Analytical Data
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Gene name
F10
- Application
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Alternative Names
F10；C10orf4；Protein FRA10AC1
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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
P00742
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Expression Region
41-488aa
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AA Sequence
ANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK
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Molecular Weight
57.8 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
The F10 protein, known as factor X or Stuart-Prower factor, plays a critical role in the coagulation cascade, functioning as a key prothrombinase that converts prothrombin to thrombin, ultimately leading to fibrin formation in blood clotting. Research on F10 recombinant protein has gained prominence due to its potential applications in hemophilia treatment, anticoagulation therapy, and enhancing our understanding of hemostasis mechanisms. Recombinant F10 can be engineered to improve its therapeutic efficacy, reduce immunogenicity, and provide a more stable production platform compared to traditional methods. The advancements in biotechnology, particularly in the fields of genetic engineering and protein expression systems, have paved the way for the development of highly purified, functional F10 proteins. Coupled with the growing interest in personalized medicine and target-specific therapies, the study of F10 recombinant proteins holds promise for innovative treatment strategies in coagulation disorders, contributing to improved patient outcomes. As the understanding of the blood coagulation pathway deepens, the targeted manipulation of F10 and its interactions with other coagulation factors presents exciting opportunities for research and therapeutic development in the field of hematology.
