Analytical Data
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Gene name
nadB
- Application
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Alternative Names
nadB；L-aspartate oxidase
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Species
E.coli
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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
P10902
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Expression Region
1-540aa
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AA Sequence
MNTLPEHSCDVLIIGSGAAGLSLALRLADQHQVIVLSKGPVTEGSTFYAQGGIAAVFDETDSIDSHVEDTLIAGAGICDRHAVEFVASNARSCVQWLIDQGVLFDTHIQPNGEESYHLTREGGHSHRRILHAADATGREVETTLVSKALNHPNIRVLERSNAVDLIVSDKIGLPGTRRVVGAWVWNRNKETVETCHAKAVVLATGGASKVYQYTTNPDISSGDGIAMAWRAGCRVANLEFNQFHPTALYHPQARNFLLTEALRGEGAYLKRPDGTRFMPDFDERGELAPRDIVARAIDHEMKRLGADCMFLDISHKPADFIRQHFPMIYEKLLGLGIDLTQEPVPIVPAAHYTCGGVMVDDHGRTDVEGLYAIGEVSYTGLHGANRMASNSLLECLVYGWSAAEDITRRMPYAHDISTLPPWDESRVENPDERVVIQHNWHELRLFMWDYVGIVRTTKRLERALRRITMLQQEIDEYYAHFRVSNNLLELRNLVQVAELIVRCAMMRKESRGLHFTLDYPELLTHSGPSILSPGNHYINR
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Molecular Weight
67.3 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
NadB, or Nicotinamide adenine dinucleotide (NAD) biosynthetic enzyme, plays a crucial role in the synthesis of NAD, an essential coenzyme involved in numerous biochemical processes, including energy metabolism, DNA repair, and cell signaling. The increasing interest in NadB is linked to its potential implications in health and disease, particularly in cancer, metabolic disorders, and microbial pathogenesis. This enzyme is also a promising target for the development of novel therapeutic agents aimed at modulating NAD levels and influencing related metabolic pathways. Research into recombinant NadB seeks to utilize genetic engineering techniques to produce this enzyme in a more efficient manner, enabling detailed studies of its structure-function relationships and its regulatory mechanisms in various biological contexts. By expressing NadB in heterologous systems, researchers can obtain high yields of functional enzyme for biochemical assays, crystallography, and structure-based drug design. Understanding NadB’s functionality and its role within NAD biosynthesis can pave the way for innovative approaches to treat diseases linked to NAD metabolism, making it a focal point of biochemistry and medicinal chemistry research.
