CASP3 (caspase 3. apoptosis-related cysteine peptidase)

GWB-1B26A8

1:62500

Suggested starting concentrations are provided. Optimal dilutions should be determined by end-user. Differences in calculated versus apparent molecular weight may be due to post-translational modifications or protein hydrophobicity. CASP3 is a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic

Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3 although Val or Ala are also accepted at this position.

Heterotetramer that consists of two anti-parallel arranged heterodimers each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit.

Highly expressed in lung spleen heart liver and kidney. Moderate levels in brain and skeletal muscle and low in testis. Also found in many cell lines highest expression in cells of the immune system.

Belongs to the peptidase C14 family [view classification]. Summary: This protein is a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits large and small that dimerize to form the active enzyme. This protein cleaves and activates caspases 6 7 and 9 and the protein itself is processed by caspases 8 9 and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein which is associated with neuronal death in Alzheimer\' s disease. Alternative splicing of this gene results in two transcript variants that encode the same protein. Selvakumar. P. . et al. . (2006) FEBS Lett. 580 (8). 2021-2026.