Analytical Data
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Gene name
NMNAT3
- Application
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Alternative Names
NMNAT3；Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96T66
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Expression Region
1-252aa
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AA Sequence
MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVN DTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHH HSKLLRSPPQMEGPDHGKALFSTPAAVPELKLLCGADVLKTFQTPNLWKD AHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHLAKEPVQNEI SATYIRRALGQGQSVKYLIPDAVITYIKDHGLYTKGSTWKGKSTQSTEGK TS
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Molecular Weight
30 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Nicotinamide mononucleotide adenylyltransferase 3 (NMNAT3) is a vital enzyme involved in the synthesis of NAD+ (nicotinamide adenine dinucleotide), a cofactor essential for numerous metabolic processes and cellular functions. NMNAT3 specifically catalyzes the conversion of nicotinamide mononucleotide (NMN) to NAD+, primarily localized in the cytoplasm and mitochondria, highlighting its crucial role in maintaining cellular NAD+ levels. Recent research has illuminated the relevance of NMNAT3 in various physiological and pathological contexts, including its involvement in neuroprotection, metabolic disorders, and aging. Studies suggest that diminished NMNAT3 activity can lead to NAD+ depletion, contributing to age-related decline in mitochondrial function and cellular energy metabolism. Consequently, understanding the structure and function of NMNAT3 has gained significant attention, with the aim of elucidating its mechanisms and potential therapeutic implications. Researchers are focusing on characterizing recombinant NMNAT3 proteins to investigate their enzymatic properties, regulatory mechanisms, and interactions with other metabolic pathways. This research is not only crucial for basic science but also offers promising avenues for developing interventions in age-related diseases and other conditions characterized by altered NAD+ homeostasis. By producing recombinant NMNAT3 for experimental studies, scientists aim to explore its role in NAD+ biosynthesis, helping to pave the way for future therapies geared toward enhancing mitochondrial health and cellular metabolism.
