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Merck
CN
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主要文件

安全信息

SRP0371

Sigma-Aldrich

PKG1alpha active human

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

别名:

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

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About This Item

CAS号:
141588-27-4
UNSPSC代码:
12352200
NACRES:
NA.32

生物来源

human

重组

expressed in baculovirus infected Sf9 cells

方案

≥70% (SDS-PAGE)

表单

aqueous solution

分子量

80 kDa

包装

pkg of 10 μg

储存条件

avoid repeated freeze/thaw cycles

浓度

0.45 mg/mL

技术

activity assay: suitable
inhibition assay: suitable

NCBI登记号

NM_001098512

UniProt登记号

Q13976

运输

dry ice

储存温度

−70°C

基因信息

human ... PRKG1(5592)

一般描述

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.

应用

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

储存分类代码

12 - Non Combustible Liquids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

新产品

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number
4008200519

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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
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

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