重组
expressed in E. coli
表单
buffered aqueous glycerol solution
比活
350-450 units/mg protein
分子量
160 kDa
运输
dry ice
储存温度
−70°C
生化/生理作用
NOS is responsible for the biosynthesis of nitric oxide from L-arginine in nervous tissues. nNOS is calcium/calmodulin dependent and has a Km = 2.0 μM for L-arginine.
外形
40Mm EPS buffer PH7.5 100mMNaCl, 5% glycerol, 5uM H4B, 100uM L-arginine.
其他说明
One unit of enzyme activity represent the amount of enzyme that produce 1nmole of nitric oxide per minute at 37oC in 40mM Tris-Hcl, or Hepes or EPPs buffer ,PH7.5 containg 5-10 uM Oxyhemoglobin. 1mM NADPH, 2uM FMN/FAD, 5uM H4B , 100uM L-arginine, 50units/ml Catalase, 5units/ml SOD, 0.1mg/ml BSA, 35ul of 9mM EDTA and and 35 ul of 150mg/ml CaM and 12.5mM CaCl2
储存分类代码
12 - Non Combustible Liquids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
常规特殊物品
此项目有
Elena Newman et al.
The Journal of biological chemistry, 279(32), 33547-33557 (2004-05-13)
The interactions of neuronal nitric-oxide synthase (nNOS) with calmodulin (CaM) and mutant forms of CaM, including CaM-troponin C chimeras, have been previously reported, but there has been no comparable investigation of CaM interactions with the other constitutively expressed NOS (cNOS)
H M Abu-Soud et al.
Proceedings of the National Academy of Sciences of the United States of America, 90(22), 10769-10772 (1993-11-15)
Nitric oxide (NO) is synthesized within the immune, vascular, and nervous systems, where it acts as a wide-ranging mediator of mammalian physiology. The NO synthases (EC 1.14.13.39) isolated from neurons or endothelium are calmodulin dependent. Calmodulin binds reversibly to neuronal
L J Roman et al.
Proceedings of the National Academy of Sciences of the United States of America, 92(18), 8428-8432 (1995-08-29)
The neuronal nitric oxide synthase (nNOS) has been successfully overexpressed in Escherichia coli, with average yields of 125-150 nmol (20-24 mg) of enzyme per liter of cells. The cDNA for nNOS was subcloned into the pCW vector under the control
Roman Fedorov et al.
Proceedings of the National Academy of Sciences of the United States of America, 101(16), 5892-5897 (2004-04-09)
The high level of amino acid conservation and structural similarity of the substrate-binding sites of the oxygenase domains of the nitric oxide synthase (NOS) isoforms (eNOSoxy, iNOSoxy, nNOSoxy) make the interpretation of the structural basis of inhibitor isoform specificity a
Dipak K Ghosh et al.
The Journal of biological chemistry, 281(20), 14173-14183 (2006-02-08)
Mammalian nitric-oxide synthases are large modular enzymes that evolved from independently expressed ancestors. Calmodulin-controlled isoforms are signal generators; calmodulin activates electron transfer from NADPH through three reductase domains to an oxygenase domain. Structures of the reductase unit and its homologs
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