High-Purity β-Nicotinamide adenine dinucleotide (NAD+)-Cellullar energy&anti-aging coenzyme for advanced formulations

Nicotinamide adenine dinucleotide (abbreviated as NAD), also known as diphosphopyridine nucleotide (abbreviated as DPN), or coenzyme I or coenzyme I. In mammals, there are two states of NAD: the oxidized form (NAD+) and the reduced form (NADH). The oxidized form (NAD+) has the maximum ultraviolet absorption spectrum at 260 nm. Through various deaminases, it accepts a hydrogen atom and an electron from the substrate, transforming into the reduced form (NADH) at 340 nm, which has the maximum absorption. β-Nicotinamide adenine dinucleotide is used as a coenzyme in redox reactions, serves as the donor of the ADP ribosyl group in ADP ribosylation reactions, and also acts as the precursor of the second messenger molecule cyclic ADP ribose. β-Nicotinamide adenine dinucleotide also acts as a substrate for bacterial DNA ligases and a group of enzymes called sirtuins, which use NAD+ to remove acetyl groups from proteins.

It is an essential coenzyme within the body, used in biochemical research, clinical diagnosis, clinical medication and drug research.
Nicotinamide adenine dinucleotide is a type of coenzyme drug. Clinically, it is mainly used for the auxiliary treatment of coronary heart disease, which can alleviate symptoms such as chest tightness and angina pectoris. Adverse reactions are occasionally manifested as dry mouth, dizziness, nausea, etc.
It participates in the energy metabolism and substance metabolism within the body, facilitating the repair and renewal of cells. It is used for the treatment of conditions such as coronary heart disease, myocarditis, and leukopenia.
Nicotinamide adenine dinucleotide is a coenzyme that transfers protons (more accurately, hydrogen ions). It appears in many metabolic reactions within cells. NADH or more precisely NADH+H+ is its reduced form. It can be reduced and can carry up to two protons (written as NADH+H+). NAD+ is the coenzyme of dehydrogenases, such as alcohol dehydrogenase (ADH), used for oxidizing ethanol. It plays an irreplaceable role in glycolysis, gluconeogenesis, the tricarboxylic acid cycle, and the respiratory chain. Intermediate products transfer the released hydrogen to NAD, converting it into NADH+H+. And NADH+H+ acts as a hydrogen carrier, synthesizing ATP through a chemical permeation coupling process in the respiratory chain. In terms of absorption, NADH+H+ has absorption peaks at 260nm and 340nm, while NAD+ has only one absorption peak at 260nm. This is an important attribute that distinguishes the two. This is also an important physical basis for many metabolic experiments to measure metabolic rates. The absorption coefficient of NAD at 260nm is 1.78*104 L/(mol*cm), while the absorption coefficient of NADH at 340nm is 6.2*10³ L/(mol*cm).

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• Nicotinamide adenine dinucleotide (NAD+) is involved in various physiological activities such as cellular substance metabolism, energy synthesis, and DNA repair of cells, and plays an important role in the body's immune function. Under healthy conditions, the concentration of NAD+ in the human body is stable, maintaining the normal functions of various cells. The concentration of NAD+ in the body determines the process and degree of cell aging, and a decrease in concentration accelerates the process of cell aging. Studies have shown that NAD+ has a protective effect on renal infarction caused by ischemic surgery, significantly reducing the levels of urea nitrogen and creatinine in the serum; NAD+ has a protective effect on renal tubular damage caused by ischemic surgery. NAD+ (nicotinamide adenine dinucleotide, abbreviated as NAD+) can effectively protect renal ischemia-induced renal damage, and NAD+ has important application value in the preparation of drugs for treating renal ischemic injury. In addition, NAD+ has certain application in the preparation of drugs for treating inflammatory pain. NAD+ participates in regulating formalin and complete Freund's adjuvant (CFA)-induced inflammatory pain through the NAD+-dependent deacetylases SIRT1 and SIRT2, and SIRT1 and SIRT2 participate in the inhibition of NAD+ on inflammatory pain through different mechanisms, thereby achieving the analgesic effect on inflammatory pain.