Protein Kinase Cδ isozyme human

>95% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution

Ca2+-activated phospholipid-dependent serine-threonine kinase δ isozyme human, PKCδ human
Enzyme Commission number:
MDL number:

Quality Level


expressed in baculovirus infected insect cells


>95% (SDS-PAGE)


buffered aqueous glycerol solution

mol wt

74-79 kDa by SDS-PAGE

UniProt accession no.

shipped in

dry ice

storage temp.


Gene Information

human ... PRKCD(5580)

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.

Unit Definition

One unit will transfer 1 nmol of phosphate to PKC epsilon substrate peptide 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.


10 - Combustible liquids

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

Certificate of Analysis

Certificate of Origin

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...
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...
Jianbin Peng et al.
Biochimica et biophysica acta, 1759(11-12), 562-572 (2006-11-25)
Ser/Thr- and Tyr-Protein kinases constitute a key switch underlying the dynamic nature and graded regulation of signal transduction and pathway activities in cellular organization. Here we describe the identification and characterization of Dusty, a single-copy gene that arose in metazoan...
Sung Chul Lee et al.
Proceedings of the National Academy of Sciences of the United States of America, 104(40), 15959-15964 (2007-09-28)
Potassium (K(+)) is an essential nutrient for plant growth and development. Plants often adapt to low K(+) conditions by increasing their K(+) uptake capability. Recent studies have led to the identification of a calcium signaling pathway that enables plants to...

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