Product Name	Caspase-3
Chinese Name	活化半胱胺酸蛋白酶蛋白-3抗体
Alias	Caspase-3 subunit p17; cleaved Caspase 3; cleaved Caspase-3; APOPAIN; CASP3; Caspase 3 apoptosis related cysteine protease; Caspase3; CPP32; CPP32B; Cysteine protease CPP32; Human cysteine protease CPP32 isoform alpha mRNA complete cds; PARP cleavage protease; SCA 1; SCA1; SREBP cleavage activity 1; Yama; CASP3_HUMAN; Caspase-3; CASP-3; Apopain; Protein Yama; SREBP cleavage activity 1; SCA-1.
literatures	Specific References  (269)     |     SL0081R has been referenced in 269 publications. [IF=18.027] Shikai Liu. et al. On-Demand Generation of Peroxynitrite from an Integrated Two-Dimensional System for Enhanced Tumor Therapy. ACS NANO. 2022;XXXX(XXX):XXX-XXX  WB ;  Human.   PubMed:35666853 [IF=16.907] Yunxiang Sun. et al. Spontaneous formation of β-sheet nano-barrels during the early aggregation of Alzheimer’s amyloid beta. Nano Today. 2021 Jun;38:101125  WB ;  Mouse.   PubMed:10.1016/j.nantod.2021.101125 [IF=16.744] Zhanlin Zhang. et al. Persistent luminescence-activated Janus nanomotors with integration of photodynamic and photothermal cancer therapies. CHEM ENG J. 2022 Dec;:141226  IHC ;  Mouse.   PubMed:10.1016/j.cej.2022.141226 [IF=14.957] Zhanwei Zhou. et al. Pore forming–mediated intracellular protein delivery for enhanced cancer immunotherapy. SCI ADV. 2022 Nov;  WB ;  Mouse.   PubMed:36399575 [IF=13.273] Long Zhao. et al. Juglone-loaded metal-organic frameworks for H2O2 self-modulating enhancing chemodynamic therapy against prostate cancer. Chem Eng J. 2022 Feb;430:133057  IHC ;  Mouse.   PubMed:10.1016/j.cej.2021.133057 [IF=11.556] Mingyue Chen. et al. Resveratrol ameliorates polycystic ovary syndrome via transzonal projections within oocyte-granulosa cell communication. Theranostics. 2022; 12(2): 782–795  WB ;  Rat.   PubMed:34976213 [IF=11.467] Jie Meng. et al. Pyroelectric Janus nanomotors to promote cell internalization and synergistic tumor therapy. J CONTROL RELEASE. 2023 May;357:342  IHC ;  Mouse.   PubMed:37030542 [IF=11.092] Junwu Wei. et al. Photothermal Propelling and Pyroelectric Potential-Promoted Cell Internalization of Janus Nanoparticles and Pyroelectrodynamic Tumor Therapy. ADV HEALTHC MATER. 2023 Mar;:2300338  IHC ;  Mouse.   PubMed:36857737 [IF=9.918] Jie Hao. et al. Multifunctional miR181a nanoparticles promote highly efficient radiotherapy for rectal cancer. MATER TODAY ADV. 2022 Dec;16:100317  WB, IHC ;  Mouse.   PubMed:10.1016/j.mtadv.2022.100317 [IF=9.91] Li, Ting, et al. "Proliferation of parenchymal microglia is the main source of microgliosis after ischaemic stroke." Brain (2013): awt287.  Mouse.   PubMed:24154617 [IF=9.811] Nicholas Andrikopoulos. et al. Inhibition of Amyloid Aggregation and Toxicity with Janus Iron Oxide Nanoparticles. Chem Mater. 2021;XXXX(XXX):XXX-XXX  WB ;  Mouse.   PubMed:10.1021/acs.chemmater.1c01947 [IF=9.429] Li, Guang. et al. Synergetic delivery of artesunate and isosorbide 5-mononitrate with reduction-sensitive polymer nanoparticles for ovarian cancer chemotherapy. J NANOBIOTECHNOL. 2022 Dec;20(1):1-13  WB ;  Human.   PubMed:36335352 [IF=9.112] Chen, Ta-Fu. et al. White matter pathology in alzheimer’s transgenic mice with chronic exposure to low-level ambient fine particulate matter. PART FIBRE TOXICOL. 2022 Dec;19(1):1-14  IHC ;  Mouse.   PubMed:35768852 [IF=8.355] Chen Z et al. Enzyme-powered Janus nanomotors launched from intratumoral depots to address drug delivery barriers. Chemical Engineering Journal,2019 375, 122109.  IHC ;  Mouse.   PubMed:doi:10.1016/j.cej.2019.122109 [IF=8.355] Xie S et al. Bacteria-propelled microrockets to promote the tumor accumulation and intracellular drug uptake. Chemical Engineering Journal,2019, 123786.  