recombinant
expressed in baculovirus infected Sf9 cells
assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
378-512 nmol/min·mg
mol wt
~99 kDa
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PDE1C(5137)
General description
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.
Physical form
Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
Preparation Note
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
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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