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Phospho-CASP3(S26) Antibody Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P42574 |
|---|---|
| Clone Names | 111026059 |
| Gene ID | 836 |
|---|---|
| Other Names | Caspase-3, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 1, SCA-1, Caspase-3 subunit p17, Caspase-3 subunit p12, CASP3, CPP32 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | CASP3 |
|---|---|
| Synonyms | CPP32 {ECO:0000303|PubMed:7983002} |
| Function | Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis (PubMed:7596430, PubMed:18723680, PubMed:20566630, PubMed:23650375, PubMed:35338844, PubMed:35446120). Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins (PubMed:7596430, PubMed:18723680, PubMed:20566630, PubMed:23650375). At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond (PubMed:7774019, PubMed:7596430, PubMed:10497198, PubMed:16374543). Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain (By similarity). Cleaves and activates caspase-6, -7 and -9 (CASP6, CASP7 and CASP9, respectively) (PubMed:7596430). Cleaves and inactivates interleukin-18 (IL18) (PubMed:9334240, PubMed:37993714). Involved in the cleavage of huntingtin (PubMed:8696339). Triggers cell adhesion in sympathetic neurons through RET cleavage (PubMed:21357690). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress (PubMed:23152800). Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction (PubMed:30878284). Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (PubMed:35446120, PubMed:35338844). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (PubMed:23845944, PubMed:33725486). |
| Cellular Location | Cytoplasm. |
| Tissue Location | 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. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a protein which is a member of thecysteine-aspartic acid protease (caspase) family. Sequentialactivation of caspases plays a central role in the execution-phaseof cell apoptosis. Caspases exist as inactive proenzymes whichundergo proteolytic processing at conserved aspartic residues toproduce two subunits, large and small, that dimerize to form theactive enzyme. This protein cleaves and activates caspases 6, 7 and9, and the protein itself is processed by caspases 8, 9 and 10. Itis the predominant caspase involved in the cleavage of amyloid-beta4A precursor protein, which is associated with neuronal death inAlzheimer's disease. Alternative splicing of this gene results intwo transcript variants that encode the same protein. [provided byRefSeq].
References
Wurstle, M.L., et al. J. Biol. Chem. 285(43):33209-33218(2010)Srikanth, C.V., et al. Science 330(6002):390-393(2010)Burke, S.P., et al. J. Biol. Chem. 285(39):30061-30068(2010)Chen, W., et al. Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 26(7):673-674(2010)Bellini, M.F., et al. Anticancer Res. 30(7):2845-2849(2010)
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