Analytical Data
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Gene name
crotalase
- Application
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Alternative Names
Thrombin-like enzyme crotalase; SVTLE; EC 3.4.21.74; Fibrinogen-clotting enzyme; Snake venom serine protease 2; SVSP
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Species
Crotalus adamanteus
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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
F8S114
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Expression Region
25-262aa
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Molecular Weight
28.8 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
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Protein Description
Crotalase, a potent phospholipase A2 enzyme derived from the venom of rattlesnakes, exhibits significant biochemical properties that have drawn interest in both pharmaceutical and biotechnological research. Its ability to hydrolyze phospholipids makes it a valuable tool for studying membrane dynamics and signal transduction pathways in eukaryotic cells. The functional versatility of crotalase has prompted researchers to explore its potential applications, including in drug delivery systems, as a molecular probe in lipid research, and for the development of therapeutics targeting inflammatory conditions. However, challenges in obtaining sufficient quantities of native crotalase for study due to its isolation from venom necessitated the development of recombinant versions of the protein. Advances in molecular cloning and protein expression technologies have facilitated the production of recombinant crotalase in various expression systems, enabling detailed structural and functional analyses. Understanding the mechanism of action of recombinant crotalase and its interaction with biological membranes is crucial for harnessing its properties effectively. This research could not only unravel the complexities of phospholipid dynamics but also contribute to the design of innovative strategies in drug design and therapy response modulation. The increasing knowledge about recombinant crotalase's mechanism and potential applications underscores the importance of this research in the realms of biochemistry and medicine, paving the way for novel avenues in therapeutic development and biomedical innovation.
