Analytical Data
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Gene name
NMNAT3
- Application
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Alternative Names
Nicotinamide-nucleotide adenylyltransferase 3 ;NMN adenylyltransferase 3Nicotinate-nucleotide adenylyltransferase 3 (EC:2.7.7.18) ;NaMN adenylyltransferase 3;Pyridine nucleotide adenylyltransferase 3 (EC:2.7.7.1) ;PNAT-3
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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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
1-215aa
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Molecular Weight
40.1 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 crucial enzyme involved in the synthesis of NAD+ (nicotinamide adenine dinucleotide), a vital cofactor in cellular metabolism and energy production. The role of NMNAT3 is particularly significant in maintaining NAD+ homeostasis in various tissues, including the brain and muscle. Research has indicated that NMNAT3 deficits are associated with neurodegenerative diseases and metabolic disorders, highlighting its potential as a therapeutic target. The production of recombinant NMNAT3 protein allows for detailed biochemical studies, enabling researchers to explore its enzymatic properties, regulation, and interactions with other metabolic pathways. Understanding the structure-function relationship of NMNAT3 through the use of recombinant proteins could lead to novel strategies for enhancing NAD+ levels in cells, thereby improving cellular health and potentially mitigating age-related decline and metabolic diseases. Additionally, the recombinant NMNAT3 can be utilized in drug discovery efforts, facilitating the identification of compounds that can modulate its activity. As a result, the study of NMNAT3 at the molecular level is pivotal for developing therapeutic interventions aimed at enhancing NAD+ metabolism and addressing various health issues related to age and metabolic dysfunctions.
