Analytical Data
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Gene name
Aspdh
- Application
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Alternative Names
Aspdh；Aspartate dehydrogenase domain-containing Protein
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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
A6ND91
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Expression Region
1-283aa
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AA Sequence
MADRGPWRVG VVGYGRLGQS LVSRLLAQGP ELGLELVFVW NRDPGRMAGS VPPSLQLQNL AALGERRPDL VVEVAHPKII HESGAQILRH ANLLVGSPSA LSDQTTERQL LEASQHWDHA VFVARGALWG AEDIRRLDAA GGLRSLRVTM ATHPDGFRLE GPLAAAHSPG PCTVLYEGPV RGLCPFAPRN SNTMAAAALA APSLGFDGVI GVLVADTSLT DMHVVDVELS GPRGPTGRSF AVHTRRENPA EPGAVTGSAT VTAFWQSLLA CCQLPSRPGI HLC
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Molecular Weight
29.9 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
Aspdh (Asparagine dehydrogenase) is an enzyme that belongs to the family of dehydrogenases, playing a crucial role in amino acid metabolism, particularly in the oxidative deamination of asparagine to aspartate. This enzymatic activity is vital for various biological processes, including nitrogen metabolism and neural function. The study of Aspdh recombinant proteins has garnered attention due to their potential applications in biotechnology and medicine, especially in understanding metabolic disorders and developing novel therapeutic strategies. Recent advancements in recombinant DNA technology have enabled the expression and purification of Aspdh, allowing for detailed biochemical characterization and functional studies. These investigations aim to elucidate the enzyme's structure-function relationship, regulatory mechanisms, and implications in disease states, such as cancer and neurodegenerative disorders. By harnessing Aspdh recombinant proteins, researchers aspire to develop targeted interventions that could modulate asparagine levels in pathological conditions, potentially paving the way for innovative treatments. The ongoing research into Aspdh not only enhances our understanding of amino acid metabolism but also contributes to the broader field of metabolic engineering, offering insights that could lead to the development of engineered strains for industrial applications or therapeutic agents for clinical use.