IHC ;  Mouse.   PubMed:doi:10.1016/j.cej.2019.123786 [IF=7.666] Ana Carla Castro-Guijarro. et al. Combination Treatment of Retinoic Acid Plus Focal Adhesion Kinase Inhibitor Prevents Tumor Growth and Breast Cancer Cell Metastasis. CELLS-BASEL. 2022 Jan;11(19):2988  WB ;  Human.   PubMed:36230951 [IF=7.6] Teng, I., et al. "Phospholipid-functionalized mesoporous silica nanocarriers for selective photodynamic therapy of cancer." Biomaterials (2013).  WB ;  Mouse.   PubMed:23810081 [IF=7.504] He, Nan, et al. "Tumor pH-responsive Release of Drug-conjugated Micelles from Fiber Fragments for Intratumoral Chemotherapy." ACS Applied Materials & Interfaces (2017).  other ;   PubMed:28876891 [IF=7.419] Abulaiti Abulizi. et al. Quince extract resists atherosclerosis in rats by down-regulating the EGFR/PI3K/Akt/GSK-3β pathway. BIOMED PHARMACOTHER. 2023 Apr;160:114330  WB ;  Rat.   PubMed:36746094 [IF=7.419] Ziyang Huang. et al. Protective effect of ZYMT, a traditional Chinese patent medicine in a mouse model of retinitis pigmentosa. BIOMED PHARMACOTHER. 2023 Jun;162:114580  IF ;  Mouse.   PubMed:36989720 [IF=7.169] Chen Ting-ting. et al. β-arrestin2 deficiency ameliorates S-100-induced autoimmune hepatitis in mice by inhibiting infiltration of monocyte-derived macrophage and attenuating hepatocyte apoptosis. ACTA PHARMACOL SIN. 2023 May;:1-17  IF,ICC ;  Mouse，Human.   PubMed:37225848 [IF=7.129] Furui Han. et al. In vivo and in vitro study on hepatotoxicity of Tris-(2, 3-dibromopropyl) isocyanurate exposure via mitochondrial and death receptor pathway. ECOTOX ENVIRON SAFE. 2022 Nov;246:114186  WB ;  Rat, Human.   PubMed:36244175 [IF=7.129] Beiyu Zhang. et al. ZnO-NPs alleviate aflatoxin B1-induced hepatoxicity in ducklings by promoting hepatic metallothionein expression. ECOTOX ENVIRON SAFE. 2023 May;256:114826  WB ;  Duck.   PubMed:36989561 [IF=6.792] Jiayi Li. et al. Toxicological effects of deltamethrin on quail cerebrum: Weakened antioxidant defense and enhanced apoptosis. Environ Pollut. 2021 Oct;286:117319  WB ;  Quail.   PubMed:33990053 [IF=6.551] Wei J et al. Endosulfan induces cardiotoxicity through apoptosis via unbalance of pro-survival and mitochondrial-mediated apoptotic pathways. Sci Total Environ . 2020 Jul 20;727:138790.  WB ;  human.   PubMed:32344260 [IF=6.543] Peng Jialing. et al. MPO/HOCl Facilitates Apoptosis and Ferroptosis in the SOD1G93A Motor Neuron of Amyotrophic Lateral Sclerosis. Oxid Med Cell Longev. 2022;2022:8217663  WB ;  Mouse.   PubMed:35178161 [IF=6.384] Xiaowei Qin. et al. Neddylation inactivation affects cell cycle and apoptosis in sheep follicular granulosa cells. J CELL PHYSIOL. 2022 May 16  WB ;  Sheep.   PubMed:35578798 [IF=6.383] Xie S et al. Bacterial microbots for acid-labile release of hybrid micelles to promote the synergistic antitumor efficacy.Acta Biomater. 2018 Sep 15;78:198-210.  IHC-P ;  Mouse.   PubMed:30036720 [IF=6.375] Zhou,et al.CXCR4 antagonist AMD3100 enhances the response of MDA-MB-231 triple-negative breast cancer cells to ionizing radiation.(2018) Cancer Letters. 418:196-203.  IHC-P + WB ;  Mouse.   PubMed:29317253 [IF=6.291] Peng Zheng. et al. Alleviative effect of melatonin on the decrease of uterine receptivity caused by blood ammonia through ROS/NF-κB pathway in dairy cow. Ecotox Environ Safe. 2022 Feb;231:113166  WB ;  Bovine.   PubMed:35030520
Research Area	Tumour  Cell biology  Neurobiology  Signal transduction  Apoptosis  Alzheimer's
Immunogen Species	Rabbit
Clonality	Polyclonal
React Species	Human, Mouse, Rat,
