Cleaved-Caspase 3 p12 Antibody (YA499)(PBS only)
(Synonyms: CASP3; CPP32; Caspase-3; CASP-3; Apopain; Cysteine protease CPP32; CPP-32; Protein Yama; SREBP cleavage activity 1; SCA-1)Cleaved-Caspase 3 Antibody (YA499) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Cleaved-Caspase 3.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, ICC/IF
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS, pH 7.4.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 1:50-1:200 |
Product Details
Cleaved-Caspase 3 Antibody (YA499) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Cleaved-Caspase 3.
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Host Rabbit
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 32, 12 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 32 kDa
Synthetic peptide corresponding to Human Caspase-3 p12.The exact sequence is proprietary to MCE.
affinity purified
Non-conjugated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, pH 7.4.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Cleaved-Caspase 3 p12 is a Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis. Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins. 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). Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress. 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. Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface. Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19].
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Subcellular Localization
Cytoplasm
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Expression
Tissue_specificity:It is highly expressed in the lungs, spleen, heart, liver, and kidneys. It is moderately expressed in the brain and skeletal muscle, and lowly expressed in the testes. It is also present in many cell lines, with the highest expression in immune system cells. -
Subunit
Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit. Interacts with BIRC6/bruce
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SwissProt ID
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Synonyms
CASP3; CPP32; Caspase-3; CASP-3; Apopain; Cysteine protease CPP32; CPP-32; Protein Yama; SREBP cleavage activity 1; SCA-1
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Research Field
Cell Biology
Documentation
References
[1]. Walsh JG, et al. Executioner caspase-3 and caspase-7 are functionally distinct proteases. Proc Natl Acad Sci U S A. 2008 Sep 2;105(35):12815-9. [Content Brief]
[2]. Nakatsumi H, et al. Identification of functional regions defining different activity in caspase-3 and caspase-7 within cells. J Biol Chem. 2010 Aug 13;285(33):25418-25. [Content Brief]
[3]. Thomsen ND, et al. Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 activation. Proc Natl Acad Sci U S A. 2013 May 21;110(21):8477-82. [Content Brief]
[4]. Peng T, et al. Pathogen hijacks programmed cell death signaling by arginine ADPR-deacylization of caspases. Mol Cell. 2022 May 19;82(10):1806-1820.e8. [Content Brief]
[5]. Liu Y, et al. Calmodulin Binding Activates Chromobacterium CopC Effector to ADP-Riboxanate Host Apoptotic Caspases. mBio. 2022 Jun 28;13(3):e0069022. [Content Brief]
[6]. Nicholson DW, et al. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature. 1995 Jul 6;376(6535):37-43. [Content Brief]
[7]. Germain M, et al. Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7. J Biol Chem. 1999 Oct 1;274(40):28379-84. [Content Brief]
[8]. Rodríguez-Hernández A, et al. Nuclear caspase-3 and caspase-7 activation, and poly(ADP-ribose) polymerase cleavage are early events in camptothecin-induced apoptosis. Apoptosis. 2006 Jan;11(1):131-9. [Content Brief]
[9]. Tewari M, et al. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 1995 Jun 2;81(5):801-9. [Content Brief]
[10]. Shi X, et al. Recognition and maturation of IL-18 by caspase-4 noncanonical inflammasome. Nature. 2023 Dec;624(7991):442-450. [Content Brief]
[11]. Akita K, et al. Involvement of caspase-1 and caspase-3 in the production and processing of mature human interleukin 18 in monocytic THP.1 cells. J Biol Chem. 1997 Oct 17;272(42):26595-603. [Content Brief]
[12]. Goldberg YP, et al. Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. Nat Genet. 1996 Aug;13(4):442-9. [Content Brief]
[13]. Cabrera JR, et al. RET modulates cell adhesion via its cleavage by caspase in sympathetic neurons. J Biol Chem. 2011 Apr 22;286(16):14628-38. [Content Brief]
[14]. Sen T, et al. OGDHL is a modifier of AKT-dependent signaling and NF-κB function. PLoS One. 2012;7(11):e48770. [Content Brief]
[15]. Ning X, et al. Apoptotic Caspases Suppress Type I Interferon Production via the Cleavage of cGAS, MAVS, and IRF3. Mol Cell. 2019 Apr 4;74(1):19-31.e7. [Content Brief]
[16]. Suzuki J, et al. Xk-related protein 8 and CED-8 promote phosphatidylserine exposure in apoptotic cells. Science. 2013 Jul 26;341(6144):403-6. [Content Brief]
[17]. Maruoka M, et al. Caspase cleavage releases a nuclear protein fragment that stimulates phospholipid scrambling at the plasma membrane. Mol Cell. 2021 Apr 1;81(7):1397-1410.e9. [Content Brief]
[18]. Hunkeler M, et al. Structures of BIRC6-client complexes provide a mechanism of SMAC-mediated release of caspases. Science. 2023 Mar 17;379(6637):1105-1111. [Content Brief]
[19]. Dietz L, et al. Structural basis for SMAC-mediated antagonism of caspase inhibition by the giant ubiquitin ligase BIRC6. Science. 2023 Mar 17;379(6637):1112-1117. [Content Brief]
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