Analytical Data
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Gene name
Coagulation Factor XI/F11
- Application
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Alternative Names
CLGN; CLG1; Collagenase; Interstitial Collagenase; Vertebrate Collagenase; Fibroblast Collagenase
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Species
Rabbit
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P13943
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Expression Region
Phe99~Pro268
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Molecular Weight
23kDa
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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
Coagulation Factor XI (F11) is a crucial component of the intrinsic pathway of blood coagulation, playing a significant role in the formation of blood clots. Its deficiency is associated with a bleeding disorder known as hemophilia C, characterized by a reduced ability to form stable blood clots. Recent studies have highlighted the potential of recombinant Factor XI proteins as therapeutic agents for managing bleeding disorders, particularly given the advances in biotechnology that allow the production of such proteins in a more controlled and efficient manner. Recombinant Factor XI is being investigated not only for its therapeutic benefits in hemophilia C but also for its role in potentially reducing thrombotic events in patients at high risk for complications. The duality of Factor XI's function—promoting coagulation while also being involved in the pathogenesis of thrombosis—presents challenges and opportunities in its application. Ongoing research aims to elucidate the structure-function relationship of Factor XI, optimize recombinant production methods, and assess the safety and efficacy of therapeutic interventions targeting F11, ultimately contributing to improved clinical outcomes for patients with bleeding disorders and those susceptible to thrombotic complications.
