Analytical Data
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Gene name
atroxlysin
- Application
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Alternative Names
(SVMP)(Atroxlysin-I)
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Species
Bothrops atrox
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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
P85420
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Expression Region
1-202aa
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Molecular Weight
30.4 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
Atroxlysin, a snake venom metalloproteinase, exhibits significant enzymatic activity, contributing to the pathogenicity of snake bites through tissue destruction and hemorrhage. Research into atroxlysin and its recombinant forms aims to elucidate its structure-function relationships, which can pave the way for therapeutic applications and antidote development. Studies have highlighted its dual role in modulating both pro-inflammatory and anti-inflammatory pathways, showcasing its potential in understanding and managing inflammatory responses. Moreover, recombinant technologies allow for the production of atroxlysin in a controlled environment, facilitating detailed analyses of its kinetics and interactions with biological substrates. This research not only expands our knowledge of venom proteins but also opens new avenues for drug discovery and the development of novel therapeutic agents capable of mitigating venom-induced damage. Understanding atroxlysin's mechanisms can lead to innovative strategies for treating venoms and inflammatory disorders, making it a focus of considerable scientific inquiry within the fields of toxicology and pharmacology.
