NAD+ - CAS 53-84-9
Catalog number: B0084-094034
Category: Inhibitor
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NAD+ is a coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It plays a role in the activity of several enzymes, such as poly(ADP)-ribose polymerases and cADP-ribose synthases. NAD+ is commonly used as an oxidizing agent.
Nutritional supplement in health care products.
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Catalog Number Size Price Stock Quantity
B0084-094034 10 g $197 In stock
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Brife Description:
coenzyme, oxidizing agent
Nadide; Coenzyme I; Beta-NAD; Diphosphopyridine nucleotide
Ingredient of health care products.
Canonical SMILES:
Brand MD1. Free Radic Biol Med. 2016 Apr 13. pii: S0891-5849(16)30021-1. doi: 10.1016/j.freeradbiomed.2016.04.001. [Epub ahead of print]
This review examines the generation of reactive oxygen species by mammalian mitochondria, and the status of different sites of production in redox signaling and pathology. Eleven distinct mitochondrial sites associated with substrate oxidation and oxidative phosphorylation leak electrons to oxygen to produce superoxide or hydrogen peroxide: oxoacid dehydrogenase complexes that feed electrons to NAD+; respiratory complexes I and III, and dehydrogenases, including complex II, that use ubiquinone as acceptor. The topologies, capacities, and substrate dependences of each site have recently clarified. Complex III and mitochondrial glycerol 3-phosphate dehydrogenase generate superoxide to the external side of the mitochondrial inner membrane as well as the matrix, the other sites generate superoxide and/or hydrogen peroxide exclusively in the matrix. These different site-specific topologies are important for redox signaling. The net rate of superoxide or hydrogen peroxide generation depends on the substrates present and the antioxidant systems active in the matrix and cytosol.
2.Expression patterns of sirtuin 1-AMPK-autophagy pathway in chronic colitis and inflammation-associated colon neoplasia in IL-10-deficient mice.
Talero E1, Alcaide A2, Ávila-Román J2, García-Mauriño S3, Vendramini-Costa D4, Motilva V2. Int Immunopharmacol. 2016 Apr 13;35:248-256. doi: 10.1016/j.intimp.2016.03.046. [Epub ahead of print]
BACKGROUND: Interleukin-10-deficient (IL-10 (-/-)) mice spontaneously develop chronic colitis and adenocarcinoma through the dysplasia sequence. Autophagy malfunction is associated to inflammatory bowel disease (IBD) and colorectal cancer (CRC) pathogenesis. Autophagy is regulated by silent information regulator-1 (SIRT1), a NAD+-dependent histone deacetylase. Our aim was to investigate the expression changes of SIRT1-AMPK-autophagy pathway in the progression from chronic colitis to CRC.
3.Roles of NAD in Protection of Axon against Degeneration via SIRT1 Pathways.
Zhang J1, Guo WH2, Qi XX1, Li GB1, Hu YL1, Wu Q1, Ding ZX1, Li HY1, Hao J3, Sun JH1. Chin J Physiol. 2016 Apr 30;59(2). pii: CJP.2016.BAD331. doi: 10.4077/CJP.2016.BAD331. [Epub ahead of print]
Axonal degeneration is a common pathological change of neurogenical disease which often arises before the neuron death. But it had not found any effective method to protect axon from degeneration. In this study we intended to confirm the protective effect of NAD, investigate the optimal administration dosage and time of NAD, and identify the relationship between SIRT1 and axonal degeneration. An axonal degeneration model was established using DRG neurons injured by vincristine to observe the protective effects of NAD to the injured axons. In addition, the potential contribution of the SIRT1 in axonal degeneration was also investigated. Through the MTT assay, immunochemistry staining, axons counting and length measuring, transmission electron microscope observation, we demonstrated that NAD played an important role in preventing axonal degeneration. Further study revealed that the expression of SIRT1 and p-Akt1 was up-regulated when NAD was added into the culturing medium.
4.SIRT1 is a critical regulator of K562 cell growth, survival, and differentiation.
Duncan MT1, DeLuca TA1, Kuo HY2, Yi M3, Mrksich M4, Miller WM5. Exp Cell Res. 2016 Apr 13. pii: S0014-4827(16)30085-4. doi: 10.1016/j.yexcr.2016.04.010. [Epub ahead of print]
Inhibition of histone deacetylases (HDACi) has emerged as a promising approach in the treatment of many types of cancer, including leukemias. Among the HDACs, Class III HDACs, also known as sirtuins (SIRTs), are unique in that their function is directly related to the cell's metabolic state through their dependency on the co-factor NAD+. In this study, we examined the relation between SIRTs and the growth, survival, and differentiation of K562 erythroleukemia cells. Using a mass spectrometry approach we previously developed, we show that SIRT expression and deacetylase activity in these cells changes greatly with differentiation state (undifferentiated vs. megakaryocytic differentiation vs. erythroid differentiation). Moreover, SIRT1 is crucially involved in regulating the differentiation state. Overexpression of wildtype (but not deacetylase mutant) SIRT1 resulted in upregulation of glycophorin A,~2-fold increase in the mRNA levels of α, γ, ε, and ζ-globins, and spontaneous hemoglobinization.
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CAS 53-84-9 NAD+

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