anti cleaved caspase 3  (Millipore)


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  • 99
    Name:
    Anti Caspase 3 antibody
    Description:
    Caspase 3 is a cytosolic protein present as a 32 kDa proenzyme in cells It is activated by proteolytic cleavage into the 20 kDa p20 and 11 kDa p11 active subunits when cells undergo apoptosis
    Catalog Number:
    c9598
    Price:
    None
    Applications:
    Anti-Caspase 3 antibody produced in rabbit is suitable for microarray and western blotting at a working dilution of 1:3000 using Jurkat human T-cell leukemia cell extract. It was used as a primary antibody for western blotting in a study to establish the biomolecular basis for the role of PCMT1 (isoaspartyl protein carboxyl-O-methyltransferase) as a part of a novel apoptosis regulatory mechanism. It was used to examine activation of caspase-3 via immunoblotting in a study to confirm the apoptosis of tumor cells mediated by AAV-ISN-T (recombinant adeno-associated virus vector with signal peptides of human insulin) administration. It was used as a primary antibody at 1:300 dilution for immunohistochemistry of deparaffinized sections of squamous cell carcinoma of the tongue containing surrounding normal tissue. It was used at a dilution of 1:1000 to detect caspase-3 and its cleaved form P20 in a study.
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    Structured Review

    Millipore anti cleaved caspase 3
    The functions of miR‐25‐3p inhibitors abolishing the effects of CHB‐PNALT‐Exo (≥A2) on the proliferation and metastasis were reversed by knockdown of TCF21 and HHIP in HepG2.2.15 cells. After siRNA‐TCF21 and siRNA‐HHIP were transfected into CHB‐PNALT‐Exo (≥A2) containing miR‐25‐3p inhibitor‐treated HepG2.2.15 cells, cell viability, apoptosis, invasion, migration and the expression of cleaved <t>caspase‐3/‐9,</t> Ki67 and E‐cadherin were detected by CCK‐8 assay (A), flow cytometry analysis (B), clone formation assay (C), transwell assay (D), scratch‐wound assay (E) and Western blot assay (F). GAPDH was used as a load control. Data are presented as the mean ± standard deviation. ** P
    Caspase 3 is a cytosolic protein present as a 32 kDa proenzyme in cells It is activated by proteolytic cleavage into the 20 kDa p20 and 11 kDa p11 active subunits when cells undergo apoptosis
    https://www.bioz.com/result/anti cleaved caspase 3/product/Millipore
    Average 99 stars, based on 31 article reviews
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    anti cleaved caspase 3 - by Bioz Stars, 2020-09
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    Images

    1) Product Images from "Exosomes secreted by chronic hepatitis B patients with PNALT and liver inflammation grade ≥ A2 promoted the progression of liver cancer by transferring miR‐25‐3p to inhibit the co‐expression of TCF21 and HHIP, et al. Exosomes secreted by chronic hepatitis B patients with PNALT and liver inflammation grade ≥ A2 promoted the progression of liver cancer by transferring miR‐25‐3p to inhibit the co‐expression of TCF21 and HHIP"

    Article Title: Exosomes secreted by chronic hepatitis B patients with PNALT and liver inflammation grade ≥ A2 promoted the progression of liver cancer by transferring miR‐25‐3p to inhibit the co‐expression of TCF21 and HHIP, et al. Exosomes secreted by chronic hepatitis B patients with PNALT and liver inflammation grade ≥ A2 promoted the progression of liver cancer by transferring miR‐25‐3p to inhibit the co‐expression of TCF21 and HHIP

    Journal: Cell Proliferation

    doi: 10.1111/cpr.12833

    The functions of miR‐25‐3p inhibitors abolishing the effects of CHB‐PNALT‐Exo (≥A2) on the proliferation and metastasis were reversed by knockdown of TCF21 and HHIP in HepG2.2.15 cells. After siRNA‐TCF21 and siRNA‐HHIP were transfected into CHB‐PNALT‐Exo (≥A2) containing miR‐25‐3p inhibitor‐treated HepG2.2.15 cells, cell viability, apoptosis, invasion, migration and the expression of cleaved caspase‐3/‐9, Ki67 and E‐cadherin were detected by CCK‐8 assay (A), flow cytometry analysis (B), clone formation assay (C), transwell assay (D), scratch‐wound assay (E) and Western blot assay (F). GAPDH was used as a load control. Data are presented as the mean ± standard deviation. ** P
    Figure Legend Snippet: The functions of miR‐25‐3p inhibitors abolishing the effects of CHB‐PNALT‐Exo (≥A2) on the proliferation and metastasis were reversed by knockdown of TCF21 and HHIP in HepG2.2.15 cells. After siRNA‐TCF21 and siRNA‐HHIP were transfected into CHB‐PNALT‐Exo (≥A2) containing miR‐25‐3p inhibitor‐treated HepG2.2.15 cells, cell viability, apoptosis, invasion, migration and the expression of cleaved caspase‐3/‐9, Ki67 and E‐cadherin were detected by CCK‐8 assay (A), flow cytometry analysis (B), clone formation assay (C), transwell assay (D), scratch‐wound assay (E) and Western blot assay (F). GAPDH was used as a load control. Data are presented as the mean ± standard deviation. ** P

    Techniques Used: Transfection, Migration, Expressing, CCK-8 Assay, Flow Cytometry, Tube Formation Assay, Transwell Assay, Scratch Wound Assay Assay, Western Blot, Standard Deviation

    The functions of CHB‐PNALT‐Exo (≥A2) promoting tumour growth in vivo were reversed by inhibition of miR‐25‐3p. HepG2.2.15 cells with CHB‐PNALT‐Exo (≥A2) or CHB‐PNALT‐Exo (≥A2) containing miR‐25‐3p inhibitor NC/miR‐25‐3p inhibitors were injected with nude mouse, respectively, (A) the photograph of tumour; (B) statistical graph of tumour volume; (C) statistical graph of tumour weight; (D) the expressions of Ki67, (E) cleaved caspase‐3 and (F) E‐cadherin was detected by IHC assay. Data are presented as the mean ± standard deviation. ** P
    Figure Legend Snippet: The functions of CHB‐PNALT‐Exo (≥A2) promoting tumour growth in vivo were reversed by inhibition of miR‐25‐3p. HepG2.2.15 cells with CHB‐PNALT‐Exo (≥A2) or CHB‐PNALT‐Exo (≥A2) containing miR‐25‐3p inhibitor NC/miR‐25‐3p inhibitors were injected with nude mouse, respectively, (A) the photograph of tumour; (B) statistical graph of tumour volume; (C) statistical graph of tumour weight; (D) the expressions of Ki67, (E) cleaved caspase‐3 and (F) E‐cadherin was detected by IHC assay. Data are presented as the mean ± standard deviation. ** P

    Techniques Used: In Vivo, Inhibition, Injection, Immunohistochemistry, Standard Deviation

    2) Product Images from "Hydrogen Peroxide–Inducible Clone-5 Regulates Mesangial Cell Proliferation in Proliferative Glomerulonephritis in Mice"

    Article Title: Hydrogen Peroxide–Inducible Clone-5 Regulates Mesangial Cell Proliferation in Proliferative Glomerulonephritis in Mice

