N4915
Nitric Oxide Synthase Neuronal Human
recombinant, expressed in E. coli
Synonym(s):
NOS, nNOS
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About This Item
UNSPSC Code:
12352200
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.
Unit Definition
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
Physical form
40Mm EPS buffer PH7.5 100mMNaCl, 5% glycerol, 5uM H4B, 100uM L-arginine.
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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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
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
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)
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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