Analytical Data
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Gene name
ALDH9A1
- Application
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Alternative Names
ALDH9A1；ALDH4；ALDH7；ALDH9；4-trimethylaminobutyraldehyde dehydrogenase
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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
P49189
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Expression Region
1-494aa
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AA Sequence
MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKE VNLAVQNAKAAFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNG KSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAG VPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKIMEMSAKGIKP VTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEI LDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQG AKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSIL SFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNV SPVELPFGGYKKSGFGRENGRVTIEYYSQLKTVCVEMGDVESAF
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Molecular Weight
53.8 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
ALDH9A1, a member of the aldehyde dehydrogenase (ALDH) superfamily, plays a critical role in the metabolism of neurotransmitters and detoxification processes. Its primary function involves the oxidation of aldehydes to their corresponding carboxylic acids, which is essential in mitigating oxidative stress and maintaining cellular homeostasis. Recent studies have highlighted the significance of ALDH9A1 in various physiological and pathological contexts, including its involvement in neurological disorders and metabolic diseases. Mutations or dysregulation of ALDH9A1 have been linked to conditions such as hyperprolinemia, which is characterized by elevated levels of proline and can lead to neurodevelopmental issues. Research into recombinant ALDH9A1 proteins has gained momentum as scientists seek to elucidate the enzyme’s structural biology and catalytic mechanisms. Recombinant production allows for a detailed analysis of the enzyme's active site and substrate interactions, paving the way for potential therapeutic interventions. Moreover, exploring the regulation of ALDH9A1 expression and activity provides insights into its biochemical pathways, further enhancing our understanding of its role in health and disease. The study of recombinant ALDH9A1 can also facilitate the development of pharmacological agents aimed at modulating its activity, thus offering promising avenues for the treatment of related disorders. In summary, the investigation of ALDH9A1 recombinant proteins is of paramount importance for understanding its biological functions and therapeutic potential, making it a focal point in current biochemical and medical research.
