Analytical Data
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Gene name
bothrombin
- Application
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Alternative Names
(SVTLE)(Factor VIII activator)(Fibrinogen-clotting enzyme)(Snake venom serine protease)(SVSP)(Venombin A)
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Species
Bothrops jararaca
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P81661
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Expression Region
1-232aa
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Molecular Weight
33.0 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
Bothrombin is a thrombin-like enzyme derived from the venom of the Bothrops asper snake, known for its potent anticoagulant properties. As a serine protease, bothrombin plays a critical role in the modulation of hemostasis, making it a subject of interest in biomedical research and therapeutic applications. The study of bothrombin is particularly relevant for developing new anticoagulant drugs, as traditional anticoagulants often come with significant risks of bleeding or resistance issues. Research into recombinant bothrombin has gained momentum due to advancements in genetic engineering techniques, enabling the production of this protein in controlled environments. Recombinant bothrombin offers advantages such as improved safety profiles, consistency in product quality, and the potential for large-scale production. Investigations into its mechanism of action have revealed how bothrombin selectively inhibits certain coagulation factors, providing insights into its unique anticoagulant effects. These findings not only enhance our understanding of blood coagulation processes but also pave the way for innovative treatments for conditions like thromboembolism and other clotting disorders. Thus, the exploration of bothrombin, particularly in its recombinant form, represents a promising frontier in the search for effective therapeutic agents in the realm of cardiovascular health.
