P0194
Protein Kinase Cζ isozyme human
≥75% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous solution
Sinónimos:
Ca2+-activated phospholipid-dependent serine-threonine kinase ζ isozyme human, PKCζ human
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5 μG
MXP 10,706.00
20 μG
MXP 24,416.00
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5 μG
MXP 10,706.00
20 μG
MXP 24,416.00
About This Item
Productos recomendados
recombinante
expressed in baculovirus infected insect cells
Nivel de calidad
Ensayo
≥75% (SDS-PAGE)
Formulario
buffered aqueous solution
enzyme activity
>800 units/mg protein
mol peso
76-80 kDa by SDS-PAGE
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−70°C
Información sobre el gen
human ... PRKCZ(5590)
Acciones bioquímicas o fisiológicas
PKCζ is a downstream enzyme in insulin signaling pathways.
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.
Idoneidad
PKC ε can transfer 1100 nmole of phosphate to PKC ε substrate peptide per minute per mg of total protein at 30 °C.
Definición de unidad
One unit will transfer 1 nanomole of phosphate to PKC epsilon substrate peptide per minute at pH 7.5 at 30 deg C.
Forma física
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.
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
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
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
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