P0194
Protein Kinase Cζ isozyme human
≥75% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous solution
Synonyme(s) :
Ca2+-activated phospholipid-dependent serine-threonine kinase ζ isozyme human, PKCζ human
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About This Item
Produits recommandés
Produit recombinant
expressed in baculovirus infected insect cells
Niveau de qualité
Pureté
≥75% (SDS-PAGE)
Forme
buffered aqueous solution
enzyme activity
>800 units/mg protein
Poids mol.
76-80 kDa by SDS-PAGE
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−70°C
Informations sur le gène
human ... PRKCZ(5590)
Actions biochimiques/physiologiques
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.
Adéquation
PKC ε can transfer 1100 nmole of phosphate to PKC ε substrate peptide per minute per mg of total protein at 30 °C.
Définition de l'unité
One unit will transfer 1 nanomole of phosphate to PKC epsilon substrate peptide per minute at pH 7.5 at 30 deg C.
Forme physique
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.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
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
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
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
YuZhi Qin et al.
Science China. Life sciences, 53(11), 1307-1314 (2010-11-04)
In this study, we show that CIPK14, a stress responsive CBL-interacting protein kinase gene, is involved in phytochrome A-mediated far-red light inhibition of greening in Arabidopsis seedlings. The CIPK14-impairment mutant cipk14 grown in continuous far-red (FR) light did not show
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