Analytical Data
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Gene name
SERPIND1
- Application
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Alternative Names
SERPIND1;HCF2;Heparin cofactor 2
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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
P05546
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Expression Region
20-499aa
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AA Sequence
GSKGPLDQLEKGGETAQSADPQWEQLNNKNLSMPLLPADFHKENTVTNDW IPEGEEDDDYLDLEKIFSEDDDYIDIVDSLSVSPTDSDVSAGNILQLFHG KSRIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGL KGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLR SVNDLYIQKQFPILLDFKTKVREYYFAEAQIADFSDPAFISKTNNHIMKL TKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNERE VVKVSMMQTKGNFLAANDQELDCDILQLEYVGGISMLIVVPHKMSGMKTL EAQLTPRVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKLMGIRMLFD KNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATTVTTVGFMPLSTQVRF TVDRPFLFLIYEHRTSCLLFMGRVANPSRS
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Molecular Weight
56 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
SERPIND1 (Serpin Family D Member 1) is a member of the serpin superfamily, which encompasses a group of proteins known for their role as serine protease inhibitors. Research has identified SERPIND1 as a crucial regulator in various physiological and pathological processes, including inflammation, cell adhesion, and extracellular matrix remodeling. Its involvement in diseases such as thrombosis, cancer, and respiratory disorders has garnered significant attention. Studies suggest that SERPIND1 may modulate the activity of key proteases involved in hemostasis and tissue repair, highlighting its potential as a therapeutic target. Furthermore, understanding the molecular mechanisms underlying SERPIND1 functions may reveal insights into its contribution to disease progression and provide avenues for novel treatment strategies. Consequently, the recombinant production of SERPIND1 protein for in vitro studies is essential to elucidate its structure-function relationships, facilitate the exploration of its biochemical properties, and evaluate its interactions with other proteins. As a result, research on SERPIND1 recombinant protein aims to advance our knowledge of its role in health and disease, paving the way for innovative therapeutic applications.
