Analytical Data
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Gene name
SERPINC1
- Application
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Alternative Names
SERPINC1;AT3;Antithrombin-III
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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
P01008
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Expression Region
1-464aa
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AA Sequence
MYSNVIGTVTSGKRKVYLLSLLLIGFWDCVTCHGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRHVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANPCVK
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Molecular Weight
81.5 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
SERPINC1, also known as Antithrombin III (ATIII), is a crucial serine protease inhibitor that plays a vital role in the regulation of blood coagulation. Its primary function is to inhibit thrombin and factor Xa, contributing to the maintenance of hemostatic balance and preventing excessive clotting. Mutations or deficiencies in the SERPINC1 gene can lead to a condition known as Antithrombin deficiency, which increases the risk of thromboembolic disorders, such as venous thrombosis and pulmonary embolism. Given its significant clinical implications, research on SERPINC1 recombinant protein has gained momentum, focusing on its potential therapeutic applications. For instance, recombinant SERPINC1 has been explored for its use in patients with hereditary or acquired antithrombin deficiencies, particularly in situations where conventional treatments, such as heparin, may be insufficient. Moreover, understanding the structure-function relationship of SERPINC1 through biotechnology allows for the design of more effective anticoagulant therapies. Recent advancements in protein engineering and expression systems have made it feasible to produce high-purity recombinant SERPINC1, which not only aids in the study of its biochemical properties but also enhances its potential utility in clinical settings. Overall, ongoing research on SERPINC1 recombinant protein holds promise for improving therapeutic strategies in managing coagulation disorders and could lead to significant advancements in patient care.
