Analytical Data
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Gene name
ASPHD1
- Application
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Alternative Names
ASPHD1；Aspartate beta-hydroxylase domain-containing Protein 1
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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
Q5U4P2
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Expression Region
1-390aa
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AA Sequence
MKEGRGSFSVERGPRKERETAQSGMWKGNSPAGSQGAAMEGTGGELGGQGNWGPEDAPGLLARASLIMLPWPLPLASSALTLLFGALTSLFLWYCYRLGSQDMQALGAGSRAGGVRGGPVGCSEAGGPSPGGPGDPGEGPRTEGLVSRRLRAYARRYSWAGMGRVRRAAQGGPGPGRGPGVLGIQRPGLLFLPDLPSAPFVPRDAQRHDVELLESSFPAILRDFGAVSWDFSGTTPPPRGWSPPLAPGCYQLLLYQAGRCQPSNCRRCPGAYRALRGLRSFMSANTFGNAGFSVLLPGARLEGRCGPTNARVRCHLGLKIPPGCELVVGGEPQCWAEGHCLLVDDSFLHTVAHNGSPEDGPRVVFIVDLWHPNVAGAERQALDFVFAPDP
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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
The study of ASPHD1 (aspartate beta-hydroxylase domain-containing protein 1) recombinant protein is rooted in its potential implications for various biological processes and disorders. ASPHD1 is an enzyme involved in the hydroxylation of aspartate residues in proteins, a modification that can influence protein stability, function, and interactions. This makes it a critical component in post-translational modifications, which are essential for proper cellular functioning. Recent research has indicated that dysregulation of such enzymes could be linked to various diseases, including certain cancers and metabolic disorders. Thus, understanding the structure and function of ASPHD1 is vital for elucidating its role in these pathological conditions. The recombinant expression of ASPHD1 allows for the production of large quantities of the protein, facilitating in vitro studies that can reveal its enzymatic activity, substrate specificity, and potential regulatory mechanisms. Such investigations could further elucidate the biological pathways in which ASPHD1 is involved, paving the way for novel therapeutic strategies that target its function. The recombinant protein also serves as a valuable tool for the development of assays that can screen for inhibitors or modulators of its activity, potentially leading to breakthroughs in the treatment of diseases associated with ASPHD1 dysregulation. Consequently, the exploration of ASPHD1 recombinant protein holds significant promise for advancing our understanding of fundamental biological processes and improving clinical outcomes in related disorders.