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0122773

    Detection of apoptotic glomerular cells in Hic-5+/+ and Hic-5-/- glomerulonephritis (GN) mice. (a) Representative TUNEL (terminal deoxynucleotidyl transferase dUTP nick end labeling) staining (upper) and cleaved caspase-3 positive cells (lower). Apoptotic glomerular cells in GN were identified by fluorescence-labeled nuclei (yellow), indicated by arrows. The nuclei of glomerular cells were counterstained with propidium iodide (red). In addition, cleaved caspase-3 positive cells were detected by immunohistochemistry and indicated by arrows. Original magnification x200, scale bar = 50 μm. (b) The number of apoptotic glomerular cells was counted and calculated in 30 full-size glomeruli. (c) The number of cleaved caspase-3 positive cells was counted and calculated in 30 full-size glomeruli. The data are shown as the means ± SD. *, P
    Figure Legend Snippet: Detection of apoptotic glomerular cells in Hic-5+/+ and Hic-5-/- glomerulonephritis (GN) mice. (a) Representative TUNEL (terminal deoxynucleotidyl transferase dUTP nick end labeling) staining (upper) and cleaved caspase-3 positive cells (lower). Apoptotic glomerular cells in GN were identified by fluorescence-labeled nuclei (yellow), indicated by arrows. The nuclei of glomerular cells were counterstained with propidium iodide (red). In addition, cleaved caspase-3 positive cells were detected by immunohistochemistry and indicated by arrows. Original magnification x200, scale bar = 50 μm. (b) The number of apoptotic glomerular cells was counted and calculated in 30 full-size glomeruli. (c) The number of cleaved caspase-3 positive cells was counted and calculated in 30 full-size glomeruli. The data are shown as the means ± SD. *, P

    Techniques Used: Hydrophobic Interaction Chromatography, Mouse Assay, TUNEL Assay, Staining, Fluorescence, Labeling, Immunohistochemistry

    3) Product Images from "Neuroprotective effect of the glucagon-like peptide-1 receptor agonist, synthetic exendin-4, in streptozotocin-induced diabetic rats"

    Article Title: Neuroprotective effect of the glucagon-like peptide-1 receptor agonist, synthetic exendin-4, in streptozotocin-induced diabetic rats

    Journal: British Journal of Pharmacology

    doi: 10.1111/j.1476-5381.2011.01272.x

    (A) Double-labelling fluorescence of sciatic nerves in nondiabetic and diabetic rats with or without exendin-4. Arrows indicate the nuclei of apoptotic Schwann cells that were dual-stained by anti-cleaved caspase 3 (green) and DAPI (blue-white). (B) Bar
    Figure Legend Snippet: (A) Double-labelling fluorescence of sciatic nerves in nondiabetic and diabetic rats with or without exendin-4. Arrows indicate the nuclei of apoptotic Schwann cells that were dual-stained by anti-cleaved caspase 3 (green) and DAPI (blue-white). (B) Bar

    Techniques Used: Fluorescence, Staining

    4) Product Images from "Lin28a Protects against Hypoxia/Reoxygenation Induced Cardiomyocytes Apoptosis by Alleviating Mitochondrial Dysfunction under High Glucose/High Fat Conditions"

    Article Title: Lin28a Protects against Hypoxia/Reoxygenation Induced Cardiomyocytes Apoptosis by Alleviating Mitochondrial Dysfunction under High Glucose/High Fat Conditions

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0110580

    Antiapoptotic effect of Lin28a overexpression on cardiomyocytes after H/R injury in HG/HF conditions. Representative images of TUNEL-stained primary neonatal cardiomyocytes after H/R stress in HG/HF conditions (A). Apoptosis of the primary cardiomyocytes determined by Cy3-annexinV/PI double staining and flow cytometry (n = 3). Region B2: late apoptotic cells (Cy3/PI, where Cy3 is cyanine-3 and PI is propidium iodide); Region B3: vital cells; Region B4: early apoptotic cells (C). Apoptotic index is expressed as the percentage of TUNEL-positive myocytes (in red) over total nuclei determined by DAPI staining(B). Apoptotic rate is expressed as the percentage of late apoptotic cells and early apoptotic cells(D). Protein expression with representative gel blots of Caspase-3, Cleaved Caspase-3, Bcl-2, Bax and β-actin (loading control) (E). Caspase-3(F); Cleaved Caspase-3(G); Bcl-2(H); Bax(I); Bax/Bcl-2 ratio(J). The columns and error bars represent means and SD. Data were obtained from at least three independent experiments.*P
    Figure Legend Snippet: Antiapoptotic effect of Lin28a overexpression on cardiomyocytes after H/R injury in HG/HF conditions. Representative images of TUNEL-stained primary neonatal cardiomyocytes after H/R stress in HG/HF conditions (A). Apoptosis of the primary cardiomyocytes determined by Cy3-annexinV/PI double staining and flow cytometry (n = 3). Region B2: late apoptotic cells (Cy3/PI, where Cy3 is cyanine-3 and PI is propidium iodide); Region B3: vital cells; Region B4: early apoptotic cells (C). Apoptotic index is expressed as the percentage of TUNEL-positive myocytes (in red) over total nuclei determined by DAPI staining(B). Apoptotic rate is expressed as the percentage of late apoptotic cells and early apoptotic cells(D). Protein expression with representative gel blots of Caspase-3, Cleaved Caspase-3, Bcl-2, Bax and β-actin (loading control) (E). Caspase-3(F); Cleaved Caspase-3(G); Bcl-2(H); Bax(I); Bax/Bcl-2 ratio(J). The columns and error bars represent means and SD. Data were obtained from at least three independent experiments.*P

    Techniques Used: Over Expression, TUNEL Assay, Staining, Double Staining, Flow Cytometry, Cytometry, Expressing

    5) Product Images from "Hydroxytyrosol Protects against Myocardial Ischemia/Reperfusion Injury through a PI3K/Akt-Dependent Mechanism"

    Article Title: Hydroxytyrosol Protects against Myocardial Ischemia/Reperfusion Injury through a PI3K/Akt-Dependent Mechanism

    Journal: Mediators of Inflammation

    doi: 10.1155/2016/1232103

    HT decreased cleaved caspase-3 expression as compared with expression levels in the I/R group and the HT+LY+I/R group ( n = 4 for each group). Data are presented as means and SEM. ∗ P
    Figure Legend Snippet: HT decreased cleaved caspase-3 expression as compared with expression levels in the I/R group and the HT+LY+I/R group ( n = 4 for each group). Data are presented as means and SEM. ∗ P

    Techniques Used: Expressing

    6) Product Images from "A11, a novel diaryl acylhydrazone derivative, exerts neuroprotection against ischemic injury in vitro and in vivo"

    Article Title: A11, a novel diaryl acylhydrazone derivative, exerts neuroprotection against ischemic injury in vitro and in vivo

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/s41401-018-0028-4

    A11 inhibited apoptosis induced by OGD. a Apoptotic cells were detected by flow cytometry. b The apoptotic rate is represented as a histogram. Western blot analysis of cleaved Caspase-3 ( c ) and p53 ( d ) in SH-SY5Y cells treated with 1 μM A11 followed by exposure to OGD and cultured for 24 h after reoxygenation ( n = 4). The results represent the mean ± SEM of three to four independent experiments. ## P
    Figure Legend Snippet: A11 inhibited apoptosis induced by OGD. a Apoptotic cells were detected by flow cytometry. b The apoptotic rate is represented as a histogram. Western blot analysis of cleaved Caspase-3 ( c ) and p53 ( d ) in SH-SY5Y cells treated with 1 μM A11 followed by exposure to OGD and cultured for 24 h after reoxygenation ( n = 4). The results represent the mean ± SEM of three to four independent experiments. ## P

    Techniques Used: Flow Cytometry, Western Blot, Cell Culture

    7) Product Images from "Endogenous Selenoprotein P, a Liver-Derived Secretory Protein, Mediates Myocardial Ischemia/Reperfusion Injury in Mice"

    Article Title: Endogenous Selenoprotein P, a Liver-Derived Secretory Protein, Mediates Myocardial Ischemia/Reperfusion Injury in Mice

