P1787
Protein Kinase CβI isozyme human
≥95% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution
Synonym(s):
Ca2+-activated phospholipid-dependent serine-threonine kinase, PKCβI
recombinant
expressed in baculovirus infected insect cells
Quality Level
Assay
≥95% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
≥700 units/mg protein
mol wt
apparent mol wt 79-80 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PRKCB(5579)
Biochem/physiol Actions
PKCβΙ is pivotal in controlling T-cell migration.
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.
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.
Other Notes
One unit will transfer 1 nmol of phosphate to histone H1 in 1 min at pH 7.4 at 30 °C.
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
Regulatory Information
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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
Oliver Batistic et al.
The Plant journal : for cell and molecular biology, 61(2), 211-222 (2009-10-17)
During adaptation and developmental processes cells respond through nonlinear calcium-decoding signaling cascades, the principal components of which have been identified. However, the molecular mechanisms generating specificity of cellular responses remain poorly understood. Calcineurin B-like (CBL) proteins contribute to decoding calcium
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
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
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