirator filter |
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RIDADR | NONH for all modes of transport |
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... |
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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... |
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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... |
PROTEIN KINASE INHIBITOR RABBIT |
ip20 |
TTYADFIASGRTGRRNAIHD |
PROTEIN KINASE A INHIBITOR 5-24 |
protein kinase inhibitor from rabbit |
H-TTYADFIASGRTGRRNAIHD |