caspase-7 Antibody (51): sc-135858
- caspase-7 Antibody (51) is a mouse monoclonal IgG2b provided at 50 µg/500 µl
- raised against amino acids 4-126 of caspase-7 of human origin
- recommended for detection of p20 subunit and full length caspase-7 of human and canine origin by WB, IP and IF; not recommended for IP
- At present, we have not yet completed the identification of the preferred secondary detection reagent(s) for caspase-7 Antibody (51). This work is in progress.
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Caspase-7 Antibody (51) is a mouse monoclonal IgG2b antibody that detects caspase-7 in human and canine samples through applications such as western blotting (WB), immunoprecipitation (IP), and immunofluorescence (IF). Caspase-7 is a crucial member of the Ced-3/caspase-1 family of cysteine proteases, which play a vital role in the apoptotic process by cleaving specific target proteins essential for cellular longevity and integrity. Caspase-7 is primarily located in the cytoplasm and is activated in response to apoptotic signals, where caspase-7 translocates to the nucleus to execute its function. The importance of caspase-7′s cellular location lies in its ability to cleave nuclear proteins, such as poly(ADP-ribose) polymerase, which is involved in DNA repair and cellular stress responses. By targeting these proteins, caspase-7 facilitates the dismantling of cellular components during apoptosis, ensuring that damaged or unwanted cells are efficiently removed. The ability of caspase-7 to interact with other caspases, such as caspase-3 and caspase-6, further underscores caspase-7′s significance in the apoptotic cascade, making caspase-7 a critical target for studies related to cell death and survival mechanisms. Anti-caspase-7 antibody (51) is an invaluable tool for researchers investigating the intricate processes of apoptosis and its implications in various diseases.
Alexa Fluor® is a trademark of Molecular Probes Inc., OR., USA
LI-COR® and Odyssey® are registered trademarks of LI-COR Biosciences
caspase-7 Antibody (51) References:
- Cisplatin-induced apoptosis in melanoma cells: role of caspase-3 and caspase-7 in Apaf-1 proteolytic cleavage and in execution of the degradative phases. | Del Bello, B., et al. 2003. Ann N Y Acad Sci. 1010: 200-4. PMID: 15033720
- Using peptidic inhibitors to systematically probe the S1' site of caspase-3 and caspase-7. | Goode, DR., et al. 2005. Org Lett. 7: 3529-32. PMID: 16048334
- Proteolysis consistent with activation of caspase-7 after severe traumatic brain injury in humans. | Zhang, X., et al. 2006. J Neurotrauma. 23: 1583-90. PMID: 17115905
- Caspase-7 mediated cleavage of proteasome subunits during apoptosis. | Jang, M., et al. 2007. Biochem Biophys Res Commun. 363: 388-94. PMID: 17880920
- Engineering a photoactivated caspase-7 for rapid induction of apoptosis. | Mills, E., et al. 2012. ACS Synth Biol. 1: 75-82. PMID: 23651071
- Polyglutamine expansion disturbs the endoplasmic reticulum formation, leading to caspase-7 activation through Bax. | Ueda, M., et al. 2014. Biochem Biophys Res Commun. 443: 1232-8. PMID: 24388981
- Lipoprotein-associated phospholipase A2 regulates macrophage apoptosis via the Akt and caspase-7 pathways. | Maeda, T., et al. 2014. J Atheroscler Thromb. 21: 839-53. PMID: 24717759
- Combined inhibition of caspase 3 and caspase 7 by two highly selective DARPins slows down cellular demise. | Flütsch, A., et al. 2014. Biochem J. 461: 279-90. PMID: 24779913
- Characterization of Hsp90 Co-Chaperone p23 Cleavage by Caspase-7 Uncovers a Peptidase-Substrate Interaction Involving Intrinsically Disordered Regions. | Martini, C., et al. 2017. Biochemistry. 56: 5099-5111. PMID: 28863261
- Different subcellular distribution of caspase-3 and caspase-7 following Fas-induced apoptosis in mouse liver. | Chandler, JM., et al. 1998. J Biol Chem. 273: 10815-8. PMID: 9556551
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
caspase-7 Antibody (51) | sc-135858 | 50 µg/500 µl | $322.00 |