Analytical Data
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Gene name
SERPINB12
- Application
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Alternative Names
SERPINB12；Serpin B12
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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
Q96P63
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Expression Region
1-425aa
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AA Sequence
MDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHF NEFSQNESKEPDPCLKSNKQKVLADSSLEGQKKTTEPLDQQAGSLNNESGLVSCYFGQLL SKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQKNPEKSRQEINF WVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDNLKGLEELERKITYEK MVAWSSSENMSEESVVLSFPRFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLY LSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNANHPFLFFIRHNKTQTILFYG RVCSP
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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
SERPINB12, also known as ovalbumin-related protein, is a member of the serine protease inhibitor (serpin) family, which plays crucial roles in various physiological processes, including regulation of proteolytic enzymes and modulation of immune responses. Its expression is notably observed in the epithelial tissues of the respiratory and gastrointestinal tracts, suggesting a potential role in host defense mechanisms. Recent studies have indicated that SERPINB12 may have implications in pathological conditions such as asthma, inflammation, and cancer, where its regulation of protease activity could influence disease progression and severity. Despite its emerging significance, the molecular mechanisms underlying SERPINB12's functions remain poorly understood, highlighting the need for further research. The production of recombinant SERPINB12 protein has become essential for investigating its biochemical properties, identification of potential substrates, and exploration of therapeutic applications. Understanding the structure-function relationship of SERPINB12 through recombinant expression systems allows for the development of targeted strategies in disease intervention, making it a valuable subject of study in both basic and applied biomedical research.
