Product: Caspase 3 Antibody
Catalog: DF6879
Description: Rabbit polyclonal antibody to Caspase 3
Application: WB IF/ICC IP
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken
Mol.Wt.: 17kDa,19kDa,35kDa; 32kD(Calculated).
Uniprot: P42574
RRID: AB_2838838

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 100ul $280 In stock
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Product Info

Source:
Rabbit
Application:
WB 1:500-1:1000, IP 1:50-1:100, IF/ICC 1:100-1:500
*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
Prediction:
Pig(86%), Bovine(100%), Horse(86%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(86%)
Clonality:
Polyclonal
Specificity:
Caspase 3 Antibody detects endogenous levels of total Caspase 3.
RRID:
AB_2838838
Cite Format: Affinity Biosciences Cat# DF6879, RRID:AB_2838838.
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:
Gene(ID):
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:
Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins such as the nuclear enzyme poly(ADP-ribose) polymerase (PARP) (1). Activation of caspase-3 requires proteolytic processing of its inactive zymogen into activated p17 and p12 fragments. Cleavage of caspase-3 requires aspartic acid at the P1 position (2).
Sequence:
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
86
Horse
86
Chicken
86
Xenopus
57
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P42574 As Substrate

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

Research Backgrounds

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.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
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.

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). Melatonin derivatives combat with inflammation-related cancer by targeting the Main Culprit STAT3. EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY (PubMed: 33248852) [IF=6.7]

Application: WB    Species: human    Sample: HCT-116 cells

Figure 10. (A) Compound P-3 triggered the explosion of ROS in HCT-116 cells. (magnification 20 ×, scale bar = 100 μm) (B) P-3 regulated the expression of proteins involved in Cyto-c/Caspase3 pathway. Data are presented as mean ± SD from three independent experiments. * P < 0.05, ** P<0.01, *** P<0.001 versus the control group.

2). The GDF11 Promotes Nerve Regeneration After Sciatic Nerve Injury in Adult Rats by Promoting Axon Growth and Inhibiting Neuronal Apoptosis. Frontiers in Bioengineering and Biotechnology (PubMed: 35059389) [IF=5.7]

Application: WB    Species: Rat    Sample: DGR Cells

FIGURE 2 GDF11 inhibited apoptosis of DGR in vitro. (A and B). Flow cytometry was used to detect the degree of apoptosis of DRG after cultured with recombinant GDF11 for 3 days. (C, D and E). DRG were cultured with recombinant GDF11 for 3 days, and mRNA expression of apoptosis-related genes Bcl2, Bax and caspase3 were detected by RT-PCR. (F, G, H and I). After DRG were cultured with recombinant GDF11 for 3 days, the protein expressions of apoptosis-related genes Bcl2, Bax and caspase3 were detected by Western blot. Statistical analysis was based on at least three different biological samples and three technical replicates, p < 0.05 was considered to be statistically significant.

3). TNF‐α induces up‐regulation of MicroRNA‐27a via the P38 signalling pathway, which inhibits intervertebral disc degeneration by targeting FSTL1. Journal of Cellular and Molecular Medicine (PubMed: 34190406) [IF=5.3]

Application: WB    Species: Human    Sample: NP cells

FIGURE 2 Overexpression of miR27a in nucleus pulposus cells inhibits apoptosis and the production of inflammatory cytokines. (A) The transfection efficiency of miR27a as detected by qPCR. (B, C, D, E and F) NP cells were transfected with miR27a mimics or NC for 24 h and then treated with 10 ng/mL TNF‐α. After 24 h, COX2 expression was detected by immunofluorescence (B, C), qPCR (D) and Western blotting (E, F). (E, G, H, I) NP cells were transfected with miR27a mimics or NC for 24 h and then treated with 10 ng/mL TNF‐α. After 24 h, Bcl2, Bax and caspase 3 expression was detected by Western blotting. (J, K) NP cells were transfected with miR27a mimics or NC for 24 h and then treated with 10 ng/mL TNF‐α. After 24 h, apoptosis was detected by flow cytometry. Statistical analysis was based on at least three different biological samples and three technical replicates; P < .05 was considered to be statistically significant. Representative images are shown

4). miR‑576‑3p overexpression enhances cisplatin sensitivity of ovarian cancer cells by dysregulating PD‑L1 and cyclin D1. Molecular Medicine Reports (PubMed: 33236151) [IF=3.4]

5). Knockdown of lncRNA MIR503HG suppresses proliferation and promotes apoptosis of non-small cell lung cancer cells by regulating miR-489-3p and miR-625-5p. PATHOLOGY RESEARCH AND PRACTICE (PubMed: 31983569) [IF=2.8]

Application: WB    Species: Human    Sample: A549 and NCI-H2170 cells

Fig. 3. Knockdown of MIR503HG promoted the apoptosis of NSCLC cells. MIR503HG shRNA or NC shRNA were transfected in A549 and NCI-H2170 cells, respectively. (A–B) The apoptosis of A549 and NCI-H2170 cells was determined after transfection 48 h using TUNEL staining, Scale bar =50 μm. (C–F) The apoptosis of A549 and NCI-H2170 cells was detected by flow cytometry with Annexin Ⅴ/PI staining after transfection 48 h. (G–H) The protein levels of Bax, Bad, Bcl-2, Survivin, caspase-3, cleaved-caspase-3, caspase-9 and cleaved-caspase-9 were determined by western blot after transfection 48 h. The data were presented as mean ± SD and significant differences were indicated as **P < 0.01

6). Schisandrin A protects intestinal cells from mycophenolic acid-induced cytotoxicity and oxidative damage. Research Square

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