Analytical Data
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Gene name
OIH
- Application
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Alternative Names
OIH；OIH；Ovoinhibitor
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Species
Chicken
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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
P10184
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Expression Region
26-472aa
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AA Sequence
VNCSLYASGIGKDGTSWVACPRNLKPVCGTDGSTYSNECGICLYNREHGANVEKEYDGECRPKHVMIDCSPYLQVVRDGNTMVACPRILKPVCGSDSFTYDNECGICAYNAEHHTNISKLHDGECKLEIGSVDCSKYPSTVSKDGRTLVACPRILSPVCGTDGFTYDNECGICAHNAEQRTHVSKKHDGKCRQEIPEIDCDQYPTRKTTGGKLLVRCPRILLPVCGTDGFTYDNECGICAHNAQHGTEVKKSHDGRCKERSTPLDCTQYLSNTQNGEAITACPFILQEVCGTDGVTYSNDCSLCAHNIELGTSVAKKHDGRCREEVPELDCSKYKTSTLKDGRQVVACTMIYDPVCATNGVTYASECTLCAHNLEQRTNLGKRKNGRCEEDITKEHCREFQKVSPICTMEYVPHCGSDGVTYSNRCFFCNAYVQSNRTLNLVSMAAC
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Molecular Weight
51.2 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 OIH (Oligomeric Insulin-degrading Enzyme Homolog) recombinant proteins has gained significant attention in the field of biochemistry and pharmacology due to their crucial role in insulin regulation and potential implications in metabolic diseases. Insulin, a vital hormone for glucose metabolism, is subjected to regulation by various enzymes, among which OIH has emerged as a key player. Research indicates that OIH is involved in the degradation of insulin, thereby influencing its availability and activity in the body. Abnormalities in OIH function have been linked to insulin resistance and diabetes, prompting scientists to explore recombinant forms of this protein for therapeutic applications. By harnessing advanced techniques in molecular biology, researchers aim to produce OIH in a recombinant form, allowing for detailed studies of its structure, function, and interaction with insulin. This work paves the way for novel therapeutic strategies, including the development of drugs that can modulate OIH activity, ultimately aiming to improve glucose homeostasis in diabetic patients and possibly other metabolic disorders. Understanding the mechanics of OIH and its role in insulin degradation holds promise for addressing the rising prevalence of metabolic diseases globally.
