P8538
Protein Kinase Cδ isozyme human
>95% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution
Synonym(s):
Ca2+-activated phospholipid-dependent serine-threonine kinase δ isozyme human, PKCδ human
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5 μG
$782.00
About This Item
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recombinant
expressed in baculovirus infected insect cells
Quality Level
assay
>95% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
74-79 kDa by SDS-PAGE
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PRKCD(5580)
Biochem/physiol Actions
PKCδ is involved in the induction of apoptosis in many cell types.
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.
Unit Definition
One unit will transfer 1 nmol of phosphate to PKC epsilon substrate peptide in 1 min at pH 7.4 at 30 °C.
Physical form
Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol.
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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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
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
Yong Xiang et al.
Plant physiology, 144(3), 1416-1428 (2007-05-31)
Plants respond to adverse environments by initiating a series of signaling processes that often involves diverse protein kinases, including calcineurin B-like protein-interacting protein kinases (CIPKs). In this study, putative CIPK genes (OsCIPK01-OsCIPK30) in the rice (Oryza sativa) genome were surveyed
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
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