P0194
Protein Kinase Cζ isozyme human
≥75% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous solution
Synonym(s):
Ca2+-activated phospholipid-dependent serine-threonine kinase ζ isozyme human, PKCζ human
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About This Item
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recombinant
expressed in baculovirus infected insect cells
Quality Level
Assay
≥75% (SDS-PAGE)
form
buffered aqueous solution
enzyme activity
>800 units/mg protein
mol wt
76-80 kDa by SDS-PAGE
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PRKCZ(5590)
Biochem/physiol Actions
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.
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.
Suitability
PKC ε can transfer 1100 nmole of phosphate to PKC ε substrate peptide per minute per mg of total protein at 30 °C.
Unit Definition
One unit will transfer 1 nanomole of phosphate to PKC epsilon substrate peptide per minute at pH 7.5 at 30 deg C.
Physical form
Solution in 20 mM HEPES, pH 7.5; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 250 mM NaCl, 0.05% Triton X-100, and 50% glycerol.
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Jun Hou et al.
Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer, 7(1), 105-114 (2011-12-03)
A challenge of cancer therapy is to optimize therapeutical options to individual patients. Cancers with similar histology may show dramatically different responses to therapy, indicating that a refined approach needs to be developed to classify tumors by intrinsic characteristics that
Hai Huang et al.
Development (Cambridge, England), 138(12), 2477-2485 (2011-05-13)
Post-translational modification by the small ubiquitin-related modifier (SUMO) is important for a variety of cellular and developmental processes. However, the precise mechanism(s) that connects sumoylation to specific developmental signaling pathways remains relatively less clear. Here, we show that Smt3 knockdown
Wendy Lee et al.
Developmental biology, 325(1), 263-272 (2008-11-18)
Homeodomain interacting protein kinase (Hipk) is a member of a novel family of serine/threonine kinases. Extensive biochemical studies of vertebrate homologs, particularly Hipk2, have identified a growing list of interactors, including proteins involved in transcriptional regulation, chromatin remodeling and essential
Masaki Kinoshita et al.
Development (Cambridge, England), 136(12), 2069-2079 (2009-05-26)
From a list of protein kinases (PKs) that are newly induced upon differentiation of mouse embryonic stem cells to mesendoderm, we identified a previously uncharacterized kinase, Vlk (vertebrate lonesome kinase), that is well conserved in vertebrates but has no homologs
YuZhi Qin et al.
Science in China. Series C, Life sciences, 51(5), 391-401 (2008-09-13)
Calcium and protein kinase serve as the common mediators to regulate plant responses to multiple stresses including salt and ABA stimulus. Here we reported a novel protein kinase (CIPK14) that regulated the responses to ABA treatment and salt stress in
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