CASP3 Recombinant Protein

Source : Escherichia Coli. CASP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 103 amino acids (176-277) and having a molecular mass of 12kDa.CASP3 is purified by proprietary chromatographic techniques. Caspase 3 Apoptosis-Related Cysteine Peptidase (CASP3) belongs to the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a key role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to generate 2 subunits, large and small, that dimerize to create the active enzyme. CASP3 protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. CASP3 is the leading caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is linked with neuronal death in Alzheimer's disease. In addition, CASP3 is involved in the cleavage of huntingtin. CASP3 also cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. CASP3 initiates cell adhesion in sympathetic neurons through RET cleavage.

Product Specifications

Product Name Alternative

Caspase 3 Apoptosis-Related Cysteine Peptidase||CPP32 Caspase 3 Apoptosis-Related Cysteine Protease||Cysteine Protease CPP32||Protein Yama||CASP-3||CPP-32||SCA-1||SREBP Cleavage Activity 1||EC 3.4.22.56||CPP32B||caspase-3||PARP Cleavage Protease||pro

Purification

Greater than 80.0% as determined by SDS-PAGE.

Components

The CASP3 solution (0.5mg/mL) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Storage Conditions

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA) .Avoid multiple freeze-thaw cycles.