Caspase 3 Antibody | Affinity Biosciences

$Fig. 3 AOS inhibited H2O2-induced apoptosis in HUVECs. Cells were pretreated using 200 lg/mL AOS before a 24 h stimulation using 400 lM H2O2, after which apoptosis was assessed by flow cytometry (a) and Hoechst 33,342 staining (b). The mRNA (c) and protein (d) levels of Bax, Bcl-2, and caspase 3. Data are expressed as mean ± S.E.M. and are representative of three independent experiments. *P\0.05 vs. control. **P \0.01 vs. control. # P \0.05 vs. H2O2. ##P \0.01 vs. H2O2$

Fig.

Figure 4.

Fig.

Figure 6 (A-C) Western blot analysis showing caspase-3/8 expression in AT2 cells.

Fig.

Supplementary Figure 4 Effect of high iodine on the expression of Cyclin A, Cyclin B, caspase 3 and cleaved caspase 3 in BCPAP and 8305C cells.

Figure 7.

Figure 2 Combination of cinobufotalin and gefitinib induces A549 cells apoptosis.

FIGURE 7 Relative protein levels of ALDH-2/4HNE/Caspase-3/cleaved caspase-3/Bax/Bcl-2 in the prefrontal cortex of CMS rats.

Figure 4 B3GALT5-AS1/CSNK2A1 axis regulates cell apoptosis.

FIGURE 5 Effect of BUB1 inhibition on the cell apoptosis and apoptosis‐related proteins.

Figure 8 | C-PC inhibits apoptosis in lung tissue and MLE-12 cells.

Figure 5 SLC25A21 overexpression induces cell apoptosis by the α-KG-mediated ROS pathway in BCa.

Figure 7.

Figure 4 The expression of caspase-9, caspase-3, and Bcl-2 in the hippocampus of each group of mice (equation M7±S, n=4).

Figure 3 High expression of miR-301 can promote the invasion and proliferation of breast cancer cells as well as inhibit their apoptosis (A) Detection of miR-301 expression level by qRT-PCR.

Fig.

Figure 4.

Fig.

Figure 3 Effects of different doses of FJD on the Bcl-2 family protein (a) and the PI3K/AKT/mTOR/NF-κB (b) signaling pathway of protein levels in tumor tissues.

Fig.

FIGURE 4 Effects of ROF on cell apoptosis and viability: (A,B) Cell viability of ETH (200 mm) and ETH + ROF groups after treatment for 24 h.

Figure 3 Expression levels of mTOR pathway proteins, ERS-associated proteins, and apoptosis-associated proteins in WT, CLP, and CLP+4-PBA mouse groups.

Figure 4 Puerarin treatment activates cell apoptosis and related proteins, while suppressing IL-6, TNF-α, and CA125 levels and modulating CD3+CD4+CD3+/CD8+ T lymphocyte percentages in OC tumor-bearing Fischer 344 rats.

Figure 6 GLP prevented the increase in cell apoptosis in the penile tissue of DMED rats.

Figure 8 Treatment with C20/C22 led to increased proapoptotic protein expression and a caspase cascade response.

Figure 9 APL extract inhibited cardiomyocyte apoptosis of Iso-induced mice.

FIGURE 1 Chronic low-dose iAs-exposure promotes the malignant progression of Caco-2 cells.

Figure 2 Overexpression of circ-ITCH inhibits prostate cancer (PCa) cell growth and colony formation and promotes apoptosis in vitro.

Figure 5 Relative expression levels of NF-κB pathway-related proteins were measured via western blot assay.

Figure 1.

Figure 5.

Product:	Caspase 3 Antibody
Catalog:	AF6311
Description:	Rabbit polyclonal antibody to Caspase 3
Application:	WB IHC IF/ICC
Reactivity:	Human, Mouse, Rat, Bovine
Prediction:	Pig, Bovine, Horse, Sheep, Rabbit, Dog
Mol.Wt.:	37kDa; 32kD(Calculated).
Uniprot:	P42574
RRID:	AB_2835170

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Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific.

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MSDS

Data Sheet

COA

Protocols

WB Handbook

IHC Protocol

IF/ICC Protocol

Product Info

Source:

Rabbit

Application:

WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:200
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:

Human,Mouse,Rat,Bovine

Prediction:

Pig(86%), Horse(86%), Sheep(100%), Rabbit(100%), Dog(100%)

Clonality:

Polyclonal

Specificity:

Caspase 3 Antibody detects endogenous levels of total Caspase 3.

RRID:

AB_2835170
Cite Format: Affinity Biosciences Cat# AF6311, RRID:AB_2835170.

