Analytical Data
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Gene name
Caspase-7/CASP7
- Application
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Alternative Names
CMH1; ICE-LAP3; MCH3; Caspase 7 Apoptosis-Related Cysteine Peptidase; Cysteine Aspartate Protease 7; Cysteinyl Aspartate Specific Proteinases 7
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P97864
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Expression Region
Ala207~Arg303
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Molecular Weight
15kDa
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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-7 (CASP7) is an essential cysteine protease that plays a crucial role in the apoptotic pathway, mediating programmed cell death which is fundamental for various physiological processes, including tissue homeostasis and immune response. As an executioner caspase, CASP7 is activated downstream of initiator caspases and is responsible for the cleavage of key cellular substrates, leading to apoptosis. Dysregulation of CASP7 activity has been implicated in numerous diseases, including cancer, neurodegenerative disorders, and inflammatory conditions, making it a potential target for therapeutic intervention. Research on recombinant Caspase-7 has gained momentum, providing both a valuable tool for studying its enzymatic activity and the molecular mechanisms of apoptosis, as well as aiding in the development of caspase inhibitors. Understanding the structure-function relationship of recombinant CASP7, alongside its interactions with other apoptotic proteins, can contribute to novel strategies for manipulating cell death pathways in disease contexts. Furthermore, the generation of specific antibodies against CASP7 and its active form enhances the ability to detect and quantify its expression in various biological samples, thereby advancing our knowledge of its role in health and disease. Overall, the study of recombinant Caspase-7 is pivotal in elucidating cell death mechanisms and paving the way for innovative therapeutic approaches targeting this critical protease.
