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)
Certificats d'analyse (COA)
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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
Yahui Li et al.
Molecular human reproduction, 17(1), 42-56 (2010-08-24)
Members of the testis-specific serine/threonine kinases (Tssk) family may have a role in sperm differentiation in the testis and/or fertilization. To gain insight into the functional relevance of these kinases, their expression was examined both at the mRNA and protein
Bingfang Xu et al.
Developmental biology, 319(2), 211-222 (2008-06-06)
Targeted deletion of Tssk1 and 2 resulted in male chimeras which produced sperm/spermatogenic cells bearing the mutant allele, however this allele was never transmitted to offspring, indicating infertility due to haploinsufficiency. Morphological defects in chimeras included failure to form elongated
Nichole Link et al.
The Journal of cell biology, 178(4), 567-574 (2007-08-08)
We examined post-eclosion elimination of the Drosophila wing epithelium in vivo where collective "suicide waves" promote sudden, coordinated death of epithelial sheets without a final engulfment step. Like apoptosis in earlier developmental stages, this unique communal form of cell death
Mayuko Akaboshi et al.
Journal of molecular biology, 377(1), 246-257 (2008-02-02)
Calcium signals mediate a multitude of plant responses to external stimuli. Calcineurin B-like (CBL) proteins and their target kinases, CBL-interacting protein kinases (CIPKs), represent important relays in plant calcium signaling. CBL interacts with CIPK through a conserved motif (NAF/FISL motif)
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