P3287
Protein kinase CβII isozyme human
>85% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution
Synonym(s):
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
Recommended Products
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 Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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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
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
YuZhi Qin et al.
Science in China. Series C, Life sciences, 51(5), 391-401 (2008-09-13)
Calcium and protein kinase serve as the common mediators to regulate plant responses to multiple stresses including salt and ABA stimulus. Here we reported a novel protein kinase (CIPK14) that regulated the responses to ABA treatment and salt stress in
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