Caspase-3 Antibody (YA5427)
(Synonyms: CASP3; CPP32; Caspase-3; CASP-3; Apopain; Cysteine protease CPP32; CPP-32; Protein Yama; SREBP cleavage activity 1; SCA-1)Caspase-3 Antibody (YA5427) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Caspase-3.
-
Host:
Mouse
-
Application:
ICC/IF, WB, IP, IHC-P
-
Reactivity :
Human, Mouse, Rat, Chicken
-
Formulation:
Supplied in PBS, pH 7.4, containing 0.5%BSA, 0.02% sodium azide as Preservative and 50% Glycerol.
-
Conjugation:
Non-conjugated
Applications
| Application |
ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
WB
WB: Western Blot
|
IHC-P
IHC-P: Immunohistochemistry-Paraffin
|
|---|---|---|---|
| Dilution Ratio | 1:50-200 | 1:500-1000 | 1:100-200 |
Product Details
Caspase-3 Antibody (YA5427) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Caspase-3.
-
Host Mouse
-
Clonality Monoclonal
-
Species ReactivityHuman, Mouse, Rat, Chicken
-
Observed Molecular WeightObserved band size: 17 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
Recombinant Protein of Active Caspase-3
affinity chromatography.
Non-conjugated
Unmodified
Product Properties
-
Appearance
Solution
-
Formulation
Supplied in PBS, pH 7.4, containing 0.5%BSA, 0.02% sodium azide as Preservative and 50% Glycerol.
-
Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
-
Shipping
Shipping with blue ice.
Background
-
Function
Caspase 3 is a central executioner caspase in apoptosis, where initiator caspase 9 activates executioner caspases 3 and 7 by proteolysis[1]. Mechanistically, caspase 3 cleaves caspase 9 at Asp330 and enhances apoptosis by relieving XIAP-mediated inhibition, rather than directly activating caspase 9[1]. This places caspase 3 within apoptosome-linked feedback control and inhibitor-of-apoptosis regulation, while preserving a distinct functional profile from caspase 7[1][2]. Compared with caspase 7, caspase 3 can cleave caspase 9 under physiologically relevant conditions, and engineered activation studies show that caspase 3 or caspase 7, but not caspase 6 alone, is sufficient to induce apoptosis[1][2]. In disease models, caspase 3 and caspase 7 deletion did not reduce infarct size or ventricular remodeling after transient myocardial ischemia-reperfusion, limiting assumptions about canonical caspase-dependent apoptosis in adult cardiomyocytes[3]. In prostate cancer samples, procaspase 3 and cleaved caspase 3 predicted biochemical progression after radical prostatectomy, supporting their use as apoptosis-related tumor markers[4]. For experimental applications, caspase 3 research benefits from isoform-aware probes because common DEVD-based peptide inhibitors and substrates cannot reliably distinguish caspase 3 from caspase 7[5].
-
Subcellular Localization
Cytoplasm
-
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
-
SwissProt ID
-
Synonyms
CASP3; CPP32; Caspase-3; CASP-3; Apopain; Cysteine protease CPP32; CPP-32; Protein Yama; SREBP cleavage activity 1; SCA-1
Documentation
References
[1]. Denault JB, et al. Caspase 3 attenuates XIAP (X-linked inhibitor of apoptosis protein)-mediated inhibition of caspase 9. Biochem J. 2007 Jul 1;405(1):11-9. [Content Brief]
[2]. Gray DC, et al. Activation of specific apoptotic caspases with an engineered small-molecule-activated protease. Cell. 2010 Aug 20;142(4):637-46. [Content Brief]
[3]. Inserte J, et al. Studies on the role of apoptosis after transient myocardial ischemia: genetic deletion of the executioner caspases-3 and -7 does not limit infarct size and ventricular remodeling. Basic Res Cardiol. 2016 Mar;111(2):18. [Content Brief]
[4]. Rodríguez-Berriguete G, et al. Prognostic value of inhibitors of apoptosis proteins (IAPs) and caspases in prostate cancer: caspase-3 forms and XIAP predict biochemical progression after radical prostatectomy. BMC Cancer. 2015 Oct 27;15:809. [Content Brief]
[5]. Batool A, et al. Eukaryotic initiation factor 4E is a novel effector of mTORC1 signaling pathway in cross talk with Mnk1. Mol Cell Biochem. 2020 Feb;465(1-2):13-26. [Content Brief]