Analytical Data
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Gene name
CTSV
- Application
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Alternative Names
CTS-L2; CTSL2; CATL2; CTSU; CTS-V; Cathepsin L2
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Species
Human
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Source
E. coli
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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
O60911
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Expression Region
Gly64~Val334
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Molecular Weight
32kDa
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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
CTSV (cathepsin V) is a cysteine protease that plays a critical role in various physiological and pathological processes, including immune response, tissue remodeling, and cancer progression. Its unique substrate specificity and involvement in the degradation of extracellular matrix components make it a focal point of research in cancer biology and tissue engineering. CTSV's dysregulation has been implicated in various diseases, particularly those characterized by aberrant proteolytic activity such as tumors, where it contributes to invasion and metastasis. The study of recombinant CTSV proteins has gained momentum due to their potential applications in therapeutic development and as biomarkers for disease states. By utilizing recombinant DNA technology, researchers can produce large quantities of CTSV in a controlled manner, allowing for in-depth studies on its enzymatic properties, regulatory mechanisms, and interactions with other proteins. Moreover, understanding the structural dynamics of CTSV through recombinant protein studies can aid in the design of specific inhibitors that could serve as novel therapeutic agents in cancer treatment and other disorders linked to proteolytic dysfunction. These insights not only enhance our understanding of CTSV's biological functions but also open avenues for innovative strategies in drug development and disease management. Overall, the continued investigation of CTSV and its recombinant forms is essential for progressing toward targeted therapies that can modulate its activity in disease contexts, thereby improving clinical outcomes.
