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P7956

Sigma-Aldrich

Protein Kinase C from rat brain

>90% (SDS-PAGE), lyophilized powder

Synonym(s):

PKC

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352200

assay

>90% (SDS-PAGE)

form

lyophilized powder

mol wt

82 kDa by SDS-PAGE

color

white

shipped in

dry ice

storage temp.

−20°C

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Biochem/physiol Actions

Ca2+-activated, phospholipid-dependent serine/threonine protein kinase.
Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and γ. Members of the second family are phospholipid-dependent but Ca2+-independent, and include PKCδ, ε, η, and θ. Members of the third family are not activated by either DAG or phorbol esters and include PKCξ, μ, and ι.
Phosphorylation appears to be an important mechanism of regulation of all PKCs. PKC plays a role in the regulation of cell transformation, growth, differentiation, ruffling, vesicle trafficking, apoptosis and gene expression.

Other Notes

Mixture of isozymes.

Unit Definition

One unit will transfer 1 nmol of phosphate per min from ATP to histone H1 at pH 7.4 at 30 °C.

Physical form

Supplied as lyophilized white powder containing Tris buffer salts, EDTA, EGTA, DTT, Tween 20, sodium chloride, leupeptin, and sucrose as stabilizer.

Reconstitution

Reconstitute with 100 μl of dH2O.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Coleen M Atkins et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 24(22), 5193-5201 (2004-06-04)
Phosphorylation of cytoplasmic polyadenylation element binding protein (CPEB) regulates protein synthesis in hippocampal dendrites. CPEB binds the 3' untranslated region (UTR) of cytoplasmic mRNAs and, when phosphorylated, initiates mRNA polyadenylation and translation. We report that, of the protein kinases activated
Girdhar K Pandey et al.
Cell research, 17(5), 411-421 (2007-05-09)
Potassium is one of the major macro-nutrients essential for a number of cellular processes in plants. Low potassium level in the soil represents a limiting factor for crop production. Recent studies have identified potassium transporters that are involved in potassium
Mayuko Akaboshi et al.
Journal of molecular biology, 377(1), 246-257 (2008-02-02)
Calcium signals mediate a multitude of plant responses to external stimuli. Calcineurin B-like (CBL) proteins and their target kinases, CBL-interacting protein kinases (CIPKs), represent important relays in plant calcium signaling. CBL interacts with CIPK through a conserved motif (NAF/FISL motif)
Yahui Li et al.
Molecular human reproduction, 17(1), 42-56 (2010-08-24)
Members of the testis-specific serine/threonine kinases (Tssk) family may have a role in sperm differentiation in the testis and/or fertilization. To gain insight into the functional relevance of these kinases, their expression was examined both at the mRNA and protein
Nichole Link et al.
The Journal of cell biology, 178(4), 567-574 (2007-08-08)
We examined post-eclosion elimination of the Drosophila wing epithelium in vivo where collective "suicide waves" promote sudden, coordinated death of epithelial sheets without a final engulfment step. Like apoptosis in earlier developmental stages, this unique communal form of cell death

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