Analytical Data
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Gene name
asd
- Application
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Alternative Names
Aspartate-beta-semialdehyde dehydrogenase
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Species
Legionella pneumophila
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O31219
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Expression Region
1-347aa
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Molecular Weight
41.8 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
Related Products
Protein Description
ASD (Atypical Serine Deaminase) is an enzyme that has garnered significant attention in recent years due to its novel role in amino acid metabolism and potential implications in various biological processes. Its primary function involves the deamination of serine to produce pyruvate and ammonia, linking cellular metabolism to amino acid homeostasis. Research into ASD has revealed its involvement in critical pathways, including those associated with cancer metabolism and neurodegenerative diseases. Abnormal expression levels of ASD have been observed in certain cancer types, suggesting a potential role in tumor progression and malignancy. Furthermore, studies indicate that ASD may influence neurotransmitter synthesis, implicating it in neurological function and disorders. The recombinant protein version of ASD allows for detailed biochemical characterization, including kinetics, substrate specificity, and the investigation of its structural properties. Understanding the functional mechanisms of ASD not only provides insights into its physiological significance but also paves the way for therapeutic development targeting metabolic dysregulation in diseases. As such, ASD and its recombinant protein derivatives represent promising areas of research in the quest for novel biomedical applications.
