Analytical Data
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Gene name
odh1
- Application
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Alternative Names
(OcDH)
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Species
Pecten maximus
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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
Q9BHM6
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Expression Region
1-399aa
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Molecular Weight
50.8 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
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Protein Description
ODH1 (Octamer-binding Protein 1) is a member of the octamer-binding transcription factor family, recognized for its role in regulating gene expression during cellular differentiation and development. Research into ODH1 has gained traction due to its potential implications in various biological processes and diseases, particularly in relation to stem cell biology and oncogenesis. Abnormal regulation of ODH1 has been linked to certain cancers, making it a subject of interest in cancer research. Recent studies have focused on the protein's structure, function, and interaction with other cellular partners, aiming to elucidate its contributions to growth and differentiation in both normal and pathological states. Additionally, understanding the signaling pathways and molecular mechanisms involving ODH1 could provide new insights into potential therapeutic targets for diseases associated with its dysregulation. The exploration of recombinant ODH1 proteins in various experimental models offers a valuable opportunity to investigate these functions further, thereby paving the way for innovative strategies in regenerative medicine and cancer therapeutics. The significance of ODH1 in transcriptional regulation and cellular processes underscores the importance of continued research in this area, contributing to our overall understanding of gene regulation and its impact on health and disease.
