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Synonyms
PKC, Protein kinase C mu
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Alternative_names
PKC, Protein kinase C mu
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Description
Involved in regulation of glycogen, sugar, and lipid metabolism
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Recombinant
Yes
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Source
Baculovirus (Sf9 insect cells)
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Purity by SDS PAGE
≥90%
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Assay
SDS-PAGE
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Activity Specifications test method
680 nmol phosphate incorporated into CREBTIDE substrate peptide per minute per mg protein at 30°C for 15 minutes using a final concentration of 50 µM ATP (0.83 µCi/assay).
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Molecular Weight
131.0 kDa
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Storage Temp
-80°C
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Shipping
dry ice
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Shelf Life
12 months
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Concentration
5µg/50 µl
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Appearance
Liquid
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Physical form description
Recombinant proteins in storage buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, 25% glycerol).
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Background Information
Protein kinase Cmu (PKCmu) is a novel member of the protein kinase C (PKC) family that differs from the other isoenzymes in structural and enzymatic properties. It is characterized by the presence of a pleckstrin homology (PH) domain and an amino-terminal hydrophobic region and has substrate specificity distinct from other PKC isoforms. PKCmu is a ubiquitous PKC isotype with the highest expression in the thymus, lung and peripheral blood mononuclear cells (1). PKCmu forms a complex in vivo with a phosphatidylinositol 4-kinase and a phosphatidylinositol-4-phosphate 5-kinase. A region of PKCmu between the amino-terminal transmembrane domain and the pleckstrin homology domain is shown to be involved in the association with the lipid kinases (2). PKCmu was also shown to associate with the B cell receptor (BCR) complex and its activity is up-regulated after cross-linking the BCR and CD19 on B cells (3). PKC mu co-precipitates with Syk and phospholipase C-γ 1/2 (PLC γ 1/2) and in vitro phosphorylation of fusion proteins showed that both Syk and PLC γ 1 are potential substrates of PKC mu in vivo. In addition, specific interaction of PKCmu and 14-3-3tau can be shown in the T cell line Jurkat by immunocoprecipitiation and by pulldown assays (4). 14-3-3tau is not a substrate of PKCmu and strongly down-regulates PKCmu kinase activity in vitro. In response to various stimuli, PKC mu activates the mitogen-activated protein kinase (p42/ERK1 MAPK cascade) but does not affect the related c-jun N-terminal kinase or p38 MAPK (5).
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Handling
Centrifuge the vial prior to opening.
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Usage
For Research Use Only! Not to be used in humans
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