Analytical Data
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Gene name
Serpine1
- Application
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Alternative Names
Serpine1；PAIRBP1；SERPINE1 mRNA-binding Protein 1；PAI1
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Species
Human
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Source
E. coli
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Tag
N-terminal His-Tag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05121
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Expression Region
His25~Pro402
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AA Sequence
HHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTT GGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQ RDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISN LLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVP MMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSAL TNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFR QFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPE EIIMDRPFLFVVRHNPTGTVLFMGQVMEP
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Molecular Weight
47 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
Serpine1, also known as plasminogen activator inhibitor-1 (PAI-1), is a critical regulatory protein involved in the fibrinolytic system, which controls blood clot dissolution and thus plays a significant role in maintaining hemostasis. Its overexpression is associated with various pathophysiological conditions, including cardiovascular diseases, diabetes, and certain cancers. Research has indicated that elevated levels of Serpine1 can contribute to tissue fibrosis and impaired wound healing, making it a potential biomarker and therapeutic target. The recombinant production of Serpine1 has gained considerable attention, as it enables the study of its functional properties, interactions with other proteins, and its role in disease mechanisms. Additionally, understanding its structure-function relationships through recombinant techniques can facilitate the development of novel therapeutic strategies aimed at modulating its activity. Recent advancements in protein expression systems have made it feasible to produce high-yield, functional Serpine1, providing valuable insights into its biological significance and potential applications in clinical settings. Thus, the study of recombinant Serpine1 not only enhances our understanding of hemostatic regulation but also opens avenues for innovative treatments for related diseases.