Conjugate:

Unconjugated.

Purification:

The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).

Storage:

Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.

Alias:

Fold/Unfold

A830040C14Rik; Apopain; CASP-3; CASP3; CASP3_HUMAN; Casp3a; Caspase 3; Caspase 3, apoptosis-related cysteine peptidase; Caspase 3, apoptosis-related cysteine protease; Caspase 3, apoptosis-related cysteine protease a; Caspase-3 subunit p12; CC3; CPP-32; CPP32; CPP32B; Cysteine protease CPP32; EC 3.4.22.56; LICE; mldy; OTTHUMP00000165052; OTTHUMP00000165053; OTTHUMP00000165054; PARP cleavage protease; Procaspase3; protein Yama; SCA 1; SCA-1; SREBP cleavage activity 1; Yama;

Immunogens

Immunogen:

Uniprot:

P42574(CASP3_HUMAN) >>Visit HPA database.

Gene(ID):

CASP3(836)

Expression:

P42574 CASP3_HUMAN:

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.

Description:

This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme.

Sequence:

P42574 CASP3_HUMAN:
Protein BLAST With
NCBI/
ExPASy/
Uniprot

MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species

Results

Score

Bovine

100

Sheep

100

Dog

100

Rabbit

100

Pig

Horse

Chicken

Xenopus

Zebrafish

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P42574 As Substrate

P42574

Site	PTM Type	Enzyme	Source
M1	Acetylation		Uniprot
T4	Phosphorylation		Uniprot
S7	Phosphorylation		Uniprot
S10	Phosphorylation		Uniprot
K11	Acetylation		Uniprot
K11	Ubiquitination		Uniprot
S12	Phosphorylation		Uniprot
K14	Ubiquitination		Uniprot
K19	Ubiquitination		Uniprot
S24	Phosphorylation		Uniprot
S26	Phosphorylation		Uniprot
S29	Phosphorylation		Uniprot
Y41	Phosphorylation		Uniprot
K57	Ubiquitination		Uniprot
S65	Phosphorylation		Uniprot
T67	Phosphorylation		Uniprot
K82	Acetylation		Uniprot
K82	Ubiquitination		Uniprot
K88	Ubiquitination		Uniprot
K105	Ubiquitination		Uniprot
K138	Ubiquitination		Uniprot
S150	Phosphorylation	Q16539 (MAPK14)	Uniprot
T152	Phosphorylation		Uniprot
C163	S-Nitrosylation		Uniprot
T174	Phosphorylation		Uniprot
S176	Phosphorylation		Uniprot
K210	Ubiquitination		Uniprot
K229	Ubiquitination		Uniprot
S249	Phosphorylation		Uniprot
K260	Ubiquitination		Uniprot
T270	Phosphorylation		Uniprot

Research Backgrounds

P42574_CASP3_HUMAN

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.

PTMs:

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.

Subcellular Location:

Cytoplasm.

Tissue Specificity:

Subunit Structure:

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.

Family&Domains:

Belongs to the peptidase C14A family.

Research Fields

· Cellular Processes > Cell growth and death > p53 signaling pathway. (View pathway)

· Cellular Processes > Cell growth and death > Apoptosis. (View pathway)

· Cellular Processes > Cell growth and death > Apoptosis - multiple species. (View pathway)

· Environmental Information Processing > Signal transduction > MAPK signaling pathway. (View pathway)

· Environmental Information Processing > Signal transduction > TNF signaling pathway. (View pathway)

· Human Diseases > Drug resistance: Antineoplastic > Platinum drug resistance.

· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).

· Human Diseases > Neurodegenerative diseases > Alzheimer's disease.

· Human Diseases > Neurodegenerative diseases > Parkinson's disease.

· Human Diseases > Neurodegenerative diseases > Amyotrophic lateral sclerosis (ALS).

· Human Diseases > Neurodegenerative diseases > Huntington's disease.

· Human Diseases > Infectious diseases: Bacterial > Epithelial cell signaling in Helicobacter pylori infection.

· Human Diseases > Infectious diseases: Bacterial > Pertussis.

· Human Diseases > Infectious diseases: Bacterial > Legionellosis.

· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.

· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.

· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.

· Human Diseases > Infectious diseases: Viral > Hepatitis B.

· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.

· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.

· Human Diseases > Cancers: Overview > Pathways in cancer. (View pathway)

· Human Diseases > Cancers: Overview > Viral carcinogenesis.

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Human Diseases > Cancers: Overview > MicroRNAs in cancer.

· Human Diseases > Cancers: Specific types > Colorectal cancer. (View pathway)

· Human Diseases > Cancers: Specific types > Small cell lung cancer. (View pathway)

· Human Diseases > Cardiovascular diseases > Viral myocarditis.

