P3287
Protein kinase CβII isozyme human
>85% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution
Sinónimos:
Ca2+-activated phospholipid-dependent serine-threonine kinase βII isozyme human, PKC βII human
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About This Item
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32
Productos recomendados
recombinant
expressed in baculovirus infected insect cells
assay
>85% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
≥500 unit/mg solid
mol wt
80 kDa by SDS-PAGE
calculated mol wt 76.9 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PRKCB(5579)
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.
Unit Definition
One unit will transfer 1 nmol of phosphate to histone H3 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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Małgorzata Beręsewicz-Haller et al.
International journal of molecular sciences, 22(16) (2021-08-28)
Ischemic episodes are a leading cause of death worldwide with limited therapeutic interventions. The current study explored mitochondrial phosphate-activated glutaminase (GLS1) activity modulation by PKCβII through GC-MS untargeted metabolomics approach. Mitochondria were used to elucidate the endogenous resistance of hippocampal
Yi Liu et al.
The Biochemical journal, 478(10), 1999-2017 (2021-05-08)
Human hepatic tryptophan 2,3-dioxygenase (hTDO) is a homotetrameric hemoprotein. It is one of the most rapidly degraded liver proteins with a half-life (t1/2) of ∼2.3 h, relative to an average t1/2 of ∼2-3 days for total liver protein. The molecular mechanism
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
Cecilia D'Angelo et al.
The Plant journal : for cell and molecular biology, 48(6), 857-872 (2006-11-10)
Intracellular release of calcium ions belongs to the earliest events in cellular stress perception. The molecular mechanisms integrating signals from different environmental cues and translating them into an optimized response are largely unknown. We report here the functional characterization of
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
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