Analytical Data
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Gene name
CASP6
- Application
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Alternative Names
MCH2; Cysteinyl Aspartate Specific Proteinases 6; Caspase 6,Apoptosis-Related Cysteine Peptidase; Apoptotic protease Mch-2
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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 95% as determined by SDS-PAGE.
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Uniprot
P55212
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Expression Region
Ala194~Asn293
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Molecular Weight
13kDa
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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
CASP6, or Caspase-6, is a cysteine protease that plays a significant role in the process of apoptosis, or programmed cell death. It is part of the caspase family, which is crucial for the execution of apoptosis in various cellular contexts. Research has indicated that CASP6 is not only involved in the apoptotic pathway but also has a role in neurodegenerative diseases, such as Alzheimer's disease, where its activation can lead to the cleavage of key substrates that impact neuronal survival. Given its importance, the expression and purification of recombinant CASP6 protein have garnered substantial interest in the scientific community. This enables researchers to study its biochemical properties, regulatory mechanisms, and interactions with other cellular components in detail. By producing CASP6 in a controlled environment, researchers can explore its enzymatic activity, substrate specificity, and potential inhibitors, which is crucial for developing therapeutic strategies targeting apoptosis-related conditions. Furthermore, studies on recombinant CASP6 may provide insights into its contribution to brain pathology and the underlying mechanisms of neurodegeneration, potentially leading to novel biomarkers or drug targets for diseases marked by dysregulated apoptosis. Thus, the investigation into recombinant CASP6 serves as a pivotal step toward understanding its functional significance in both physiological and pathological processes.
