Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Companion Products
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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. Other applications were tested in BD Biosciences Pharmingen during antibody development only or reported in the literature.
Development References (5)
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Bredt DS, Hwang PM, Glatt CE, Lowenstein C, Reed RR, Snyder SH. Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase. Nature. 1991; 351(6329):714. (Biology). View Reference
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Nathan C. Nitric oxide as a secretory product of mammalian cells. FASEB J. 1992; 6(12):3051-3064. (Biology). View Reference
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Sasaki M, Gonzalez-Zulueta M, Huang H. Dynamic regulation of neuronal NO synthase transcription by calcium influx through a CREB family transcription factor-dependent mechanism. Proc Natl Acad Sci U S A. 2000; 97(15):8617-8622. (Biology: Immunofluorescence, Western blot). View Reference
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Schuh K, Uldrijan S, Telkamp M, Rothlein N, Neyses L. The plasmamembrane calmodulin-dependent calcium pump: a major regulator of nitric oxide synthase I. J Cell Biol. 2001; 155(2):201-205. (Biology: Immunoprecipitation, Western blot). View Reference
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Yu Q, Shao R, Qian HS, George SE, Rockey DC. Gene transfer of the neuronal NO synthase isoform to cirrhotic rat liver ameliorates portal hypertension. J Clin Invest. 2000; 105(6):741-748. (Biology: Immunohistochemistry, Western blot). View Reference
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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.