Nitric Oxide Synthase 1 (Neuronal) (NOS1) (AA 1095-1289) antibody

Antigen: Nitric Oxide Synthase 1 (Neuronal) (NOS1)

Synonyms: NOS, nNOS, IHPS1, INOS, NOS2A, HEP-NOS, NO, bNOS, NOS-I, Nos-1, 2310005C01Rik, iNOS, Nos-2, Nos2a, i-NOS, NOS-II, iNos, nos, NOS2, NOS1, nos2

Binding Site: AA 1095-1289

Clonality: Monoclonal (16)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF), Immunohistochemistry (IHC)

Catalog no.: ABIN967894

Additional Information

Alternative name: nNOS/NOS Type I

Immunogen: Human nNOS

Cross-Reactivity: Rat (Rattus), Mouse (Murine), Dog (Canine)

Format: Liquid

Isotype: IgG2a

Clone: 16

Description: Nitric oxide synthase (NOS), a cell-type specific enzyme, catalyzes the synthesis of nitric oxide (NO). NO is a short-lived radical that transmits cellular signals involved in vasorelaxation, neurotransmission, and cytotoxicity. In neurons and endothelial cells, constitutive NOS (cNOS) is activated by agonists that increase intracellular Ca2+ levels and enhance calmodulin binding. Neuronal NOS (nNOS or bNOS) and endothelial NOS (ECNOS) have recognition sites for NADPH, FAD, FMN, and calmodulin and are regulated in a similar manner. However, both have been shown to be distinct gene products of about 155 kDa and 140 kDa, respectively, and the human forms show 52% amino acid identity. Neuronal NOS and induced macrophage NOS (iNOS) share 51% amino acid homology with the greatest degree of divergence in the calmodulin binding domain. Neuronal NOS, a cytosolic protein present mainly in neural tissues, has been purified and characterized from rat cerebellum. The NO synthesized by this enzyme acts as a neurotransmitter. ECNOS has been cloned from human vascular endothelium as well as from bovine aortic endothelial cells (BAEC) and has a unique N-myristylation consensus sequence that may explain its membrane localization. This antibody is routinely tested by western blot analysis.
Synonyms: NOS Type I, Neuronal Nitric Oxide Synthase

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.

Molecular Weight: 155 kDa

Comments:

Related Products: ABIN968545, ABIN967389

Application Details

Concentration: 250 µg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution containing BSA, glycerol.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at -20° C.

Restrictions: For Research Use only

Images

Western blot analysis of nNOS on a rat pituitary lysate. Lane 1: 1:2500, lane 2: 1: 5000, lane 3: 1: 10,000 dilution of the mouse anti-nNOS antibody.

Immunofluorescence staining on a rabbit brain section.

Immunohistochemical staining of a formalin-fixed paraffin-embedded rat brain tissue section with no pre-treatment (20X magnification).

Publications

Product: Nathan: "Nitric oxide as a secretory product of mammalian cells." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 6, Issue 12, pp. 3051-64, 1992 (PubMed).

Bredt, Hwang, Glatt et al.: "Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase." in: Nature, Vol. 351, Issue 6329, pp. 714-8, 1991 (PubMed).

Yu, Shao, Qian et al.: "Gene transfer of the neuronal NO synthase isoform to cirrhotic rat liver ameliorates portal hypertension." in: The Journal of clinical investigation, Vol. 105, Issue 6, pp. 741-8, 2000 (PubMed).

Sasaki, Gonzalez-Zulueta, Huang et al.: "Dynamic regulation of neuronal NO synthase transcription by calcium influx through a CREB family transcription factor-dependent mechanism." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 97, Issue 15, pp. 8617-22, 2000 (PubMed).

Schuh, Uldrijan, Telkamp et al.: "The plasmamembrane calmodulin-dependent calcium pump: a major regulator of nitric oxide synthase I." in: The Journal of cell biology, Vol. 155, Issue 2, pp. 201-5, 2001 (PubMed).