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SRP5251

Sigma-Aldrich

PKC-α, active, GST tagged from Xanopus sp.

PRECISIO®, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

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Synonym(s):
MGC82897, PRKCA
UNSPSC Code:
12352200
NACRES:
NA.32

biological source

Xenopus sp.

recombinant

expressed in baculovirus infected Sf9 cells

product line

PRECISIO®

Assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

specific activity

186-290 nmol/min·mg

mol wt

~103 kDa

NCBI accession no.

application(s)

cell analysis

shipped in

dry ice

storage temp.

−70°C

Gene Information

Xenopus laevis ... prkca(447031)

General description

Protein kinase C-α (PKC-α) is a member of the PKC family of serine- and threonine-specific protein kinases that can be activated by calcium and the secondary messenger diacylglycerol. The protein is expressed in the dorsal ectoderm of Xenopus.

Biochem/physiol Actions

Protein kinase C-α (PKC-α) has been reported to play roles in many different cellular processes, such as cell adhesion, cell transformation, cell cycle checkpoint and cell volume control. It has been identified as a fundamental regulator of cardiac contractility and Ca2+ handling in myocytes.

Physical form

Supplied in 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 10 mM glutathione, 0.1 mM EDTA, 0.25 mM DTT, 0.1 mM PMSF, 25% glycerol.

Preparation Note

After opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles.

Legal Information

PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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aPKC phosphorylates p27Xic1, providing a mechanistic link between apicobasal polarity and cell-cycle control.
Sabherwal N
Developmental Cell, 31(5), 559-571 (2014)
PKC-alpha regulates cardiac contractility and propensity toward heart failure.
Braz JC
Nature Medicine, 10(3), 248-254 (2004)
Protein kinase C isozymes have distinct roles in neural induction and competence in Xenopus.
Otte AP and Moon RT
Cell, 68(6), 1021-1029 (1992)
Yi Liu et al.
The Biochemical journal, 478(10), 1999-2017 (2021-05-08)
Human hepatic tryptophan 2,3-dioxygenase (hTDO) is a homotetrameric hemoprotein. It is one of the most rapidly degraded liver proteins with a half-life (t1/2) of ∼2.3 h, relative to an average t1/2 of ∼2-3 days for total liver protein. The molecular mechanism

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