· Organismal Systems > Immune system > Natural killer cell mediated cytotoxicity. (View pathway)

· Organismal Systems > Immune system > IL-17 signaling pathway. (View pathway)

· Organismal Systems > Nervous system > Serotonergic synapse.

References

1). Li X et al. Upregulation of BCL-2 by acridone derivative through gene promoter i-motif for alleviating liver damage of NAFLD/NASH. NUCLEIC ACIDS RESEARCH 2020 Jul 25;gkaa615. (PubMed: 32710621) [IF=14.9]

Application: WB Species: human Sample: HepG2

Figure 4. Effect of A22 on anti-apoptosis in 0.5 mM palmitic acid oil (PA) induced cell model. (A) Effect of A22 on cell viability for anti-apoptotic protective effect. (B) Effect of A22 on transcription of BCL-2 and BAX with measurement of mRNA levels. (C) Effect of A22 on protein expressions related with apoptosis (left), which were quantitatively analyzed (right). All the experiments were repeated for three times.

2). Wang QY et al. 2,3′,4,4′,5-Pentachlorobiphenyl induces mitochondria-dependent apoptosis mediated by AhR/Cyp1a1 in mouse germ cells. Journal of Hazardous Materials 2023 Mar 05;445(130547) (PubMed: 37055962) [IF=13.6]

3). Ye Wu et al. Precise editing of FGFR3-TACC3 fusion genes with CRISPR-Cas13a in glioblastoma. Molecular Therapy 2021 Jul 16;S1525-0016(21)00356-7. (PubMed: 34274537) [IF=12.4]

4). Fan H et al. Heat shock protein 22 modulates NRF1/TFAM-dependent mitochondrial biogenesis and DRP1-sparked mitochondrial apoptosis through AMPK-PGC1α signaling pathway to alleviate the early brain injury of subarachnoid hemorrhage in rats. Redox Biology 2021 Apr;40:101856. (PubMed: 33472123) [IF=11.4]

Application: WB Species: rat Sample: brain

Fig. 6. Hsp22 regulates PGC1α via AMPK signaling pathway in rats after SAH Beam balance scores, Modified Garcia scores and Brainwater content in various groups. n = 6 per group. (B) Representative photomicrographs of TUNEL staining and quantitative analyses in the indicated groups. n = 4 per group. Scale bar = 100 μm. (C) Typical photomicrographs showing double immunofluorescence staining of PGC1α (green) and NeuN (red) in diverse experimental groups. n = 4 per group. Scale bar = 50 μm. (D) Western blot images and quantitative analyses of p-AMPK/AMPK, PGC1α, Drp1, Nrf1, TFAM, UCP2, Cleaved caspase-3/Caspase-3, Bcl2, Bax, Cytosolic and mitochondrial cytochrome c. n = 6 per group. Bars represent mean ± SD. **P < 0.01, *P < 0.05 vs. Sham group. ##P < 0.01, #P < 0.05 vs. SAH + Vehicle group. &&P < 0.01, &P < 0.05 vs. SAH + hsp22+scramble siRNA. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

5). Tian S et al. Widening the Lens on Prothioconazole and Its Metabolite Prothioconazole-Desthio: Aryl Hydrocarbon Receptor-Mediated Reproductive Disorders through in Vivo, in Vitro, and in Silico Studies. ENVIRONMENTAL SCIENCE & TECHNOLOGY 2022 Dec 20;56(24):17890-17901. (PubMed: 36332113) [IF=11.4]

6). Zhang R et al. AKAP8L enhances the stemness and chemoresistance of gastric cancer cells by stabilizing SCD1 mRNA. Cell Death & Disease 2022 Dec 15;13(12):1041. (PubMed: 36522343) [IF=9.0]

7). Zhu H et al. CircGCN1L1 promotes synoviocyte proliferation and chondrocyte apoptosis by targeting miR-330-3p and TNF-α in TMJ osteoarthritis. Cell Death & Disease 2020 Apr 24;11(4):284 (PubMed: 32332704) [IF=9.0]

