Analytical Data
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Gene name
OC
- Application
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Alternative Names
OC；PLA2L；Otoconin-90
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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
Q16625
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Expression Region
1-522aa
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AA Sequence
MSSRPLESPPPYRPDEFKPNHYAPSNDIYGGEMHVRPMLSQPAYSFYPED EILHFYKWTSPPGVIRILSMLIIVMCIAIFACVASTLAWDRGYGTSLLGG SVGYPYGGSGFGSYGSGYGYGYGYGYGYGGYTDPRAAKGFMLAMAAFCFI AALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPT AQSSGSLYGSQIYALCNQFYTPAATGLYVDQYSYHYCVVDPQEAIAIVLG FMIIVAFALIIFFAVKTRRKMDRYDKSNILWDKEHIYDEQPPNVEEWVKN VSAGTQDVPSPPSDYVERVDSPMAYSSNGKVNDKRFYPESSYKSTPVPEV VQELPLTSPVDDFRQPRYSSGGNFETPSKRAPAKGRAGRSKRTEQDHYET DYTTGGESCDELEEDWIREYPPITSDQQRQLYKRNFDTGLQEYKSLQSEL DEINKELSRLDKELDDYREESEEYMAAADEYNRLKQVKGSADYKSKKNHC KQLKSKLSHIKKMVGDYDRQKT
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Molecular Weight
84 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
The study of optically active (OC) recombinant proteins has gained significant interest in the fields of biotechnology, pharmaceuticals, and structural biology due to their potential applications in therapeutic development and diagnostic tools. Recombinant proteins, produced through genetic engineering techniques, allow for the mass production of proteins with specific desired properties, including enhanced stability, activity, and specificity. OC proteins, which possess unique optical properties, can be utilized in various bioimaging applications and are essential for understanding protein interactions and mechanisms within biological systems. The increasing demand for biopharmaceuticals and the advancement of more efficient production methodologies, such as cell-free systems and yeast expression systems, have facilitated the exploration of OC recombinant proteins. This research focuses on optimizing expression systems, improving purification processes, and characterizing the biochemical properties of these proteins. Moreover, the ability to manipulate the optical characteristics of these proteins opens new avenues for their use in real-time monitoring of cellular processes, drug delivery systems, and biosensors. Overall, the exploration of OC recombinant proteins represents a promising frontier in protein science, with the potential to contribute to innovative solutions for various industrial and medical challenges.
