Description
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- 1/2 (PLC 1/2) and in vitro phosphorylation of fusion proteins showed that both Syk and PLC 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).
Biomolecule/Target: N/A
Synonyms: PKC, Protein kinase C mu
Alternates names: PKC, Protein kinase C mu
Taglines: Involved in regulation of glycogen, sugar, and lipid metabolism
NCBI Gene ID #: 4908
NCBI Gene Symbol: NTF3
Gene Source: N/A
Accession #: P20783
Recombinant: Yes
Source: Baculovirus (Sf9 insect cells)
Purity by SDS-PAGEs: 98%
Assay: SDS-PAGE
Purity: N/A
Assay #2: HPLC
Endotoxin Level: N/A
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).
Biological activity: The ED as determined by the dose-dependent induction of choline acetyl transferase activity in rat basal forebrain primary septal cell cultures was found to be in the range of 20-50 ng/ml.
Results: N/A
Binding Capacity: N/A
Unit Definition: N/A
Molecular Weight: 131.0 kDa
Concentration: 5µg/50 µl
Appearance: Liquid
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).
Reconstitution Instructions: Reconstitute in HO to a concentration of 0.1-1.0 mg/ml.
Amino acid sequence: N/A