NMNAT1 Mouse
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, NMNAT1, NMN/NaMN adenylyltransferase 1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, D4Cole1e, Nmnat.
Greater than 95.0% as determined by SDS-PAGE.
Description
NMNAT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285 a.a) and having a molecular mass of 34.7kDa. NMNAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, NMNAT1, NMN/NaMN adenylyltransferase 1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, D4Cole1e, Nmnat.
MGSSHHHHHH SSGLVPRGSH MGSMDSSKKT EVVLLACGSF NPITNMHLRL FELAKDYMHA TGKYSVIKGI ISPVGDAYKK KGLIPAHHRI IMAELATKNS HWVEVDTWES LQKEWVETVK VLRYHQEKLA TGSCSYPQSS PALEKPGRKR KWADQKQDSS PQKPQEPKPT GVPKVKLLCG ITNDISSTKI RRALRRGQSI RYLVPDLVQE YIEKHELYNT ESEGRNAGVT LAPLQRNAAE AKHNHSTL.
Product Science Overview
Nicotinamide Nucleotide Adenylyltransferase 1 (NMNAT1) is an enzyme that plays a crucial role in the biosynthesis of nicotinamide adenine dinucleotide (NAD+), a vital coenzyme in cellular metabolism. NMNAT1 is one of several nicotinamide nucleotide adenylyltransferases and is specifically localized to the cell nucleus . The recombinant form of NMNAT1, derived from mice, has been extensively studied for its potential therapeutic applications.
NMNAT1 catalyzes the formation of NAD+ from nicotinamide mononucleotide (NMN) and ATP . This reaction is essential for maintaining cellular NAD+ levels, which are critical for various metabolic processes, including DNA repair, gene expression, and cell signaling. The enzyme’s activity leads to the activation of nuclear deacetylases, such as SIRT1, which play a protective role in damaged neurons .
Recent studies have highlighted the neuroprotective properties of NMNAT1. For instance, recombinant human NMNAT1 (rh-NMNAT1) has been shown to reduce infarct volume, improve functional outcomes, and decrease blood-brain barrier (BBB) permeability in mice after ischemic stroke . This protective effect is mediated through the NAD+/SIRT1 signaling pathway, which helps maintain BBB integrity and reduce cell apoptosis in ischemic microvessels .
Additionally, NMNAT1 has been associated with various diseases. Mutations in the NMNAT1 gene have been linked to Leber congenital amaurosis 9, a severe retinal dystrophy that leads to early-onset blindness . The enzyme’s role in NAD+ biosynthesis makes it a potential target for therapeutic interventions in neurodegenerative diseases and other conditions associated with NAD+ deficiency.
