protein

NAMPT Protein, Mouse (P.pastoris, His)

HY-P701315

20 μg;50 μg;100 μg

250;480;770 USD

NAMPT Protein, Mouse (P.pastoris, His)

proteins

P. pastoris

20 μg;50 μg;100 μg

250;480;770 USD

NAMPT protein has dual functions of cytokine and adipokine. Due to limited ATP activation, its secreted form lacks enzymatic activity. It catalyzes the condensation of nicotinamide and 5-phosphoribosyl-1-pyrophosphate to produce nicotinamide mononucleotide, which is critical for NAD biosynthesis. NAMPT Protein, Mouse (P.pastoris, His) is the recombinant mouse-derived NAMPT protein, expressed by P. pastoris , with N-10*His labeled tag. The total length of NAMPT Protein, Mouse (P.pastoris, His) is 491 a.a., with molecular weight of 57.9 kDa.

Mouse

The NAMPT protein exhibits dual functionality, acting both as a cytokine with immunomodulating properties and as an adipokine with anti-diabetic properties. Interestingly, its secreted form lacks enzymatic activity, attributed in part to the limited activation by ATP in the extracellular space and plasma due to its low levels. Functionally, NAMPT catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate, yielding nicotinamide mononucleotide—an intermediate crucial in the biosynthesis of NAD. As the rate-limiting component in the mammalian NAD biosynthesis pathway, NAMPT plays a pivotal role in modulating circadian clock function. Its NAMPT-dependent oscillatory production of NAD governs the oscillation of clock target gene expression by releasing the core clock component, the CLOCK-BMAL1 heterodimer, from NAD-dependent SIRT1-mediated suppression.

rHuNicotinamide phosphoribosyltransferase/NAMPT, His; Pre-B cell-enhancing factor; Nicotinamide phosphoribosyltransferase; NAmPRTase; Nampt; Pre-B-cell colony-enhancing factor 1; Visfatin; NAMPT; PBEF; PBEF1

Greater than 85% as determined by reducing SDS-PAGE.

Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 0.5 M NaCl, 6%Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.