Analytical Data
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Gene name
SERPINI2
- Application
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Alternative Names
SERPINI2；MEPI；PI14；；Serpin I2
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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
O75830
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Expression Region
1-405aa
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AA Sequence
MDTIFLWSLL LLFFGSQASR CSAQKNTEFA VDLYQEVSLS HKDNIIFSPL GITLVLEMVQ LGAKGKAQQQ IRQTLKQQET SAGEEFFVLK SFFSAISEKK QEFTFNLANA LYLQEGFTVK EQYLHGNKEF FQSAIKLVDF QDAKACAEMI STWVERKTDG KIKDMFSGEE FGPLTRLVLV NAIYFKGDWK QKFRKEDTQL INFTKKNGST VKIPMMKALL RTKYGYFSES SLNYQVLELS YKGDEFSLII ILPAEGMDIE EVEKLITAQQ ILKWLSEMQE EEVEISLPRF KVEQKVDFKD VLYSLNITEI FSGGCDLSGI TDSSEVYVSQ VTQKVFFEIN EDGSEAATST GIHIPVIMSL AQSQFIANHP FLFIMKHNPT ESILFMGRVT NPDTQEIKGR DLDSL
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Molecular Weight
46 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
SERPINI2, a member of the serpin superfamily, has garnered attention due to its potential role in various biological processes, including inflammation and cell apoptosis. Research indicates that SERPINI2 may function as a serine protease inhibitor, regulating proteins involved in these critical pathways. Dysregulation of SERPINI2 has been implicated in several pathological conditions, including neurodegenerative diseases and cancer, making it a candidate for therapeutic targeting. Its expression pattern in different tissues and during development suggests that it may play essential roles in tissue homeostasis. The recombinant expression of SERPINI2 allows for detailed studies of its structure-function relationships and biological activity, which can provide insights into its mechanism of action. Moreover, understanding the regulatory mechanisms governing SERPINI2 has the potential to unveil novel approaches for intervention in diseases where this protein is involved. As such, the recombinant production of SERPINI2 is pivotal not only for academic research but also for the development of future therapeutics aimed at mitigating its dysregulation-associated disorders.
