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mouse CASP3 Antibody (N-term S12)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P70677 |
| Other Accession | NP_033940.1 |
| Reactivity | Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 31475 Da |
| Antigen Region | 1-30 aa |
| Gene ID | 12367 |
|---|---|
| Other Names | Caspase-3, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, LICE, Protein Yama, SREBP cleavage activity 1, SCA-1, Caspase-3 subunit p17, Caspase-3 subunit p12, Casp3, Cpp32 |
| Target/Specificity | This mouse CASP3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of mouse CASP3. |
| Dilution | WB~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | mouse CASP3 Antibody (N-term S12) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | Casp3 |
|---|---|
| Synonyms | Cpp32 {ECO:0000303|PubMed:8934524} |
| Function | Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis (PubMed:16469926, PubMed:8934524). Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins (PubMed:16469926, PubMed:8934524). At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9 (CASP6, CASP7 and CASP9, respectively). Cleaves and inactivates interleukin-18 (IL18) (By similarity). Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes (By similarity). Cleaves and inhibits serine/threonine- protein kinase AKT1 in response to oxidative stress (PubMed:12124386). 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) (By similarity). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (PubMed:25231987, PubMed:33725486). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (By similarity). |
| Cellular Location | Cytoplasm {ECO:0000250|UniProtKB:P42574}. |
| Tissue Location | Highest expression in spleen, lung, liver, kidney and heart (PubMed:9038361). Lower expression in brain, skeletal muscle and testis (PubMed:9038361). |
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Provided below are standard protocols that you may find useful for product applications.
Background
CASP3 is involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9 (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes.
References
Srikanth, C.V., et al. Science 330(6002):390-393(2010)
Li, F., et al. Cell Stem Cell 7(4):508-520(2010)
Wang, L., et al. J. Neurosci. 30(39):13201-13210(2010)
Gascon, E., et al. J. Neurosci. 30(37):12414-12423(2010)
Bohsali, A., et al. BMC Microbiol. 10, 237 (2010) :
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