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms19030878

    SeP KO mice reduces apoptotic cells after myocardial I/R. LV tissue sections were subjected to TUNEL and 4′,6-diamidino-2-phenylindole (DAPI) staining. ( A ) Representative examples of TUNEL-positive myocytes in the ischemic area. Arrows indicate TUNEL-positive myocytes. ( B ) The number of TUNEL-positive myocytes was expressed as a percentage of total nuclei detected using DAPI staining. Heart homogenates were prepared from SeP KO and WT mice subjected to 30 min of ischemia and 24 h of reperfusion. Immunoblot analyses were performed using ( C ) anti-cleaved caspase-3 and GAPDH antibody. ( D ) Results of quantitative analysis of cleaved caspase-3 are shown. Data represent means from at least five mice each. * p
    Figure Legend Snippet: SeP KO mice reduces apoptotic cells after myocardial I/R. LV tissue sections were subjected to TUNEL and 4′,6-diamidino-2-phenylindole (DAPI) staining. ( A ) Representative examples of TUNEL-positive myocytes in the ischemic area. Arrows indicate TUNEL-positive myocytes. ( B ) The number of TUNEL-positive myocytes was expressed as a percentage of total nuclei detected using DAPI staining. Heart homogenates were prepared from SeP KO and WT mice subjected to 30 min of ischemia and 24 h of reperfusion. Immunoblot analyses were performed using ( C ) anti-cleaved caspase-3 and GAPDH antibody. ( D ) Results of quantitative analysis of cleaved caspase-3 are shown. Data represent means from at least five mice each. * p

    Techniques Used: Mouse Assay, TUNEL Assay, Staining

    8) Product Images from "A protease-activated receptor 1 antagonist protects against global cerebral ischemia/reperfusion injury after asphyxial cardiac arrest in rabbits"

    Article Title: A protease-activated receptor 1 antagonist protects against global cerebral ischemia/reperfusion injury after asphyxial cardiac arrest in rabbits

    Journal: Neural Regeneration Research

    doi: 10.4103/1673-5374.199011

    Effects of the PAR1 antagonist SCH79797 (SCH) and the PI3K/Akt inhibitor LY29004 (LY) on caspase 3 expression and activation after transient global cerebral ischemia/reperfusion (I/R) injury (western blot assay). (A) Representative immunoblots for pro-caspase 3 and cleaved caspase 3 in hippocampal tissue homogenates from the studied groups 48 hours after I/R. (B) Densitometry analysis results for cleaved caspase 3 at 48 hours after I/R. The graph shows the optical density ratio of cleaved caspase 3 to β-actin using data combined from three independent experiments after normalization to the loading control. Sham group: Sham-operated control rabbits; saline group: rabbits subjected to 3 minutes of cardiac arrest and administered saline; SCH group: rabbits subjected to 3 minutes of cardiac arrest and treated with the PAR1 receptor antagonist SCH79797 (25 μg/kg, intravenously) 10 minutes after cardiopulmonary resuscitation; LY + SCH group: rabbits that received the PI3K/Akt inhibitor LY29004 (3 mg/kg, intravenously) 10 minutes before SCH79797 administration. Data are expressed as the mean ± SD. Differences among groups were analyzed by one-way analysis of variance followed by Bonferroni post hoc tests. ** P
    Figure Legend Snippet: Effects of the PAR1 antagonist SCH79797 (SCH) and the PI3K/Akt inhibitor LY29004 (LY) on caspase 3 expression and activation after transient global cerebral ischemia/reperfusion (I/R) injury (western blot assay). (A) Representative immunoblots for pro-caspase 3 and cleaved caspase 3 in hippocampal tissue homogenates from the studied groups 48 hours after I/R. (B) Densitometry analysis results for cleaved caspase 3 at 48 hours after I/R. The graph shows the optical density ratio of cleaved caspase 3 to β-actin using data combined from three independent experiments after normalization to the loading control. Sham group: Sham-operated control rabbits; saline group: rabbits subjected to 3 minutes of cardiac arrest and administered saline; SCH group: rabbits subjected to 3 minutes of cardiac arrest and treated with the PAR1 receptor antagonist SCH79797 (25 μg/kg, intravenously) 10 minutes after cardiopulmonary resuscitation; LY + SCH group: rabbits that received the PI3K/Akt inhibitor LY29004 (3 mg/kg, intravenously) 10 minutes before SCH79797 administration. Data are expressed as the mean ± SD. Differences among groups were analyzed by one-way analysis of variance followed by Bonferroni post hoc tests. ** P

    Techniques Used: Expressing, Activation Assay, Western Blot

    9) Product Images from "PYR-41, A UBIQUITIN-ACTIVATING ENZYME E1 INHIBITOR, ATTENUATES LUNG INJURY IN SEPSIS"

    Article Title: PYR-41, A UBIQUITIN-ACTIVATING ENZYME E1 INHIBITOR, ATTENUATES LUNG INJURY IN SEPSIS

    Journal: Shock (Augusta, Ga.)

    doi: 10.1097/SHK.0000000000000931

    Detection of apoptosis in the lungs of mice after CLP Mice were sham-operated or subjected to CLP with intravenous injection of vehicle (20% DMSO in saline) or PYR-41 (5 mg/kg) immediately after CLP. Lungs were harvested at 20 h after CLP. (A) Lung tissue sections were immunostained with terminal deoxynucleotidyl transferase dUTP nick end-labeling (TUNEL; green) for apoptotic cells and propidium iodide (red) staining for nuclei. Representative images of each group at 200× magnification. (B) Graphical representation of TUNEL-positive staining cells averaged over 10 microscopic fields per mouse. (C) Western blot analysis of cleaved caspase-3 in lung tissue homogenates. Actin is used as a loading control. Blots were scanned and quantified with densitometry. The levels of protein expression in the sham group are designated 1 for comparison. Data are expressed as mean ± standard error (n = 5/group). * P
    Figure Legend Snippet: Detection of apoptosis in the lungs of mice after CLP Mice were sham-operated or subjected to CLP with intravenous injection of vehicle (20% DMSO in saline) or PYR-41 (5 mg/kg) immediately after CLP. Lungs were harvested at 20 h after CLP. (A) Lung tissue sections were immunostained with terminal deoxynucleotidyl transferase dUTP nick end-labeling (TUNEL; green) for apoptotic cells and propidium iodide (red) staining for nuclei. Representative images of each group at 200× magnification. (B) Graphical representation of TUNEL-positive staining cells averaged over 10 microscopic fields per mouse. (C) Western blot analysis of cleaved caspase-3 in lung tissue homogenates. Actin is used as a loading control. Blots were scanned and quantified with densitometry. The levels of protein expression in the sham group are designated 1 for comparison. Data are expressed as mean ± standard error (n = 5/group). * P

    Techniques Used: Mouse Assay, Injection, TUNEL Assay, Staining, Western Blot, Expressing

    10) Product Images from "Thromboxane promotes smooth muscle phenotype commitment but not remodeling of hypoxic neonatal pulmonary artery"

    Article Title: Thromboxane promotes smooth muscle phenotype commitment but not remodeling of hypoxic neonatal pulmonary artery

    Journal: Fibrogenesis & Tissue Repair

    doi: 10.1186/s13069-015-0037-6

    Immunostaining for apoptotic markers, active caspase 3 ( a ) and BAX ( b ), was analyzed by laser scanning cytometry in frozen sections of pulmonary artery from control and PPHN animals, following chronic exposure to U46619 added daily for 72 h in the absence of serum. Results expressed as integral intensity/mm 2  area (** p
    Figure Legend Snippet: Immunostaining for apoptotic markers, active caspase 3 ( a ) and BAX ( b ), was analyzed by laser scanning cytometry in frozen sections of pulmonary artery from control and PPHN animals, following chronic exposure to U46619 added daily for 72 h in the absence of serum. Results expressed as integral intensity/mm 2 area (** p

    Techniques Used: Immunostaining, Cytometry

    11) Product Images from "MicroRNA-181a knockdown protects HepaRG cells from Dichlorvos-induced oxidative stress and apoptosis"