Applications	WB=1:500-2000 ELISA=1:5000-10000 IHC-P=1:100-500 ICC=1:100 IF=1:100-500 （Paraffin sections need antigen repair） not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user.
Theoretical molecular weight	17/32kDa
Cellular localization	cytoplasmic
Form	Liquid
Concentration	1mg/ml
immunogen	KLH conjugated synthetic peptide derived from human caspase-3 p17 subunit: 80-175/277
Lsotype	IgG
Purification	affinity purified by Protein A
Buffer Solution	0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
Storage	Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.
Attention	This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
PubMed	PubMed
Product Detail	The caspase family of cysteine proteases play a key role in apoptosis. Caspase 3 is the most extensively studied apoptotic protein among caspase family members. Caspase 3 is synthesized as inactive pro enzyme that is processed in cells undergoing apoptosis by self proteolysis and/or cleavage by other upstream proteases (e.g. Caspases 8, 9 and 10). The processed form of Caspase 3 consists of large (17kDa) and small (12kDa) subunits which associate to form an active enzyme. Caspase 3 is cleaved at Asp28 Ser29 and Asp175 Ser176. The active Caspase 3 proteolytically cleaves and activates other caspases (e.g. Caspases 6, 7 and 9), as well as relevant targets in the cells (e.g. PARP and DFF). Alternative splicing of this gene results in two transcript variants which encode the same protein. In immunohistochemical studies Caspase 3 expression has been shown to be widespread but not present in all cell types (e.g. commonly reported in epithelial cells of skin, renal proximal tubules and collecting ducts). Differences in the level of Caspase 3 have been reported in cells of short lived nature (eg germinal centre B cells) and those that are long lived (eg mantle zone B cells). Caspase 3 is the predominant caspase involved in the cleavage of amyloid beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. Reacts with Caspase-3 subunit p17 and precursor. Function: 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. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. 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. Subcellular Location: Cytoplasm. Tissue Specificity: 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. Post-translational modifications: Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa. S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol. Similarity: Belongs to the peptidase C14A family. SWISS: P42574 Gene ID: 836 Database links: Entrez Gene: 836 Human Entrez Gene: 12367 Mouse Entrez Gene: 397244 Pig Entrez Gene: 100008840 Rabbit Entrez Gene: 25402 Rat Omim: 600636 Human SwissProt: P42574 Human SwissProt: P70677 Mouse SwissProt: Q95ND5 Pig SwissProt: Q8MJC3 Rabbit SwissProt: P55213 Rat Unigene: 141125 Human Unigene: 34405 Mouse Unigene: 10562 Rat Caspase3广泛分布于各种不同类型的细胞中，是Caspase家族中最重要的凋亡执行者之一，激活的Caspase-3能使许多与细胞结构、细胞周期及DNA修复等相关蛋白或激酶失活，从而使Apoptosis.
Product Picture	Sample: Lane 1: Spleen (Mouse) Lysate at 40 ug Lane 2: Lung (Mouse) Lysate at 40 ug Lane 3: Lymph node (Mouse) Lysate at 40 ug Lane 4: Cerebrum (Mouse) Lysate at 40 ug Lane 5: NIH/3T3 (Mouse) Cell Lysate at 30 ug Lane 6: Spleen (Rat) Lysate at 40 ug Lane 7: Lung (Rat) Lysate at 40 ug Lane 8: Lymph node (Rat) Lysate at 40 ug Lane 9: Cerebrum (Rat) Lysate at 40 ug Lane 10: Hela (Human) Cell Lysate at 30 ug Primary: Anti-Caspase-3 (SL0081R) at 1/1000 dilution Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution Predicted band size: 35 kD Observed band size: 37 kD Sample: Lane 1: Raji (Human) Cell Lysate at 30 ug Lane 2: NIH/3T3 (Mouse) Cell Lysate at 30 ug Lane 3: Lung (Mouse) Lysate at 40 ug Lane 4: Lung (Rat) Lysate at 40 ug Primary: Anti-Caspase-3 (SL0081R) at 1/1000 dilution Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution Predicted band size: 35 kD Observed band size: 37 kD Sample: Kidney (Mouse) Lysate at 40 ug Primary: Anti-Caspase-3 (SL0081R) at 1/300 dilution Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution Predicted band size: 28 kD Observed band size: 17 kD Sample: Lung(Mouse) Lysate at 40 ug Hela(Human) Cell Lysate at 30 ug NIH/3T3(Mouse) Cell Lysate at 30 ug Primary: Anti-Caspase-3 (SL0081R) at 1/1000 dilution Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution Predicted band size: 35/29/19/17 kD Observed band size: 38 kD Tissue/cell: rat brain tissue; 4% Paraformaldehyde-fixed and paraffin-embedded; Antigen retrieval: citrate buffer ( 0.01M, pH 6.0 ), Boiling bathing for 15min; Block endogenous peroxidase by 3% Hydrogen peroxide for 30min; Blocking buffer (normal goat serum,C-0005) at 37℃ for 20 min; Incubation: Anti-Caspase-3 Polyclonal Antibody, Unconjugated(SL0081R) 1:200, overnight at 4癈, followed by conjugation to the secondary antibody(SP-0023) and DAB(C-0010) staining Tissue/cell: rabbit pancreas tissue; 4% Paraformaldehyde-fixed and paraffin-embedded; Antigen retrieval: citrate buffer ( 0.01M, pH 6.0 ), Boiling bathing for 15min; Block endogenous peroxidase by 3% Hydrogen peroxide for 30min; Blocking buffer (normal goat serum,C-0005) at 37℃ for 20 min; Incubation: Anti-Caspase-3 Polyclonal Antibody, Unconjugated(SL0081R) 1:300, overnight at 4癈, followed by conjugation to the secondary antibody(SP-0023) and DAB(C-0010) staining Tissue/cell: NIH/3T3 cell; 4% Paraformaldehyde-fixed; Triton X-100 at room temperature for 20 min; Blocking buffer (normal goat serum, C-0005) at 37°C for 20 min; Antibody incubation with (Caspase-3) polyclonal Antibody, Unconjugated (SL0081R) 1:100, 90 minutes at 37°C; followed by a FITC conjugated Goat Anti-Rabbit IgG antibody at 37°C for 90 minutes, DAPI (blue, C02-04002) was used to stain the cell nuclei. The figure annotation: The blue histogram is unstained cells . The Orange histogram is cells stained with Rabbit IgG/FITC (SL0295P-FITC). The green histogram is cells stained with Rabbit Anti-Caspase-3/FITC Conjugated antibody (SL0081R-FITC). Controls Positive control: HepG 2 cells Isotype control: Cell lines treated with Rabbit IgG/FITC (SL0295P-FITC) instead of the primary antibody to confirm that primary antibody binding is specific. 2μg in 1 00μL1 X PBS containing 0.5% BSA. The figure annotation: The blue histogram is unstained cells. The Orange histogram is cells stained with Rabbit IgG/FITC (SL0295P-FITC). The green histogram is cells stained with Rabbit Anti-Caspase-3/FITC Conjugated antibody (SL0081R-FITC). Controls Positive control: A549 cells Isotype control: Cell lines treated with Rabbit IgG/FITC(SL0295P-FITC) instead of the primary antibody to confirm that primary antibody binding is specific. 3μg in 1 00 μL 1 X PBS containing 0.5% BSA. Blank control:Mouse spleen. Primary Antibody (green line): Rabbit Anti-Caspase-3 antibody (SL0081R) Dilution: 2μg /10^6 cells; Isotype Control Antibody (orange line): Rabbit IgG . Secondary Antibody : Goat anti-rabbit IgG-AF488 Dilution: 1μg /test. Protocol The cells were fixed with 4% PFA (10min at room temperature)and then permeabilized with 0.1% PBST for 20 min at room temperature. The cells were then incubated in 5%BSA to block non-specific protein-protein interactions for 30 min at room temperature .Cells stained with Primary Antibody for 30 min at room temperature. The secondary antibody used for 40 min at room temperature. Acquisition of 20,000 events was performed.

