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R8282

Sigma-Aldrich

PRKG1, active, GST tagged human

PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Synonym(s):

CGKI, DKFZp686K042, FLJ36117, MGC71944, PGK

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

recombinant

expressed in baculovirus infected Sf9 cells

Quality Level

product line

PRECISIO® Kinase

Assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

specific activity

663-897 nmol/min·mg

mol wt

~100 kDa

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... PRKG1(5592)

Biochem/physiol Actions

PRKG1 is a homodimer, with each monomer containing a regulatory cGMP-binding domain and a catalytic domain. By Northern blot analysis PRKG1 was shown to be expressed at highest levels in bladder, uterus, adrenal gland, and fallopian tube. PRKG1 plays an important stimulatory role in platelet activation. Expression of recombinant PRKG1 in a reconstituted cell model enhanced von Willebrand factor-induced activation of the platelet integrin alpha-IIb/beta-3. Prkg1 knockout mice showed impaired platelet responses to VWF or low doses of thrombin and prolonged bleeding time. Human platelet aggregation induced by VWF or low-dose thrombin was inhibited by PRKG1 inhibitors but enhanced by cGMP.

Physical form

Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.

Legal Information

PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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S Orstavik et al.
Genomics, 42(2), 311-318 (1997-06-01)
The type I cGMP-dependent protein kinase (cGK) has been shown to play a crucial role in the relaxation of vascular smooth muscle by lowering the intracellular level of calcium. Two isoforms of type I cGK have been described, type I
Zhenyu Li et al.
Cell, 112(1), 77-86 (2003-01-16)
It is currently accepted that cGMP-dependent protein kinase (PKG) inhibits platelet activation. Here, we show that PKG plays an important stimulatory role in platelet activation. Expression of recombinant PKG in a reconstituted cell model enhanced von Willebrand factor (vWF)-induced activation

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