Analytical Data
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Gene name
Coagulation Factor II/F2
- Application
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Alternative Names
Coagulation factor II Cleaved into the following 4 chains: Activation peptide fragment 1 Activation peptide fragment 2 Thrombin light chain Thrombin heavy chain
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Species
Human
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Source
Yeast
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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
P00734
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Expression Region
44-622aa
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Molecular Weight
67.3 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
Coagulation Factor II, also known as prothrombin, plays a pivotal role in the coagulation cascade, converting to thrombin and subsequently facilitating the formation of fibrin clots which are essential for hemostasis. Deficiencies or dysfunctions in Factor II can lead to bleeding disorders, making it a critical target for therapeutic interventions. The recombinant version of Factor II/F2 has garnered attention due to its potential for treating such conditions while minimizing the risk of virus transmission associated with plasma-derived products. Advances in recombinant DNA technology have enabled the efficient production of this protein in various expression systems, enhancing its availability and purity. Researchers have focused on optimizing the structure and functional properties of recombinant Factor II to improve its pharmacokinetics and biological activity, aligning with the body's natural coagulation processes. Ongoing studies address formulation stability, dosing regimens, and immunogenicity, which are vital for successful clinical application. The development of recombinant Factor II not only represents a significant advancement in hemophilia management but also holds promise for broader therapeutic implications in coagulopathy and surgical contexts.
