Analytical Data
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Gene name
Aldh3a1
- Application
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Alternative Names
Aldehyde dehydrogenase 4 (Aldehyde dehydrogenase family 3 member A1) (Dioxin-inducible aldehyde dehydrogenase 3)
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P47739
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Expression Region
2-453aa
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Molecular Weight
57.8 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
Aldehyde dehydrogenase 3A1 (ALDH3A1) is a crucial enzyme involved in the detoxification of aldehydes and the metabolism of retinoids. It plays a significant role in cellular protection against oxidative stress by catalyzing the conversion of toxic aldehydes into less harmful carboxylic acids. Given its implications in various physiological and pathological processes, including cancer development, neurodegenerative disorders, and alcohol metabolism, ALDH3A1 has garnered considerable research interest. The overexpression of ALDH3A1 in certain tumors suggests its potential as a biomarker for cancer diagnosis and prognosis. Furthermore, recombinant ALDH3A1 proteins have been produced for studying enzyme kinetics, determining structure-function relationships, and developing therapeutic strategies that target aldehyde detoxification pathways. Understanding the structural properties and catalytic mechanisms of ALDH3A1 through recombinant techniques can further elucidate its biological functions and contribute to novel approaches in treating diseases related to aldehyde accumulation. The ongoing research on ALDH3A1 not only enhances our comprehension of metabolic pathways but also opens new avenues for clinical applications in oncology and other fields where aldehyde toxicity is a concern.
