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Caspase-3 Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, E |
|---|---|
| Primary Accession | P42574 |
| Other Accession | NP_004337, 14790119 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | 30 kDa |
| Application Notes | Caspase-3 antibody can be used for detection of Caspase-3 by immunohistochemistry at 5 µg/mL. |
| Gene ID | 836 |
|---|---|
| Other Names | Caspase-3 Antibody: CPP32, SCA-1, CPP32B, CPP32, Caspase-3, Apopain, CASP-3, caspase 3, apoptosis-related cysteine peptidase |
| Target/Specificity | CASP3; At least two isoforms of Caspase-3 are known to exist. |
| Reconstitution & Storage | Caspase-3 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. |
| Precautions | Caspase-3 Antibody is for research use only and 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
Caspase-3 Antibody: Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. The apoptotic subfamily can be further divided into initiator caspases, which are activated in response to death signals, and executioner caspases, which are activated by the initiator caspases and are responsible for cleavage of cellular substrates that ultimately lead to cell death. Caspase-3 is synthesized as an inactive proenzyme that undergoes proteolytic cleavage by caspases 8, 9 and 10 to produce 2 subunits, termed p20 and p11. These subunits dimerize to form the active enzyme. Caspase-3 proteolytically cleaves and activates other proteins such as caspases 6, 7 and 9.
References
Martinon F and Tschopp J. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases. Cell 2004; 117:561-74
Zhivotovsky B and Orrenius S. Caspase-2 function in response to DNA damage. Biochim. Biophys. Res. Comm. 2005; 331:859-67.
Wolf BB and Green DR. Suicidal tendencies: apoptotic cell death by caspase family proteinases. J. Biol. Chem. 1999; 274:20049-52.
Slee EA, Adrain C, and Martin SJ. Serial killers: ordering caspase activation events in apoptosis. Cell Death Diff. 1999; 6:1067-74.
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