Analytical Data
-
Gene name
CASP7
- Application
-
Alternative Names
CASP7；MCH3；Caspase-7
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P55210
-
Expression Region
1-303aa
-
AA Sequence
MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLFSKKKKNVTMRSIKT TRDRVPTYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKC FRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVI YGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSG PINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILE EHGKDLEIMQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELY FSQHHHHHH
-
Molecular Weight
35 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Related Products
Protein Description
CASP7, or Caspase-7, is a key member of the cysteine-aspartic protease (caspase) family, which plays a critical role in the execution phase of apoptosis, a programmed cell death essential for maintaining cellular homeostasis and development. The research surrounding CASP7 has gained significant attention due to its involvement in various pathological conditions, including cancer, neurodegenerative diseases, and inflammatory disorders. Unlike other caspases, CASP7 is often regarded as an executioner protease, activating cellular pathways that lead to apoptosis by cleaving specific substrates. The study of recombinant CASP7 proteins is pivotal for understanding its biochemical properties, substrate specificity, and regulatory mechanisms, as well as their implications in disease progression. Recombinant protein technology enables researchers to produce CASP7 in a controlled environment, allowing for detailed investigations into its functional characteristics and interactions with other proteins. Moreover, understanding the structure-function relationship of CASP7 may pave the way for the development of novel therapeutics aimed at modulating its activity in various diseases, particularly in contexts where apoptosis is dysregulated. Therefore, the exploration of CASP7 recombinant proteins is not only critical for basic biological research but also holds promise for advancing therapeutic strategies in apoptosis-related diseases.
