Analytical Data
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Gene name
VCATH
- Application
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Alternative Names
VCATH；Viral cathepsin
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q91CL9
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Expression Region
114-324aa
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AA Sequence
PLEFDWRRLNKVTSVKNQGMCGACWAFATLGSLESQFAIKHDQLINLSEQQLIDCDFVDVGCDGGLLHTAYEAVMNMGGIQAENDYPYEANNGPCRVNAAKFVVRVKKCYRYVTLFEEKLKDLLRIVGPIPVAIDASDIVGYKRGIIRYCENHGLNHAVLLVGYGVENGIPFWILKNTWGADWGEQGYFRVQQNINACGIKNELPSSAEIY
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Molecular Weight
31.1 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
VCATH, a novel recombinant protein derived from the venom of the spider venom, has garnered significant attention in the field of molecular biology and pharmacology due to its unique properties and potential therapeutic applications. Research indicates that VCATH possesses antimicrobial and cytotoxic activities, making it a valuable candidate for developing new antibiotics and anticancer therapies. The ongoing global threat of antibiotic resistance necessitates innovative solutions, and VCATH's ability to target specific bacterial membranes presents a promising avenue for overcoming this challenge. Additionally, its selectivity towards cancer cells while sparing normal cells hints at the potential for targeted cancer treatments with reduced side effects. Studies have focused on the protein's structure-function relationship, aiming to elucidate the mechanisms by which VCATH exerts its biological effects and to optimize its efficacy through biochemical engineering. As the demand for new therapeutic agents rises, VCATH represents a compelling example of harnessing natural compounds for biomedical advancements, paving the way for new strategies in treating infectious diseases and cancer.
