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nNOS (rat), (recombinant)

ALX-201-854-0010 10 µg 494.00 USD
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Product Details

Alternative Name:Nitric oxide synthase (neuronal), NOS I
MW:~160kDa/subunit; homodimer.
Source:Produced in E. coli. Untagged rat nNOS.
UniProt ID:P29476
Formulation:Liquid. In 50 mM TRIS, pH 7.4, containing 0.1 mM EDTA, 10% glycerol, 100 mM NaCl, 0.1 mM DTT, 10 µM tetrahydrobiopterin.
Purity:≥90% (SDS-PAGE)
Specific Activity:≥500 U/mg. 1 U is defined as the amount of enzyme required to produce 1 nmol of NO (nitric o)xide per minute at 37°C. NO synthesis is measured by the conversion of oxyhemoglobin to methemoglobin.
Shipping:Dry Ice
Long Term Storage:-80°C
Use/Stability:Stable for at least 1 year after receipt when stored at -80°C. Keep stock vial on ice during experiments.
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
Scientific Background:Nitric oxide synthases are a family of enzymes catalyzing the production of nitric oxide (NO) from L-arginine. NO is an important cellular signaling molecule. It helps modulate vascular tone, insulin secretion, airway tone, and peristalsis, and is involved in angiogenesis and neural development. It may function as a retrograde neurotransmitter. Nitric oxide is mediated in mammals by the calcium-calmodulin controlled isoenzymes eNOS (endothelial NOS) and nNOS (neuronal NOS). The inducible isoform, iNOS, is involved in immune response, binds calmodulin at physiologically relevant concentrations, and produces NO as an immune defense mechanism, as NO is a free radical with an unpaired electron. It is the proximate cause of septic shock and may function in autoimmune disease.
Regulatory Status:RUO - Research Use Only

General Literature References

The Oxyhemoglobin Assay: M. Feelisch, et al.; Meth. Nitric Oxide Research 455 (1996),
High-level expression of functional rat neuronal nitric oxide synthase in Escherichia coli: L.J. Roman, et al.; PNAS 92, 8428 (1995), Abstract; Full Text
Nitric oxide synthases reveal a role for calmodulin in controlling electron transfer: H.M. Abu-Soud and D.J. Stuehr; PNAS 90, 10769 (1993), Abstract; Full Text

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