Analytical Data
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Gene name
Cruzipain
- Application
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Alternative Names
Cruzaine (Major cysteine proteinase)
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Species
Trypanosoma cruzi
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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
P25779
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Expression Region
123-467aa
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Molecular Weight
43.9 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
Cruzipain is a cysteine protease derived from the protozoan parasite *Trypanosoma cruzi*, the causative agent of Chagas disease, which affects millions of people, primarily in Latin America. This enzyme plays a crucial role in the parasite's lifecycle and pathogenesis, facilitating processes such as host cell invasion and immune evasion. Given its importance, cruzipain has become a significant target for drug development, with the potential to lead to novel therapeutic strategies against Chagas disease. Traditional treatments are often inadequate, prompting researchers to explore cruzipain inhibitors that could selectively disrupt the enzyme's function, thereby impairing the parasite's ability to survive in the host. The recombinant production of cruzipain allows for comprehensive structural and functional studies, which can elucidate its mechanisms and identify effective inhibitors. Understanding the enzyme's structure-function relationships is essential for designing targeted drugs that can effectively combat the disease and improve patient outcomes. Consequently, research on cruzipain continues to be critical not only for developing new pharmacological therapies but also for advancing the overall understanding of *T. cruzi* biology and pathogenicity.