    Article Title: MicroRNA-181a knockdown protects HepaRG cells from Dichlorvos-induced oxidative stress and apoptosis

    Journal: International Journal of Clinical and Experimental Pathology

    doi:

    The effect of miR-181a on DDVP induced cell apoptosis and ROS production. HepaRG cells were pretreated with miR-181a inhibitor/inhibitor NC for 12 h before DDVP treatment for 24 h (300 μM). A. The cell viability in different groups was analyzed by using CCK-8 kit. Cell viability was significantly inhibited in DDVP + inhibitor NC group and DDVP + miR-181a inhibitor group when compared with the controls. However, miR-181a inhibitor reversed DDVP-induced cell viability inhibition. B. The cell apoptosis was detected by flow cytometry. miR-181a inhibitor weakened DDVP-induced cell apoptosis. C, D. miR-181a inhibitor decreased DDVP-induced caspase-3 activity and ROS production. E. Cell viability was analyzed by using CCK-8 kit. miR-181a mimics promoted DDVP-induced cell viability inhibition. F. miR-181a mimics upregulated DDVP-induced cell apoptosis. G, H. miR-181a mimics enhanced DDVP-induced caspase-3 activity and ROS production.* P
    Figure Legend Snippet: The effect of miR-181a on DDVP induced cell apoptosis and ROS production. HepaRG cells were pretreated with miR-181a inhibitor/inhibitor NC for 12 h before DDVP treatment for 24 h (300 μM). A. The cell viability in different groups was analyzed by using CCK-8 kit. Cell viability was significantly inhibited in DDVP + inhibitor NC group and DDVP + miR-181a inhibitor group when compared with the controls. However, miR-181a inhibitor reversed DDVP-induced cell viability inhibition. B. The cell apoptosis was detected by flow cytometry. miR-181a inhibitor weakened DDVP-induced cell apoptosis. C, D. miR-181a inhibitor decreased DDVP-induced caspase-3 activity and ROS production. E. Cell viability was analyzed by using CCK-8 kit. miR-181a mimics promoted DDVP-induced cell viability inhibition. F. miR-181a mimics upregulated DDVP-induced cell apoptosis. G, H. miR-181a mimics enhanced DDVP-induced caspase-3 activity and ROS production.* P

    Techniques Used: CCK-8 Assay, Inhibition, Flow Cytometry, Cytometry, Activity Assay

    Bcl-2 downregulation inhibited the protective effect of miR-181a inhibitor on DDVP-induced HepaRG cell cytotoxic. Bcl-2 was knocked down by transfected with si-Bcl-2 to evaluate its function in the miR-181a protected DDVP-induced cell toxicity, including cell viability, apoptosis, ROS production. The cells were divided into following groups: control, DDVP group, miR-181a inhibitor + DDVP group, si-Bcl-2 + miR-181a inhibitor + DDVP group. A. The downregulation of Bcl-2 reversed the protective effect of miR-181a inhibitor on the HepaRG cell viability, when compared with non-transfection treatment group. B. miR-181a inhibitor could rescue the increased apoptosis portion caused by DDVP, however, when transfected with si-Bcl-2, these effects diminished, as can be seen from the increased level of apoptosis portion. C. When transfected with si-Bcl-2, theactivity of caspase-3 in HepaRG cell was significantly increased when compared with miR-181a inhibitor + DDVP group. D. The ROS production, valued as relative luciferase units, in HepaRG cells transfected with si-Bcl-2 was significantly increased, when compared with miR-181a inhibitor + DDVP group. E. The expression of caspase-3 and Bcl-2 in HepaRG cells with different treatments was detected by western blot analysis, respectively. F. The caspase-3 and Bcl-2 expression value was determined by relative optical density, respectively. * P
    Figure Legend Snippet: Bcl-2 downregulation inhibited the protective effect of miR-181a inhibitor on DDVP-induced HepaRG cell cytotoxic. Bcl-2 was knocked down by transfected with si-Bcl-2 to evaluate its function in the miR-181a protected DDVP-induced cell toxicity, including cell viability, apoptosis, ROS production. The cells were divided into following groups: control, DDVP group, miR-181a inhibitor + DDVP group, si-Bcl-2 + miR-181a inhibitor + DDVP group. A. The downregulation of Bcl-2 reversed the protective effect of miR-181a inhibitor on the HepaRG cell viability, when compared with non-transfection treatment group. B. miR-181a inhibitor could rescue the increased apoptosis portion caused by DDVP, however, when transfected with si-Bcl-2, these effects diminished, as can be seen from the increased level of apoptosis portion. C. When transfected with si-Bcl-2, theactivity of caspase-3 in HepaRG cell was significantly increased when compared with miR-181a inhibitor + DDVP group. D. The ROS production, valued as relative luciferase units, in HepaRG cells transfected with si-Bcl-2 was significantly increased, when compared with miR-181a inhibitor + DDVP group. E. The expression of caspase-3 and Bcl-2 in HepaRG cells with different treatments was detected by western blot analysis, respectively. F. The caspase-3 and Bcl-2 expression value was determined by relative optical density, respectively. * P

    Techniques Used: Transfection, Luciferase, Expressing, Western Blot

    12) Product Images from "Panobinostat, a histone deacetylase inhibitor, suppresses leptomeningeal seeding in a medulloblastoma animal model"

    Article Title: Panobinostat, a histone deacetylase inhibitor, suppresses leptomeningeal seeding in a medulloblastoma animal model

    Journal: Oncotarget

    doi: 10.18632/oncotarget.18132

    Effect of panobinostat on histone acetylation, apoptosis, cell cycle, IDs and differentiation-related signal pathway in medulloblastoma cells Immunoblotting of whole cell lysates prepared from MB cells treated with panobinostat. The representative western blot result shows panobinostat clearly regulated acetyl-Histone H3 (Ac-H3), cleaved caspase-3, CCND1, IDs, synaptophysin and NeuroD1.
    Figure Legend Snippet: Effect of panobinostat on histone acetylation, apoptosis, cell cycle, IDs and differentiation-related signal pathway in medulloblastoma cells Immunoblotting of whole cell lysates prepared from MB cells treated with panobinostat. The representative western blot result shows panobinostat clearly regulated acetyl-Histone H3 (Ac-H3), cleaved caspase-3, CCND1, IDs, synaptophysin and NeuroD1.

    Techniques Used: Western Blot

    Therapeutic effect of panobinostat in a UW426-effLuc medulloblastoma leptomeningeal seeding model UW426-effLuc mice were treated 3 days later with panobinostat (10 mg/kg once daily for 2 weeks). (A and B) Serial bioluminescence image (BLI) of representative mice in each group. Quantification of BLI results shows that panobinostat reduced intracranial tumor burden and inhibited spinal cord seeding. (C) Representative longitudinal sections of whole craniospinal neuraxis of the mice with UW426-effLuc. Immunofluorescence with acetyl-H3 (green), Ki-67 (red), cleaved caspase-3 (green), ID3 (green) and synaptophysin (red). Representative images reveal increased Ac-H3, cleaved caspase-3 and synaptophysin and decreased Ki-67 and ID3 in (D) cerebellar mass and (E) leptomeningeal disseminated tumor cell layers. Scale bars, 100 μm. Cells were counterstained with 4′,6′-diamidino-2-phenylindole (blue). (F) A plot of overall survival is estimated by the Kaplan-Meier method. Panobinostat treatment significantly enhances the survival of mice bearing UW426-effLuc. *p
    Figure Legend Snippet: Therapeutic effect of panobinostat in a UW426-effLuc medulloblastoma leptomeningeal seeding model UW426-effLuc mice were treated 3 days later with panobinostat (10 mg/kg once daily for 2 weeks). (A and B) Serial bioluminescence image (BLI) of representative mice in each group. Quantification of BLI results shows that panobinostat reduced intracranial tumor burden and inhibited spinal cord seeding. (C) Representative longitudinal sections of whole craniospinal neuraxis of the mice with UW426-effLuc. Immunofluorescence with acetyl-H3 (green), Ki-67 (red), cleaved caspase-3 (green), ID3 (green) and synaptophysin (red). Representative images reveal increased Ac-H3, cleaved caspase-3 and synaptophysin and decreased Ki-67 and ID3 in (D) cerebellar mass and (E) leptomeningeal disseminated tumor cell layers. Scale bars, 100 μm. Cells were counterstained with 4′,6′-diamidino-2-phenylindole (blue). (F) A plot of overall survival is estimated by the Kaplan-Meier method. Panobinostat treatment significantly enhances the survival of mice bearing UW426-effLuc. *p

