Analytical Data
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Gene name
botrocetin
- Application
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Alternative Names
Snake venom metalloproteinase von Willebrand factor-dependent platelet coagglutinin
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Species
Bothrops jararaca
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Source
E. coli
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Tag
N- His-KSI
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P22028
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Expression Region
1-25aa
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Molecular Weight
18.0 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
Botrocetin is a recombinant protein derived from the venom of the Brazilian pit viper, Bothrops asper, known for its unique ability to facilitate platelet aggregation in the presence of von Willebrand factor (vWF). This protein plays a crucial role in the study of hemostasis and thrombosis, as it mimics the physiological interaction between platelets and vWF, which is essential for normal blood clotting. Research on botrocetin has gained significance due to its potential applications in understanding various bleeding disorders, particularly those related to von Willebrand disease. Additionally, the use of recombinant techniques to produce botrocetin allows for the generation of higher purity and more consistent protein products compared to traditional extraction methods from snake venom. This recombinant approach paves the way for in-depth studies of its structure-function relationships and its interactions with other hemostatic factors. Moreover, botrocetin serves as an important tool in the development of diagnostic assays and therapeutic agents aimed at managing bleeding risks. Given the complexity of the coagulation process, ongoing research into botrocetin provides valuable insights into platelet biology and potential therapeutic strategies for conditions associated with abnormal hemostasis.
