Caspase-9 Antibody (YA5356)
(Synonyms: CASP9; MCH6; Caspase-9; CASP-9; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3; ICE-like apoptotic protease 6; ICE-LAP6)
Based on 1 Customer Validation
Caspase-9 Antibody (YA5356) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Caspase-9.
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Host:
Mouse
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Application:
WB, IHC-P, ICC/IF, IP
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Reactivity :
Human, Mouse, Rat, chicken
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Formulation:
Supplied in PBS, pH 7.4, containing 0.5%BSA, 0.02% sodium azide as Preservative and 50% Glycerol.
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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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IP
IP: Immunoprecipitation
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|---|---|---|
| Dilution Ratio | 1:1000-5000 | 1:200 | 1:200 | 1:50-300 |
Product Details
Caspase-9 Antibody (YA5356) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Caspase-9.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat, chicken
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Observed Molecular WeightObserved band size: 46 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.
Synthetic Peptide of Caspase 9
affinity chromatography.
Non-conjugated
Unmodified
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, pH 7.4, containing 0.5%BSA, 0.02% sodium azide as Preservative and 50% Glycerol.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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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.
Verification Images
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Immunohistochemical analysis of paraffin-embedded human colon cancer using Caspase-9 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P85664, 1/300) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human ovarian cancer using Caspase-9 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P85664, 1/300) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human prostate cancer using Caspase-9 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P85664, 1/300) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human tonsil using Caspase-9 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P85664, 1/300) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human cervical cancer using Caspase-9 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P85664, 1/300) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human liver using Caspase-9 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P85664, 1/300) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human stomach cancer using Caspase-9 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P85664, 1/300) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
Background
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Function
Caspase 9 plays a central role in the mitochondrial, or intrinsic, apoptotic pathway, where cytochrome c release promotes apoptosome formation with Apaf-1 and procaspase-9[1]. Mechanistically, activated caspase 9 cleaves and activates effector caspases 3 and 7, linking mitochondrial dysfunction to proteolytic cell death execution[1][2]. In disease models, diminished Apaf-1 activity reduced cytochrome c-dependent caspase activation in ovarian cancer cell lines, while ischemic hippocampal neurons showed caspase 9 activation before neuronal death[2][3]. Compared with caspase 8 in the extrinsic pathway, caspase 9 primarily mediates the intrinsic route to caspase 3 activation in ischemic neurons and TNFR-mediated hepatocyte apoptosis[3][4]. For experimental applications, Apaf-1 ligands inhibited apoptosome-mediated procaspase-9 activation and reduced apoptotic phenotypes in mitochondrial apoptosis models[5].
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Expression
Tissue_specificity:It is widely distributed throughout the body, with the highest expression level in the heart, moderate expression levels in the liver, skeletal muscle, and pancreas, and low expression levels in all other tissues. In the heart, it is specifically expressed in cardiomyocytes. -
Isoforms & Post-Translational Modification
P55211 has 4 isomers: P55211-1: 46281 Da (predicted); P55211-2: 30184 Da (predicted); P55211-3: 17397 Da (predicted); P55211-4: 36564 Da (predicted).
Cleavages at Asp-315 by granzyme B and at Asp-330 by caspase-3 generate the two active subunits. Caspase-8 and -10 can also be involved in these processing events;Phosphorylated at Thr-125 by MAPK1/ERK2. Phosphorylation at Thr-125 is sufficient to block caspase-9 processing and subsequent caspase-3 activation. Phosphorylation on Tyr-153 by ABL1/c-Abl; occurs in the response of cells to DNA damage;(Microbial infection) ADP-riboxanation by C.violaceum CopC blocks CASP9 processing, preventing CASP9 activation and ability to mediate intrinsic apoptosis;Ubiquitinated by BIRC6; this activity is inhibited by DIABLO/SMAC -
Subunit
Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 35 kDa (p35) and a 10 kDa (p10) subunit. Caspase-9 and APAF1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome C and ATP. Interacts (inactive form) with EFHD2. Interacts with HAX1. Interacts with BIRC2/c-IAP1, XIAP/BIRC4, BIRC5/survivin, BIRC6/bruce and BIRC7/livin. Interacts with ABL1 (via SH3 domain); the interaction is direct and increases in the response of cells to genotoxic stress and ABL1/c-Abl activation. Interacts with BCL2L10 (PubMed:19255499). Interacts with NleF from pathogenic E.coli
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SwissProt ID
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Synonyms
CASP9; MCH6; Caspase-9; CASP-9; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3; ICE-like apoptotic protease 6; ICE-LAP6
Documentation
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Data Sheet (261 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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User Guide for Antibodies (1077 KB)
References
[1]. Allan LA, et al. Apoptosis and autophagy: Regulation of caspase-9 by phosphorylation. FEBS J. 2009 Nov;276(21):6063-73. [Content Brief]
[2]. Wolf BB, et al. Defective cytochrome c-dependent caspase activation in ovarian cancer cell lines due to diminished or absent apoptotic protease activating factor-1 activity. J Biol Chem. 2001 Sep 7;276(36):34244-51. [Content Brief]
[3]. Cao G, et al. Cloning and characterization of rat caspase-9: implications for a role in mediating caspase-3 activation and hippocampal cell death after transient cerebral ischemia. J Cereb Blood Flow Metab. 2002 May;22(5):534-46. [Content Brief]
[4]. Imao M, et al. Differential caspase-9-dependent signaling pathway between tumor necrosis factor receptor- and Fas-mediated hepatocyte apoptosis in mice. Liver Int. 2006 Feb;26(1):137-46. [Content Brief]
[5]. Malet G, et al. Small molecule inhibitors of Apaf-1-related caspase- 3/-9 activation that control mitochondrial-dependent apoptosis. Cell Death Differ. 2006 Sep;13(9):1523-32. [Content Brief]
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