Analytical Data
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Gene name
OCM
- Application
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Alternative Names
OCM；OCM1；OCMN；Oncomodulin-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
P0CE72
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Expression Region
2-109aa
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AA Sequence
MKHHHHHHASITDVLSADDIAAALQECRDPDTFEPQKFFQTSGLSKMSAN QVKDVFRFIDNDQSGYLDEEELKFFLQKFESGARELTESETKSLMAAADN DGDGKIGAEEFQEMVHS
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Molecular Weight
13 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
OCM (Oligomeric Cytoplasmic Membrane) proteins are a class of recombinant proteins that have garnered significant attention in the field of molecular biology and biotechnology. These proteins play essential roles in various cellular processes, including membrane integrity, signal transduction, and intercellular communication. The study of OCM recombinant proteins is particularly relevant due to their potential applications in therapeutics, vaccine development, and as biomolecular tools. The ability to express and purify OCM proteins in heterologous systems, such as bacteria, yeast, or mammalian cells, has allowed researchers to investigate their structural and functional properties extensively. Advances in protein engineering, including the use of fusion tags, optimization of expression conditions, and refolding protocols, have enabled scientists to produce these proteins in a more accessible and efficient manner. Furthermore, the elucidation of the mechanistic pathways involving OCM proteins provides insights into their role in various diseases, including cancer and neurodegenerative disorders. As research progresses, the exploration of OCM recombinant proteins continues to pave the way for innovative strategies in drug design and development, highlighting their importance in both fundamental research and applied sciences. Overall, the ongoing investigation into OCM proteins underscores the significance of understanding complex biological molecules and their potential applications in improving human health and disease management.