    Techniques Used: Mouse Assay, Immunofluorescence

    13) Product Images from "Branched chain amino acids attenuate major pathologies in mouse models of retinal degeneration and glaucoma"

    Article Title: Branched chain amino acids attenuate major pathologies in mouse models of retinal degeneration and glaucoma

    Journal: Heliyon

    doi: 10.1016/j.heliyon.2018.e00544

    Suppression of ER stress by BCAAs leads to suppression of cleaved caspase-3 in mouse models. (A) Western blot analysis of 19-month-old rd12 mice treated with BCAAs, or water as a control. Extracts from dissected neural retinas and the combination of retinal pigment epithelium (RPE), choroid, and sclera (RPE/choroid) were analyzed with an anti-CHOP or cleaved caspase-3 antibody. Complete scans of western blots are shown in Fig. S4E. (B) Vertical retinal sections of 21-day-old rd10 mice stained with or without an anti-CHOP antibody (red). Abbreviations: RNFL, retinal nerve fiber layer; GCL, Ganglion cell layer; IPL, Inner plexiform layer; INL, Inner nuclear layer; OPL, Outer plexiform layer; ONL, Outer nuclear layer; IS, inner segment of the photoreceptor cell; OS, outer segment of the photoreceptor cell; and RPE, Retinal pigment epithelium. (C) Vertical retinal sections of 18-month-old GLAST (+/−) mice stained with or without an anti-CHOP antibody. Note that more cells remained in the GCL of BCAA-treated mouse than in that of control mouse. Note also that more cells were strongly stained by the CHOP antibody (arrowheads) in control mouse than in BCAA-treated mouse. Scale bars: 20 μm in B and C.
    Figure Legend Snippet: Suppression of ER stress by BCAAs leads to suppression of cleaved caspase-3 in mouse models. (A) Western blot analysis of 19-month-old rd12 mice treated with BCAAs, or water as a control. Extracts from dissected neural retinas and the combination of retinal pigment epithelium (RPE), choroid, and sclera (RPE/choroid) were analyzed with an anti-CHOP or cleaved caspase-3 antibody. Complete scans of western blots are shown in Fig. S4E. (B) Vertical retinal sections of 21-day-old rd10 mice stained with or without an anti-CHOP antibody (red). Abbreviations: RNFL, retinal nerve fiber layer; GCL, Ganglion cell layer; IPL, Inner plexiform layer; INL, Inner nuclear layer; OPL, Outer plexiform layer; ONL, Outer nuclear layer; IS, inner segment of the photoreceptor cell; OS, outer segment of the photoreceptor cell; and RPE, Retinal pigment epithelium. (C) Vertical retinal sections of 18-month-old GLAST (+/−) mice stained with or without an anti-CHOP antibody. Note that more cells remained in the GCL of BCAA-treated mouse than in that of control mouse. Note also that more cells were strongly stained by the CHOP antibody (arrowheads) in control mouse than in BCAA-treated mouse. Scale bars: 20 μm in B and C.

    Techniques Used: Western Blot, Mouse Assay, Staining

    14) Product Images from "Intranasal epidermal growth factor treatment rescues neonatal brain injury"

    Article Title: Intranasal epidermal growth factor treatment rescues neonatal brain injury

    Journal: Nature

    doi: 10.1038/nature12880

    Enhanced EGFR expression in oligodendrocyte lineage cells prevents oligodendrocyte death and promotes proliferation of OPCs in white matter a–d, Representative 40x confocal images of Rep + PI + cells from Nx and Hyp WM at P11 in Rep and Rep-hEGFR mice. e, At P11 and P18, Hyp resulted in a significant increase in the number of OL cells undergoing apoptosis (Rep + casp3 + ). Enhanced EGFR expression prevented this increase at all time points, except P60 where no difference was evident. Comparison of the Hyp Rep with the Hyp Rep-hEGFR groups demonstrates that hEGFR in OL lineage cells is protective against apoptosis induced by Hyp (n=4 mice per group and per age; One-way ANOVA, Bonferroni post hoc test for individual comparisons). f, PI was injected intraperitoneally (IP) 1-hour prior to sacrifice. A significant increase in the number of Rep + PI + OL cells indicated membrane disruption contributing to cell death (n=3 mice per group; One-way ANOVA, Bonferroni post hoc test for individual comparisons). g–j, Representative 40x confocal images of Rep + NG2 + OPCs from Nx and Hyp WM at P18 in the Rep and Rep-hEGFR mice. k , At P11 and P18, Rep-hEGFR Nx mice had more NG2 + expressing OPCs compared to the Rep Nx group. Hyp resulted in a significant increase in the number of Rep + NG2 + OPCs in both Rep and Rep-hEGFR groups, however, overexpression of hEGFR did not have an additive effect (n=4 mice per group and per age; One-way ANOVA, Bonferroni post hoc test for individual comparisons). l, At P11 and P18, the Rep-hEGFR group had more Rep + Ki67 + cells, however this did not reach significance (P > 0.05). Hyp resulted in enhanced OL-lineage proliferation at P11 and P18, but hEGFR overexpression did not have a significantly additive effect, when compared to the Rep Hyp group. k,l, n=4 mice per group and per age; One-way ANOVA, Bonferroni post hoc test for individual comparisons. m, More OPCs were in a proliferative state in Rep-hEGFR Nx mice compared to Rep Nx. Hyp enhanced OPC proliferation, and overexpression of hEGFR resulted in a significantly additive increase compared to the Rep Hyp group (n=3 mice per group; One-way ANOVA, Bonferroni post hoc test for individual comparisons). All histograms are presented as means ± s.e.m. Scale bars, 50μm (a–d, g–j) . ^P=0.05; *P
    Figure Legend Snippet: Enhanced EGFR expression in oligodendrocyte lineage cells prevents oligodendrocyte death and promotes proliferation of OPCs in white matter a–d, Representative 40x confocal images of Rep + PI + cells from Nx and Hyp WM at P11 in Rep and Rep-hEGFR mice. e, At P11 and P18, Hyp resulted in a significant increase in the number of OL cells undergoing apoptosis (Rep + casp3 + ). Enhanced EGFR expression prevented this increase at all time points, except P60 where no difference was evident. Comparison of the Hyp Rep with the Hyp Rep-hEGFR groups demonstrates that hEGFR in OL lineage cells is protective against apoptosis induced by Hyp (n=4 mice per group and per age; One-way ANOVA, Bonferroni post hoc test for individual comparisons). f, PI was injected intraperitoneally (IP) 1-hour prior to sacrifice. A significant increase in the number of Rep + PI + OL cells indicated membrane disruption contributing to cell death (n=3 mice per group; One-way ANOVA, Bonferroni post hoc test for individual comparisons). g–j, Representative 40x confocal images of Rep + NG2 + OPCs from Nx and Hyp WM at P18 in the Rep and Rep-hEGFR mice. k , At P11 and P18, Rep-hEGFR Nx mice had more NG2 + expressing OPCs compared to the Rep Nx group. Hyp resulted in a significant increase in the number of Rep + NG2 + OPCs in both Rep and Rep-hEGFR groups, however, overexpression of hEGFR did not have an additive effect (n=4 mice per group and per age; One-way ANOVA, Bonferroni post hoc test for individual comparisons). l, At P11 and P18, the Rep-hEGFR group had more Rep + Ki67 + cells, however this did not reach significance (P > 0.05). Hyp resulted in enhanced OL-lineage proliferation at P11 and P18, but hEGFR overexpression did not have a significantly additive effect, when compared to the Rep Hyp group. k,l, n=4 mice per group and per age; One-way ANOVA, Bonferroni post hoc test for individual comparisons. m, More OPCs were in a proliferative state in Rep-hEGFR Nx mice compared to Rep Nx. Hyp enhanced OPC proliferation, and overexpression of hEGFR resulted in a significantly additive increase compared to the Rep Hyp group (n=3 mice per group; One-way ANOVA, Bonferroni post hoc test for individual comparisons). All histograms are presented as means ± s.e.m. Scale bars, 50μm (a–d, g–j) . ^P=0.05; *P