Cartpieces

• 
• 1

  1Delete

• 
• 5

  5Delete

• 
• S

  SDelete

• 
• R

  RDelete

• 
• +

  +Delete

• 
• 1

  1Delete

• Delete

• Delete

• 
• 1

  1Delete

• 
• 1

  1Delete

• 
• $

  $Delete

• 
• 0

  0Delete

• 
• 5

  5Delete

• 
• $

  $Delete

• 
• 0

  0Delete

• 
• 0

  0Delete

• 
• 1

  1Delete

• 
• C

  CDelete

• 
• C

  CDelete

• 

• Delete

• 
• i

  iDelete

• 
• i

  iDelete

• Delete

• 
• 1

  1Delete

• Delete

• 
• 1

  1Delete

• 
• 1

  1Delete

• 
• 0

  0Delete

• Delete

• 
• 2

  2Delete

• 
• 1

  1Delete

• 
• 0

  0Delete

• 
• 0

  0Delete

• 
• 0

  0Delete

• 
• 0

  0Delete

• 
• 0

  0Delete

• 
• 0

  0Delete

• 
• 1

  1Delete

• 
• 1

  1Delete

• Delete

• 
• -

  -Delete

• 
• -

  -Delete

• 
• 0

  0Delete

• Delete

• 
• t

  tDelete

• 
• 0

  0Delete

• 
• 0

  0Delete

• 
• 0

  0Delete

• 
• f

  fDelete

• Delete

• Delete

• Delete

• Delete

• Delete

• Delete

• Delete

• Delete

• Delete

• Delete

• Delete

• Delete

• Delete

• Delete

• 
• 5

  5Delete

• 
• $

  $Delete

• Delete

• 
• 0

  0Delete

• Delete

• Delete

• Delete

• 
• R

  RDelete

• 
• 5

  5Delete

• 
• A

  ADelete

Totalgoods,subtotals:￥Checkout