Analytical Data
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Gene name
Caspase-3/CASP3
- Application
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Alternative Names
CPP32; CPP32B; SCA1; Apoptain; Yama; Apoptosis-Related Cysteine Peptidase; Cysteinyl Aspartate Specific Proteinases 3; SREBP cleavage activity 1
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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
p42574
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Expression Region
Ser29~His277
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Molecular Weight
14/18/20kDa
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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
Caspase-3, also known as CASP3, is a crucial cysteine protease that plays a key role in the execution phase of apoptosis, or programmed cell death. Its activation is a critical step in various cellular processes, including the response to stress, development, and immune regulation. Dysregulation of Caspase-3 activity has been implicated in numerous diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases, making it a significant focus of biomedical research. The study of recombinant Caspase-3 proteins allows researchers to better understand the molecular mechanisms underlying its activation and regulation. By producing and purifying CASP3 in a recombinant form, scientists can analyze its enzymatic properties, substrate specificity, and interactions with other proteins. This research not only contributes to our understanding of apoptotic pathways but also aids in the development of potential therapeutic strategies that can modulate Caspase-3 activity. Additionally, recombinant Caspase-3 can serve as a valuable tool for drug screening and the identification of novel small molecules that can either inhibit or enhance its activity, further advancing the field of targeted therapies in diseases characterized by aberrant apoptotic signaling. Overall, the investigation of Caspase-3 through recombinant protein studies is essential for elucidating its role in health and disease, with potential applications in improving clinical outcomes for various conditions associated with apoptosis dysregulation.
