caspase-7 p10 Antibody (E-11): sc-271747

caspase-7 p10 Antibody (E-11) is a mouse monoclonal IgG1 antibody that detects caspase-7 in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Caspase-7 is a crucial cysteine protease that plays a significant role in the apoptotic process, functioning as an executioner caspase that mediates morphological changes associated with cell death by cleaving various substrates. Caspase-7 is involved in the activation of pro-inflammatory cytokines, thereby linking apoptosis to inflammation, which has implications in various diseases, including cancer and neurodegenerative disorders. Caspase-7 is located in the cytoplasm and is expressed in a variety of tissues, including lung, skeletal muscle, liver, kidney, spleen, and heart, as well as in cell lines like Jurkat cells. Human caspase-7 gene is located on chromosome 10q25.3 and encodes a 303 amino acid protein that is cleaved into active p20 and p10 subunits, forming a heterodimeric complex that becomes catalytically active during apoptosis. Caspase-7′s ability to interact with other proteins in the apoptotic pathway underscores its importance in regulating cell death and maintaining cellular homeostasis, making anti-caspase-7 antibody (E-11) an essential tool for researchers studying apoptosis and related processes.

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caspase-7 p10 Antibody (E-11) References:

1. Detection of Plasmid-Mediated β-Lactamase Genes and Emergence of a Novel AmpC (CMH-1) in Enterobacter cloacae at a Medical Center in Southern Taiwan.  |  Ku, YH., et al. 2018. J Clin Med. 8: PMID: 30577544
2. The molecular mechanism and evolutionary divergence of caspase 3/7-regulated gasdermin E activation.  |  Xu, H., et al. 2024. Elife. 12: PMID: 38489483
3. Mch3, a novel human apoptotic cysteine protease highly related to CPP32.  |  Fernandes-Alnemri, T., et al. 1995. Cancer Res. 55: 6045-52. PMID: 8521391
4. ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis.  |  Duan, H., et al. 1996. J Biol Chem. 271: 1621-5. PMID: 8576161
5. Processing and activation of CMH-1 by granzyme B.  |  Gu, Y., et al. 1996. J Biol Chem. 271: 10816-20. PMID: 8631895
6. In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains.  |  Fernandes-Alnemri, T., et al. 1996. Proc Natl Acad Sci U S A. 93: 7464-9. PMID: 8755496
7. Chromosomal localization of the human genes, CPP32, Mch2, Mch3, and Ich-1, involved in cellular apoptosis.  |  Tiso, N., et al. 1996. Biochem Biophys Res Commun. 225: 983-9. PMID: 8780721
8. Cytotoxic T-cell-derived granzyme B activates the apoptotic protease ICE-LAP3.  |  Chinnaiyan, AM., et al. 1996. Curr Biol. 6: 897-9. PMID: 8805307
9. Chromosomal mapping of cell death proteases CPP32, MCH2, and MCH3.  |  Bullrich, F., et al. 1996. Genomics. 36: 362-5. PMID: 8812467
10. Activation of CPP32 and Mch3 alpha in wild-type p53-induced apoptosis.  |  Chandler, JM., et al. 1997. Biochem J. 322 (Pt 1): 19-23. PMID: 9078237

The preferred caspase-7 antibody is caspase-7 Antibody (10-1-62): sc-56063.