    Techniques Used: Expressing, Mouse Assay, Injection, Over Expression

    15) Product Images from "Opposing Effects of Pigment Epithelium-Derived Factor on Breast Cancer Cell versus Neuronal Survival: Implication for Brain Metastasis and Metastasis-Induced Brain Damage"

    Article Title: Opposing Effects of Pigment Epithelium-Derived Factor on Breast Cancer Cell versus Neuronal Survival: Implication for Brain Metastasis and Metastasis-Induced Brain Damage

    Journal: Cancer Research

    doi: 10.1158/0008-5472.CAN-11-1904

    PEDF rapidly impacted the proliferation and viability of breast cancer cells implanted in the mouse brain A, Immunofluorescence for PEDF-FLAG protein (anti-FLAG, red) in PEDF-231-BR ins tumors 5 hrs (left), 24 hrs (middle) and 72 hrs post-implantation (right). Nuclei are counterstained with DAPI (blue). B, H E stained sections of mouse brains with control 231-BR ins tumor cells (left), PEDF-231-BR ins tumor cells (middle), and a saline control injection (right) 24 hrs post-implantation. C, Immunofluorescence for a proliferation marker (anti-Ki67, green) in control lesions (left) and in PEDF lesions (right) 24 hrs post-implantation. Xenograft breast cancer cells were co-labeled for human-specific-mitochondria (red) and nuclei counterstained with DAPI (blue). D, Percentage of Ki67-positive cells in control and PEDF lesions after 24 hrs. E, Apoptotic cells expressing Cleaved-Caspase3 (green) in control (left) and in PEDF-231-BR ins lesions (right) 24 hrs post-implantation. F, Percentage of Cleaved-Caspase-3-positive cells in control and PEDF lesions after 24 hrs. Five mice injected with control cells and five mice injected with PEDF-231-BR ins cells were averaged from two experiments for these analyses.
    Figure Legend Snippet: PEDF rapidly impacted the proliferation and viability of breast cancer cells implanted in the mouse brain A, Immunofluorescence for PEDF-FLAG protein (anti-FLAG, red) in PEDF-231-BR ins tumors 5 hrs (left), 24 hrs (middle) and 72 hrs post-implantation (right). Nuclei are counterstained with DAPI (blue). B, H E stained sections of mouse brains with control 231-BR ins tumor cells (left), PEDF-231-BR ins tumor cells (middle), and a saline control injection (right) 24 hrs post-implantation. C, Immunofluorescence for a proliferation marker (anti-Ki67, green) in control lesions (left) and in PEDF lesions (right) 24 hrs post-implantation. Xenograft breast cancer cells were co-labeled for human-specific-mitochondria (red) and nuclei counterstained with DAPI (blue). D, Percentage of Ki67-positive cells in control and PEDF lesions after 24 hrs. E, Apoptotic cells expressing Cleaved-Caspase3 (green) in control (left) and in PEDF-231-BR ins lesions (right) 24 hrs post-implantation. F, Percentage of Cleaved-Caspase-3-positive cells in control and PEDF lesions after 24 hrs. Five mice injected with control cells and five mice injected with PEDF-231-BR ins cells were averaged from two experiments for these analyses.

    Techniques Used: Immunofluorescence, Staining, Injection, Marker, Labeling, Expressing, Mouse Assay

    16) Product Images from "Bcl2L12-mediated inhibition of effector caspase-3 and caspase-7 via distinct mechanisms in glioblastoma"

    Article Title: Bcl2L12-mediated inhibition of effector caspase-3 and caspase-7 via distinct mechanisms in glioblastoma

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.0712034105

    αB-crystallin cocompartmentalizes with and selectively binds to the caspase-3 zymogen and its cleavage intermediates. ( A ) Bcl2L12 V5 -expressing Ink4a / Arf -deficient astrocytes were treated with STS (1 μM) for the indicated periods of time,
    Figure Legend Snippet: αB-crystallin cocompartmentalizes with and selectively binds to the caspase-3 zymogen and its cleavage intermediates. ( A ) Bcl2L12 V5 -expressing Ink4a / Arf -deficient astrocytes were treated with STS (1 μM) for the indicated periods of time,

    Techniques Used: Expressing

    17) Product Images from "Branched chain amino acids attenuate major pathologies in mouse models of retinal degeneration and glaucoma"

    Article Title: Branched chain amino acids attenuate major pathologies in mouse models of retinal degeneration and glaucoma

    Journal: Heliyon

    doi: 10.1016/j.heliyon.2018.e00544

    Suppression of ER stress by BCAAs leads to suppression of cleaved caspase-3 in mouse models. (A) Western blot analysis of 19-month-old rd12 mice treated with BCAAs, or water as a control. Extracts from dissected neural retinas and the combination of retinal pigment epithelium (RPE), choroid, and sclera (RPE/choroid) were analyzed with an anti-CHOP or cleaved caspase-3 antibody. Complete scans of western blots are shown in Fig. S4E. (B) Vertical retinal sections of 21-day-old rd10 mice stained with or without an anti-CHOP antibody (red). Abbreviations: RNFL, retinal nerve fiber layer; GCL, Ganglion cell layer; IPL, Inner plexiform layer; INL, Inner nuclear layer; OPL, Outer plexiform layer; ONL, Outer nuclear layer; IS, inner segment of the photoreceptor cell; OS, outer segment of the photoreceptor cell; and RPE, Retinal pigment epithelium. (C) Vertical retinal sections of 18-month-old GLAST (+/−) mice stained with or without an anti-CHOP antibody. Note that more cells remained in the GCL of BCAA-treated mouse than in that of control mouse. Note also that more cells were strongly stained by the CHOP antibody (arrowheads) in control mouse than in BCAA-treated mouse. Scale bars: 20 μm in B and C.
    Figure Legend Snippet: Suppression of ER stress by BCAAs leads to suppression of cleaved caspase-3 in mouse models. (A) Western blot analysis of 19-month-old rd12 mice treated with BCAAs, or water as a control. Extracts from dissected neural retinas and the combination of retinal pigment epithelium (RPE), choroid, and sclera (RPE/choroid) were analyzed with an anti-CHOP or cleaved caspase-3 antibody. Complete scans of western blots are shown in Fig. S4E. (B) Vertical retinal sections of 21-day-old rd10 mice stained with or without an anti-CHOP antibody (red). Abbreviations: RNFL, retinal nerve fiber layer; GCL, Ganglion cell layer; IPL, Inner plexiform layer; INL, Inner nuclear layer; OPL, Outer plexiform layer; ONL, Outer nuclear layer; IS, inner segment of the photoreceptor cell; OS, outer segment of the photoreceptor cell; and RPE, Retinal pigment epithelium. (C) Vertical retinal sections of 18-month-old GLAST (+/−) mice stained with or without an anti-CHOP antibody. Note that more cells remained in the GCL of BCAA-treated mouse than in that of control mouse. Note also that more cells were strongly stained by the CHOP antibody (arrowheads) in control mouse than in BCAA-treated mouse. Scale bars: 20 μm in B and C.

