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- Table of Contents
4 Citations 6 Q&As
103 Citations 17 Q&As
116 Citations 4 Q&As
117 Citations 5 Q&As
148 Citations 16 Q&As
46 Citations 15 Q&As
32 Citations 16 Q&As
26 Citations 16 Q&As
56 Citations 15 Q&As
18 Citations 5 Q&As
58 Citations 16 Q&As
49 Citations 4 Q&As
12 Citations 14 Q&As
16 Citations 16 Q&As
17 Citations 15 Q&As
12 Citations 16 Q&As
1 Citations
Facts about Caspase-3.
Human | |
---|---|
Gene Name: | CASP3 |
Uniprot: | P42574 |
Entrez: | 836 |
Belongs to: |
---|
peptidase C14A family |
Apopain; apoptosis-related cysteine protease; CASP3; CASP-3; caspase 3, apoptosis-related cysteine peptidase; Caspase3; Caspase-3; CPP32; CPP-32; CPP32B; CPP32SREBP cleavage activity 1; Cysteine protease CPP32; EC 3.4.22; EC 3.4.22.56; LICE-1; PARP cleavage protease; procaspase3; Protein Yama; SCA-1; YAMA
Mass (kDA):
31.608 kDA
Human | |
---|---|
Location: | 4q35.1 |
Sequence: | 4; NC_000004.12 (184627696..184649475, complement) |
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.
Cytoplasm.
PMID: 7983002 by Fernandes-Alnemri T., et al. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme.
PMID: 7774019 by Tewari M., et al. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase.
*Showing only the more recent 20. More publications can be found for each product on its corresponding product page