Analytical Data
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Gene name
contortrixobin
- Application
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Alternative Names
Fibrinogen-clotting enzyme (Snake venom serine protease) (SVSP) (Venombin B)
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Species
Agkistrodon contortrix
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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
P82981
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Expression Region
1-234aa
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Molecular Weight
32.4 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
Contortrixobin, derived from the venom of the southeastern pygmy rattlesnake (*Sistrurus catenatus*), is a neurotoxin that has garnered significant interest in biomedical research due to its unique properties as a disintegrin-like protein. This small, non-enzymatic protein specifically targets integrins, which are vital in cell adhesion and signaling processes, making contortrixobin a promising candidate for therapeutic applications such as anti-cancer treatments and wound healing. The protein exhibits a high affinity for αvβ3 and αvβ5 integrins, which are often overexpressed in various tumor types, thus enabling potential targeted delivery mechanisms for drug therapies. Furthermore, understanding contortrixobin's structure and mechanism of action can provide insights into the evolution of venom proteins and their roles in predation and defense. Researchers are actively investigating its ability to inhibit angiogenesis and alter cellular behavior, thereby contributing to the development of novel pharmacological agents. As studies continue to unravel the molecular pathways influenced by contortrixobin, its application in clinical settings may pave the way for innovative treatments for cancer and other diseases characterized by aberrant cell adhesion and migration.
