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Merck
CN

N4915

Sigma-Aldrich

Nitric Oxide Synthase Neuronal Human

recombinant, expressed in E. coli

Synonym(s):

NOS, nNOS

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About This Item

UNSPSC Code:
12352200
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recombinant

expressed in E. coli

form

buffered aqueous glycerol solution

specific activity

350-450 units/mg protein

mol wt

160 kDa

shipped in

dry ice

storage temp.

−70°C

Biochem/physiol Actions

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.

Physical form

40Mm EPS buffer PH7.5 100mMNaCl, 5% glycerol, 5uM H4B, 100uM L-arginine.

Other Notes

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

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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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
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
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

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