    Techniques Used: Western Blot, Mouse Assay, Staining

    18) Product Images from "Osteopontin regulates proliferation, apoptosis, and migration of murine claudin-low mammary tumor cells"

    Article Title: Osteopontin regulates proliferation, apoptosis, and migration of murine claudin-low mammary tumor cells

    Journal: BMC Cancer

    doi: 10.1186/s12885-016-2396-9

    Quantification of ( a , b ) Ki67 immunofluorescence or ( d , e ) cleaved caspase 3 immunofluorescence in ( a , d ) RJ348 cells or (B,E) RM11A cells after treatment with a GC control siRNA or OPN-siRNA 2 . The percentage of Ki67 positive or cleaved caspase 3 positive cells following OPN-siRNA 2 treatment are presented relative to cells treated with the GC control siRNA. c phospho-histone H3 immunofluorescence in RJ348 cells following administration of 5 μg of an OPN neutralizing antibody or 5 μg of a control antibody. The percentage of phospho-histone H3 positive cells following OPN neutralizing antibody treatment is presented relative to the control antibody. A paired t-test was used to determine statistical significance, * p ˂0.05, n ≥ 3
    Figure Legend Snippet: Quantification of ( a , b ) Ki67 immunofluorescence or ( d , e ) cleaved caspase 3 immunofluorescence in ( a , d ) RJ348 cells or (B,E) RM11A cells after treatment with a GC control siRNA or OPN-siRNA 2 . The percentage of Ki67 positive or cleaved caspase 3 positive cells following OPN-siRNA 2 treatment are presented relative to cells treated with the GC control siRNA. c phospho-histone H3 immunofluorescence in RJ348 cells following administration of 5 μg of an OPN neutralizing antibody or 5 μg of a control antibody. The percentage of phospho-histone H3 positive cells following OPN neutralizing antibody treatment is presented relative to the control antibody. A paired t-test was used to determine statistical significance, * p ˂0.05, n ≥ 3

    Techniques Used: Immunofluorescence

    19) Product Images from "Electrophysiological Correlates of Blast-Wave Induced Cerebellar Injury"

    Article Title: Electrophysiological Correlates of Blast-Wave Induced Cerebellar Injury

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-31728-4

    Immunofluorescence images of calbindin-D28K ( A , B ) and cleaved caspase-3 ( C , D ) in control, 24 hours and 7 days after blast injury. Sagittal sections with enlarged fragments from the paramedian lobules (insets) captured at 40x magnification and quantification results are presented. Paramedial lobules double stained for calbindin-D28K (red) and caspase-3 (green) showing no colocalization of caspase-3 in Purkinje cells ( E , F ). Bar plots present quantification of: 1) a cell count for: calbindin-28k ( A ), and capsase-3 ( C ) positive cells, and 2) calbindin-28k fluorescence signal ( B ). No appreciable changes in the levels of calbindin-D28K or cleaved caspase-3 were observed between control and the injured cerebella (p > 0.05).
    Figure Legend Snippet: Immunofluorescence images of calbindin-D28K ( A , B ) and cleaved caspase-3 ( C , D ) in control, 24 hours and 7 days after blast injury. Sagittal sections with enlarged fragments from the paramedian lobules (insets) captured at 40x magnification and quantification results are presented. Paramedial lobules double stained for calbindin-D28K (red) and caspase-3 (green) showing no colocalization of caspase-3 in Purkinje cells ( E , F ). Bar plots present quantification of: 1) a cell count for: calbindin-28k ( A ), and capsase-3 ( C ) positive cells, and 2) calbindin-28k fluorescence signal ( B ). No appreciable changes in the levels of calbindin-D28K or cleaved caspase-3 were observed between control and the injured cerebella (p > 0.05).

    Techniques Used: Immunofluorescence, Staining, Cell Counting, Fluorescence

    20) Product Images from "Astragalus Polysaccharide Promotes Adriamycin-Induced Apoptosis in Gastric Cancer Cells"

    Article Title: Astragalus Polysaccharide Promotes Adriamycin-Induced Apoptosis in Gastric Cancer Cells

    Journal: Cancer Management and Research

    doi: 10.2147/CMAR.S237146

    APS enhances adriamycin-mediated increases in both the expression and activity of caspase-3 cleavage as well as in DNA fragmentation. Notes: Human gastric cancer SGC-7901 cells were incubated with APS (100 µg/mL) and/or adriamycin (0.1 µg/mL) for 24 h. ( A ) and ( B ) The level of cleaved caspase-3 was examined by Western blotting, and β-actin was used as a loading control. The relative protein level of cleaved caspase-3 was normalized to that of β-actin. ( C ) Caspase-3 activity was detected by a fluorometric plate reader. ( D and E ) Cellular DNA fragmentation was examined by an ELISA kit. Data are expressed as mean ± SD. N = 3–5. * p
    Figure Legend Snippet: APS enhances adriamycin-mediated increases in both the expression and activity of caspase-3 cleavage as well as in DNA fragmentation. Notes: Human gastric cancer SGC-7901 cells were incubated with APS (100 µg/mL) and/or adriamycin (0.1 µg/mL) for 24 h. ( A ) and ( B ) The level of cleaved caspase-3 was examined by Western blotting, and β-actin was used as a loading control. The relative protein level of cleaved caspase-3 was normalized to that of β-actin. ( C ) Caspase-3 activity was detected by a fluorometric plate reader. ( D and E ) Cellular DNA fragmentation was examined by an ELISA kit. Data are expressed as mean ± SD. N = 3–5. * p

    Techniques Used: Expressing, Activity Assay, Incubation, Western Blot, Enzyme-linked Immunosorbent Assay

    21) Product Images from "A neuroprotective agent that inactivates prodegenerative TrkA and preserves mitochondria"

    Article Title: A neuroprotective agent that inactivates prodegenerative TrkA and preserves mitochondria

    Journal: The Journal of Cell Biology

    doi: 10.1083/jcb.201705085

    Foretinib suppresses the expression or activity of genes and proteins associated with sympathetic neuron death and degeneration and protects mitochondria. (A and B) Changes in gene expression in mouse sympathetic neurons withdrawn from NGF for 9 h ( bimEL , puma/bbc3 , trib3 , ddit3 , and hrk mRNAs) or 12 h ( pmaip1/noxa , gadd45γ , tap63 mRNAs) with or without foretinib (Foret) by quantitative RT-PCR; n ≥ 3 independent experiments. (C–G). WB analysis of mouse sympathetic neurons withdrawn from NGF with or without 500 nM foretinib for 10–12 (C and F), 18 (D and E), or 24 (G) h. Blots were probed with antibodies to the indicated proteins, including phosphorylated (p) JNK, activated (a) Bax, cleaved caspase-3 (cc3), or αII-spectrin (cleaved [cl] and full-length [f.l.]), and reprobed for βIII-tubulin (tuj1), ERK1/2, or GAPDH to control for loading. (H and I) Mouse sympathetic neurons withdrawn from NGF in the presence or absence of foretinib for 12 h, immunostained for cytochrome c (red, cyt-c) or βIII-tubulin (green), and quantified for neurons with diffuse cytochrome c (I), as indicated by arrows in H. (I) ***, P
    Figure Legend Snippet: Foretinib suppresses the expression or activity of genes and proteins associated with sympathetic neuron death and degeneration and protects mitochondria. (A and B) Changes in gene expression in mouse sympathetic neurons withdrawn from NGF for 9 h ( bimEL , puma/bbc3 , trib3 , ddit3 , and hrk mRNAs) or 12 h ( pmaip1/noxa , gadd45γ , tap63 mRNAs) with or without foretinib (Foret) by quantitative RT-PCR; n ≥ 3 independent experiments. (C–G). WB analysis of mouse sympathetic neurons withdrawn from NGF with or without 500 nM foretinib for 10–12 (C and F), 18 (D and E), or 24 (G) h. Blots were probed with antibodies to the indicated proteins, including phosphorylated (p) JNK, activated (a) Bax, cleaved caspase-3 (cc3), or αII-spectrin (cleaved [cl] and full-length [f.l.]), and reprobed for βIII-tubulin (tuj1), ERK1/2, or GAPDH to control for loading. (H and I) Mouse sympathetic neurons withdrawn from NGF in the presence or absence of foretinib for 12 h, immunostained for cytochrome c (red, cyt-c) or βIII-tubulin (green), and quantified for neurons with diffuse cytochrome c (I), as indicated by arrows in H. (I) ***, P

