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N2783

Sigma-Aldrich

Nitric Oxide Synthase, Inducible from mouse

recombinant, expressed in E. coli, buffered aqueous solution

Szinonimák:

Inducible Nitric Oxide Synthase, NOS II, iNOS, macNOS

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)

About This Item

Enzyme Commission szám:
1.14.13.39 (BRENDA, IUBMB)
MDL-szám:
MFCD00803363
UNSPSC kód:
12352303
NACRES:
NA.32

rekombináns

expressed in E. coli

Minőségi szint

200

form

buffered aqueous solution

specifikus aktivitás

≥4.0 units/mg protein

molekulatömeg

130 kDa (homodimer)
 130 kDa (subunit, homodimer)

UniProt elérési szám

P29477

kiszállítva

dry ice

tárolási hőmérséklet

−70°C

Géninformáció

mouse ... Nos2(18126)

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Általános leírás

Inducible nitric oxide synthase (iNOS), also known as inflammatory nitric oxide synthase, is a calcium independent isoenzyme, involved in synthesis of nitric oxide (NO). It is a soluble enzyme encoded by the gene mapped to mouse chromosome 11. iNOS is active in dimeric form and its activity is induced by cytokines and various other stimuli. iNOS is expressed in various inflammatory conditions.

Alkalmazás

Nitric Oxide Synthase, Inducible from mouse has been used in immunohistochemical studies. It is also used to evaluate the therapeutic efficacy of inducible nitric oxide synthase (NOS) on reperfusion-induced microcirculatory alterations and hemodynamic adverse effects in the microvasculature of skeletal muscle.

Biokémiai/fiziológiai hatások

Tumor-derived inducible nitric oxide synthase (iNOS) plays a vital role in stimulating tumor growth and vessel maturation. Therefore, it is considered to be a potential therapeutic target for anti-vascular cancer therapies. Unchecked activity of iNOS leads to overproduction of nitric oxide (NO), which is toxic for living cells. iNOS activity can be controlled at both transcription and translational level by regulating protein stability, dimerization, phosphorylation, cofactor binding and availability of oxygen and L-arginine as substrates. iNOS plays a vital role in excisional wound repair and exhibits gene therapy strategy to advance wound healing process in iNOS-deficient conditions such as diabetes and steroid treatment.
NOS is responsible for the biosynthesis of nitric oxide from L-arginine. iNOS is not calcium/calmodulin dependent and has a Km = 16 μM for L-arginine.

Egység definíció

One unit will produce 1.0 μmol of nitric oxide per minute at 37 °C in 50 mM HEPES, pH 7.4, containing 1 mM arginine, 1 mM magnesium acetate, 0.15 mM NADPH, 4.5 μM oxyhemoglobin, 18 μM tetrahydrobiopterin and 180 μM DTT.

Fizikai forma

Solution in 50 mM HEPES, pH 7.4, with 10% glycerol, 8 μM tetrahydrobiopterin

Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

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Dokumentumtár megtekintése

Mapping of the gene for inducible nitric oxide (NO) synthase of mouse macrophages to chromosome 11, close to Evi-2, nu, and Idd-4.
Jenkins NA
Genomics, 19(2), 402-404 (1994)
Investigating the role of tumour cell derived iNOS on tumour growth and vasculature in vivo using a tetracycline regulated expression system.
Papaevangelou E
International Journal of Cancer. Journal International Du Cancer, 138(11), 2678-2687 (2016)
Reversal of impaired wound repair in iNOS-deficient mice by topical adenoviral-mediated iNOS gene transfer.
Yamasaki K
The Journal of Clinical Investigation, 101(5), 967-971 (1998)
Nitric oxide and nitric oxide synthase during
early lactation in water buffalo dams
M.E. Pero
Rev. Med. Vet. (Toulouse), 157, 16-19 (2006)
P A Marsden et al.
FEBS letters, 307(3), 287-293 (1992-08-03)
The constitutive calcium/calmodulin-dependent nitric oxide (NO) synthase expressed in vascular endothelium shares common biochemical and pharmacologic properties with neuronal NO synthase. However, recent cloning and molecular characterization of NO synthase from bovine endothelial cells indicated the existence of a family
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