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Merck
CN

SRP5057

Sigma-Aldrich

PDE1C, active, GST tagged human

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

别名:

Hcam3

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关于此项目

UNSPSC代码:
12352200
NACRES:
NA.32
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重组

expressed in baculovirus infected Sf9 cells

方案

≥70% (SDS-PAGE)

表单

buffered aqueous glycerol solution

比活

378-512 nmol/min·mg

分子量

~99 kDa

NCBI登记号

运输

dry ice

储存温度

−70°C

基因信息

human ... PDE1C(5137)

一般描述

PDE1C is a member of the phosphodiesterases (PDE) family which catalyzes the hydrolysis of cyclic nucleotides cAMP and cGMP to the corresponding nucleoside 5-prime-monophosphates. PDE1C binds both cAMP and cGMP with high affinity and hydrolyzes both substrates with similar rates of catalysis. PDE1C is a calmodulin-dependent PDE and is stimulated by calcium-calmodulin complex. PDE1C is expressed at high levels in human cardiac myocytes with an intracellular distribution distinct from that of other phosphodiesterases. PDE1C levels decrease in all conditions that inhibited cell proliferation and PDE1C is a useful marker in studying the dynamics of proliferation and migration of various cells.

外形

Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.

制备说明

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

储存分类代码

10 - Combustible liquids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

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分析证书(COA)

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K Loughney et al.
The Journal of biological chemistry, 271(2), 796-806 (1996-01-12)
cDNAs corresponding to two human calcium, calmodulin (CaM)-regulated 3',5'-cyclic nucleotide phosphodiesterases (PDEs) were isolated. One, Hcam1 (PDE1A3), corresponds to the bovine 61-kDa CaM PDE (PDE1A2). The second, Hcam3 (PDE1C), represents a novel phosphodiesterase gene. Hcam1 encodes a 535-amino acid protein
Fabrice Vandeput et al.
The Journal of biological chemistry, 282(45), 32749-32757 (2007-08-30)
Isoforms in the PDE1 family of cyclic nucleotide phosphodiesterases were recently found to comprise a significant portion of the cGMP-inhibited cAMP hydrolytic activity in human hearts. We examined the expression of PDE1 isoforms in human myocardium, characterized their catalytic activity

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