Analytical Data
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Gene name
Ociad1
- Application
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Species
Rat
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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
Q5XIG4
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Expression Region
1-247aa
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Molecular Weight
35.1 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
Ociad1, a member of the OC (overlapping CDS) family, has garnered attention in recent years due to its potential roles in developmental processes and cellular functions. Initially identified in vertebrate systems, Ociad1 has been implicated in various biological pathways, including cell differentiation, apoptosis, and immune response regulation. The research surrounding Ociad1 focuses on its structure and function, as understanding its protein interactions and signaling mechanisms could reveal insights into its regulatory roles in both normal physiology and disease states. Abnormal expression of Ociad1 has been linked to several pathologies, including cancer and autoimmune disorders, prompting scientists to explore its potential as a biomarker and therapeutic target. Current studies aim to elucidate the molecular mechanisms by which Ociad1 exerts its effects, leveraging advanced techniques such as recombinant protein expression and functional assays. By dissecting the complexities of Ociad1’s interactions within cellular environments, researchers hope to uncover novel approaches for manipulating its activity, thus paving the way for potential clinical applications. This burgeoning field of study not only enhances our understanding of Ociad1’s intrinsic biological functions but also contributes to the broader quest for effective treatments for diseases associated with its dysregulation.
