Analytical Data
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Gene name
SVMP
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简介
SVMP protein, while lacking significant hemorrhagic activity, functions by inactivating serpins through limited proteolysis of their reactive-site loops. SVMP Protein, Crotalus adamanteus (His) is the recombinant SVMP protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Alternative Names
Snake venom metalloproteinase adamalysin-2; SVMP; EC 3.4.24.46; Adamalysin II; Proteinase II
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Species
Others
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P34179
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Expression Region
Q1-P203
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AA Sequence
QQNLPQRYIELVVVADRRVFMKYNSDLNIIRTRVHEIVNIINGFYRSLNIDVSLVNLEIWSGQDPLTIQSSSSNTLNSEGLWREKVLLNKKKKDNAQLLTAIEFKCETLGKAYLNSMCNPRSSVGIVKDHSPINLLVAVTMAHELGHNLGMEHDGKDCLRGASLCIMRPGLTPGRSYEFSDDSMGYYQKFLNQYKPQCILNKP
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Protein Length
Full Length
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Molecular Weight
27.1 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
SVMPs (snake venom metalloproteinases) are a diverse group of metalloproteinases found in snake venoms, playing crucial roles in prey immobilization and digestion. They are known for their ability to degrade various components of the extracellular matrix, which facilitates tissue damage and enhances the spread of venom. The study of SVMPs has garnered significant interest due to their potential applications in pharmacology, particularly in the development of novel therapeutic agents for conditions such as cancer, cardiovascular diseases, and inflammation. Understanding their structure-function relationships is vital for harnessing their properties. Recent advances in recombinant protein technology have enabled the production and characterization of SVMPs in controlled environments, facilitating detailed studies on their biological activities and interactions. This research also aims to identify specific inhibitors that could serve as antidotes or therapeutics. Given the increasing interest in venom-derived compounds as a source of drug discovery, research on SVMPs is pivotal in expanding our understanding of venom biology and its potential medical applications.
