Analytical Data
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Gene name
Pro-Caspase-3/Pro-CASP3
- Application
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Alternative Names
Caspase-3; CASP3; Apopain; Cysteine protease CPP32; CPP-32; Protein Yama; SREBP cleavage activity 1; SCA-1; CPP32
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Species
Human
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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
AAA65015
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Expression Region
M1-H277
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Protein Length
Full Length
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Molecular Weight
34 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
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Protein Description
Pro-Caspase-3, also known as Pro-CASP3, is a crucial aspartic protease that plays a pivotal role in the apoptosis pathway, which regulates programmed cell death in multicellular organisms. As a zymogen, Pro-Caspase-3 is synthesized in an inactive form and requires proteolytic processing to become activated, triggering a cascade of events that lead to cellular apoptosis. This activation is crucial for various physiological processes, including development and immune responses. Dysregulation of Pro-Caspase-3 is implicated in several pathologies, including cancer, where its inactivation can contribute to tumor growth and resistance to therapy. Conversely, excessive activation may lead to neurodegenerative diseases. Consequently, understanding the structure, function, and regulation of Pro-Caspase-3 is of significant interest in both basic and translational research. The generation and study of recombinant Pro-Caspase-3 proteins allow researchers to investigate its activation mechanisms and interactions with other apoptotic factors. This knowledge can ultimately inform therapeutic strategies aimed at manipulating its activity for the treatment of various diseases. Research on recombinant Pro-Caspase-3 not only enhances our understanding of apoptotic mechanisms but also aids in the design of inhibitors or activators that can serve as potential drugs in cancer therapy or neuroprotection. Overall, the study of Pro-Caspase-3 is integral to advancing our understanding of cell death processes and developing innovative therapeutic approaches.
