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SRP0371

Sigma-Aldrich

PKG1alpha active human

recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE)

Synonym(s):

PRKG1, PRKGR1B, protein kinase, cGMP-dependent, type I

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About This Item

CAS Number:
141588-27-4
UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in baculovirus infected Sf9 cells

Assay

≥70% (SDS-PAGE)

form

aqueous solution

mol wt

80 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

0.45 mg/mL

technique(s)

activity assay: suitable
inhibition assay: suitable

NCBI accession no.

NM_001098512

UniProt accession no.

Q13976

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... PRKG1(5592)

General description

cGMP dependent Human PKG1alpha (GenBank Accession No. NM_001098512), full length with N-terminal His-tag, MW = 80 kDa, expressed in Baculovirus infected Sf9 cell expression system.

Application

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Alok K Sharma et al.
The Journal of biological chemistry, 283(47), 32860-32869 (2008-09-11)
Nitric oxide and nitrovasodilators induce vascular smooth muscle cell relaxation in part by cGMP-dependent protein kinase I (PKG-Ialpha)-mediated activation of myosin phosphatase (MLCP). Mechanistically it has been proposed that protein-protein interactions between the N-terminal leucine zipper (LZ) domain of PKG-Ialpha
Mark J Ranek et al.
Nature communications, 11(1), 5237-5237 (2020-10-22)
Proteotoxicity from insufficient clearance of misfolded/damaged proteins underlies many diseases. Carboxyl terminus of Hsc70-interacting protein (CHIP) is an important regulator of proteostasis in many cells, having E3-ligase and chaperone functions and often directing damaged proteins towards proteasome recycling. While enhancing
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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