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P3738

Sigma-Aldrich

Protein Kinase G Iβ human

≥95% (SDS-PAGE), recombinant, expressed in baculovirus infected Sf9 cells, buffered aqueous glycerol solution

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Synonym(s):
cyclic-Guanosine Monophosphate-dependent Protein Kinase 1β human
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in baculovirus infected Sf9 cells

Quality Level

Assay

≥95% (SDS-PAGE)

form

buffered aqueous glycerol solution

specific activity

≥1.5 units/mg protein (20-fold stimulation by cGMP (5 μM))

mol wt

76 kDa (monomer)

UniProt accession no.

relevant disease(s)

cancer

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... PRKG1(5592)

Application

Protein Kinase G is a serine/threonine-specific protein kinase that is activated by cGMP. Protein Kinase G Iβ is used to induce apoptosis and inhibit cell proliferation.

Biochem/physiol Actions

Protein Kinase G Iβ induces apoptosis in certain cell lines such as human breast cancer cell lines MCF-7 and MDA-MB-468. It inhibits cell proliferation and induces apoptosis in colon cancer cell lines.

Unit Definition

One unit will phosphorylate 1 micromole of VASPtide(RRKVSKQE) substrate per minute in 10 mM HEPES, pH 7.4, 5 mM MgCl2, 1 mM DTE and 0.2 mM EDTA.

Physical form

Solution in 20 mM Tris buffer, pH 7.4, 1 mM EDTA, 1 mM β-mercaptoethanol, 100 mM NaCl, 10 U/ml Trasylol, and 50% glycerol.

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Atsuko Deguchi et al.
Cancer research, 65(18), 8442-8447 (2005-09-17)
Recent studies indicate that the induction of apoptosis in human colon cancer cells by certain nonsteroidal antiinflammatory drugs involves increased expression of 15-LOX-1 and synthesis of its major product 13-S-hydroxyoctadecadienoic acid (13-S-HODE). Evidence was obtained that this occurs via a
Faranak Fallahian et al.
Cell biochemistry and function, 30(3), 183-190 (2011-11-19)
Activation of protein kinase G (PKG) by cyclic guanosine 3,5-monophosphate (cGMP) has become of considerable interest as a novel molecular approach for the induction of apoptosis in cancer cells. This study was conducted to investigate the role of PKG isoforms
D Pöhler et al.
FEBS letters, 374(3), 419-425 (1995-11-06)
Detailed studies of differences in distinct cGMP kinase isoforms are highly dependent on expression of large amounts of these enzyme isoforms that are not easily purified by conventional methods. Here cGMP-dependent protein kinases, the type I beta soluble form from

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