Application: WB Species: human Sample: synovial cells

Fig. 5 MiR-330-3p mediates the function of circGCN1L1 in human TMJ synoviocyte. a The synovial cells from the control patient were transiently transfected with miR-330-3p mimics, miR-330-3p mimic NC, miR-330-3p inhibitor, or miR-330-3p inhibitor NC, respectively. Forty-eight hours later, the levels of MMP13, MMP3, COL2A1, and ADAMTS4 were detected using WB. N = 4 (four independent experiments). b CircGCNL1 with/ without miR-330-3p mimics was transfected into co-cultured synoviocytes. After 2 days of co-culture, proteins were extracted from chondrocytes in the lower chamber, and WB was performed to detect the levels of MMP13, MMP3, COL2A1, ADAMTS4, TNF-α, p65, Bcl-2, Bax, caspase-3, and cleaved caspase-3. N = 4 (four independent experiments). Data are presented as mean ± S.D. One-way ANOVA with Bonferroni test was performed. WB western blotting, NC normal control, MMP matrix metalloproteinase, TNF tumor necrosis factor, Bcl-2 B-cell lymphoma-2, Bax BCL2-associated X, COL2A1 collagen type II alpha 1.

Application: WB Species: human Sample: human TMJ synoviocyte

Fig. 5 |MiR-330-3p mediates the function of circGCN1L1 in human TMJ synoviocyte..b CircGCNL1 with/without miR-330-3p mimics was transfected into co-cultured synoviocytes. After 2 days of co-culture, proteins were extracted from chondrocytes in the lower chamber, and WB was performed to detect the levels of MMP13, MMP3, COL2A1, ADAMTS4, TNF-α, p65, Bcl-2, Bax, caspase-3, and cleaved caspase-3. N = 4 (four independent experiments). Data are presented as mean ± S.D. One-way ANOVA with Bonferroni test was performed. WB western blotting, NC normal control, MMP matrix metalloproteinase, TNF tumor necrosis factor, Bcl-2 B-cell lymphoma-2, Bax BCL2-associated X,COL2A1 collagen type II alpha 1.

8). Liu P et al. Cytotoxicity of adducts formed between quercetin and methylglyoxal in PC-12 cells. Food Chemistry 2021 Aug 1;352:129424. (PubMed: 33706136) [IF=8.8]

Application: WB Species: Rat Sample: PC-12 cells

Fig. 5. Effect of treatments of MGO, Que-mono-MGO, and Que-di-MGO on the expression levels of apoptotic markers and components of AKT and Nrf2-HO-1/NQO-1 signaling pathways. Significant differences (p < 0.05) between samples of different treatments are marked with different letters on each column.

9). Wu H et al. LNC473 regulating APAF1 IRES-dependent translation via competitive sponging miR574 and miR15b: Implications in colorectal cancer. Molecular Therapy-Nucleic Acids 2020 Sep 4;21:764-779. (PubMed: 32784109) [IF=8.8]

Application: WB Species: Human Sample: HCT116 and SW480 Cells

Figure 6 LNC473-miR574/miR15b-APAF1 Signaling Axis in HCT116 and SW480 Cells (A) IF and ISH combination assay revealing the co-localization of APAF1 protein with included ncRNAs in HCT116 cells. Scale bars, 5 μm. (B and C) The levels of APAF1 mRNA (B) and protein (C) were determined after interfering LNC473 expression in HCT116 and SW480 cells by qPCR and IF assays. Scale bars, 20 μm. (D) The expression of apoptosis-related proteins including APAF1 was detected after interfering LNC473 expression in HCT116 and SW480 cells by western blot assay. (E and F) Rescue experiments showing the APAF1 levels in HCT116 and SW480 cells with exposure to the co-transfection of pcDH-LNC473 vector and miR574-5p or miR15b-5p mimic by qPCR (E) and western blot (F) assays. (G) Pattern diagram of APAF1-CDS and APAF1-IRES-CDS vectors. (H and I) APAF1 protein expression was determined in HCT116 and SW480 cells treated with APAF1-IRES-CDS vector, or pcDH-LNC473 and APAF1-IRES-CD co-transfection by western blot (H) and IF assays (I). Scale bars, 5 μm. (J) The percentage (%) of cell apoptosis in cells upon co-overexpressing APAF1-CDS or APAF1-IRE-CDS and LNC473 as assayed by flow cytometry. All tests were performed at least three times. Data were expressed as mean ± SD. ns (nonsignificant), p > 0.05; ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001, ∗∗∗∗p < 0.0001.

10). Shi M et al. Synthesis, characterization, and cytotoxicity analysis of selenium nanoparticles stabilized by Morchella sextelata polysaccharide. International Journal of Biological Macromolecules 2023 May 27; (PubMed: 37247714) [IF=8.2]

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Caspase 3 Antibody - #AF6311

Related products

Related Downloads

MSDS

Data Sheet

COA

Protocols

WB Handbook

IHC Protocol

IF/ICC Protocol

Product Info

Immunogens

Predictions

PTMs - P42574 As Substrate

Research Backgrounds

Research Fields

References

Restrictive clause