    Techniques Used: Expressing, Activity Assay, Quantitative RT-PCR, Western Blot

    22) Product Images from "Protective Role of Taurine against Arsenic-Induced Mitochondria-Dependent Hepatic Apoptosis via the Inhibition of PKC?-JNK Pathway"

    Article Title: Protective Role of Taurine against Arsenic-Induced Mitochondria-Dependent Hepatic Apoptosis via the Inhibition of PKC?-JNK Pathway

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0012602

    Immunoblot analysis on Mitochondrion-dependent pathway in absence (As) and presence of taurine (TAU+As). Panel A: Mitochondrial cytochrome c, complex IV subunit was used as loading control. Panel B: Cytosolic cytochrome c, Panel C: Caspase 9, Panel D: Apaf 1, Panel E: Caspase 3, Panel F: PARP. β actin was used as an internal control. Data represent the average ± SD of 6 separate experiments in each group. “a” indicates the significant difference between the normal control and As treated groups, “b” indicates the significant difference between the As treated and taurine treated groups (TAU+As). (P a
    Figure Legend Snippet: Immunoblot analysis on Mitochondrion-dependent pathway in absence (As) and presence of taurine (TAU+As). Panel A: Mitochondrial cytochrome c, complex IV subunit was used as loading control. Panel B: Cytosolic cytochrome c, Panel C: Caspase 9, Panel D: Apaf 1, Panel E: Caspase 3, Panel F: PARP. β actin was used as an internal control. Data represent the average ± SD of 6 separate experiments in each group. “a” indicates the significant difference between the normal control and As treated groups, “b” indicates the significant difference between the As treated and taurine treated groups (TAU+As). (P a

    Techniques Used:

    Immunoblot analysis of caspase 3 and hepatocytes viability in response to SB203580 and SP600125. Hepatyocytes were pre-treated with 10 µM SB203580 and SP600125 for 15 min, then treated with As (10 µM), taurine (25 mM, added 1 h prior to As treatment) for 8 h. Panel A: effects of SP600125 on Caspase 3, Panel B: effects of SB203580 on Caspase 3, β actin was used as an internal control. Panel C: effects of SP600125 on cell viability, Panel D: effects of SB203580 on cell viability. Data represent the average ± SD of 6 separate experiments in each group. “a” indicates the significant difference between the normal control and As treated groups, “b” indicates the significant difference between the As treated and taurine treated groups. (P a
    Figure Legend Snippet: Immunoblot analysis of caspase 3 and hepatocytes viability in response to SB203580 and SP600125. Hepatyocytes were pre-treated with 10 µM SB203580 and SP600125 for 15 min, then treated with As (10 µM), taurine (25 mM, added 1 h prior to As treatment) for 8 h. Panel A: effects of SP600125 on Caspase 3, Panel B: effects of SB203580 on Caspase 3, β actin was used as an internal control. Panel C: effects of SP600125 on cell viability, Panel D: effects of SB203580 on cell viability. Data represent the average ± SD of 6 separate experiments in each group. “a” indicates the significant difference between the normal control and As treated groups, “b” indicates the significant difference between the As treated and taurine treated groups. (P a

    Techniques Used:

    23) Product Images from "Electrophysiological Correlates of Blast-Wave Induced Cerebellar Injury"

    Article Title: Electrophysiological Correlates of Blast-Wave Induced Cerebellar Injury

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-31728-4

    Immunofluorescence images of calbindin-D28K ( A , B ) and cleaved caspase-3 ( C , D ) in control, 24 hours and 7 days after blast injury. Sagittal sections with enlarged fragments from the paramedian lobules (insets) captured at 40x magnification and quantification results are presented. Paramedial lobules double stained for calbindin-D28K (red) and caspase-3 (green) showing no colocalization of caspase-3 in Purkinje cells ( E , F ). Bar plots present quantification of: 1) a cell count for: calbindin-28k ( A ), and capsase-3 ( C ) positive cells, and 2) calbindin-28k fluorescence signal ( B ). No appreciable changes in the levels of calbindin-D28K or cleaved caspase-3 were observed between control and the injured cerebella (p > 0.05).
    Figure Legend Snippet: Immunofluorescence images of calbindin-D28K ( A , B ) and cleaved caspase-3 ( C , D ) in control, 24 hours and 7 days after blast injury. Sagittal sections with enlarged fragments from the paramedian lobules (insets) captured at 40x magnification and quantification results are presented. Paramedial lobules double stained for calbindin-D28K (red) and caspase-3 (green) showing no colocalization of caspase-3 in Purkinje cells ( E , F ). Bar plots present quantification of: 1) a cell count for: calbindin-28k ( A ), and capsase-3 ( C ) positive cells, and 2) calbindin-28k fluorescence signal ( B ). No appreciable changes in the levels of calbindin-D28K or cleaved caspase-3 were observed between control and the injured cerebella (p > 0.05).

    Techniques Used: Immunofluorescence, Staining, Cell Counting, Fluorescence

    24) Product Images from "Inhibition of prolyl hydroxylases by dimethyloxaloylglycine after stroke reduces ischemic brain injury and requires hypoxia inducible factor-1?"

    Article Title: Inhibition of prolyl hydroxylases by dimethyloxaloylglycine after stroke reduces ischemic brain injury and requires hypoxia inducible factor-1?

    Journal: Neurobiology of Disease

    doi: 10.1016/j.nbd.2011.10.020

    PHD inhibitor treatment reduced activation of caspase-3 in the ischemic cortex
    Figure Legend Snippet: PHD inhibitor treatment reduced activation of caspase-3 in the ischemic cortex

    Techniques Used: Activation Assay

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  • 94
    Millipore anti caspase3 antibody
    The biological action of EA microprobe: ( a ). Experimental setup for in vitro cell viability (figure is not to scale), ( b ). Cell viability assay: The microprobe is effective as a DC power source (positive control) compared to negative controls (ultrasound only and no action). ( c ) Ex vivo experiment using mouse liver. ( d ) The expression of <t>caspase3</t> was detected by immunofluorescence and immunohistochemistry. Positive caspase3 is counterstained with DAP in immunofluorescence and hematoxylin in immunohistochemistry. The control group (electrode insertion only) was compared with the experimental group. ( e ) Analysis of immunofluorescence: integrated density and corrected cell fluorescence were measured. Error bars represent SD; n ≥ 4; p-value was determined using a two-tailed t-test. *p
    Anti Caspase3 Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore rabbit anti mouse active cleaved caspase 3 antibodies
    Anti-β3 antibody decreased AKT phosphorylation and increased apoptosis in HUVECs. ( A ) Human anti–HPA-1a IgG and murine anti-β3 sera significantly reduced AKT phosphorylation in HUVECs. ( B ) Human anti–HPA-1a IgG significantly increased <t>caspase-3</t> activation. Results are pooled from 4 independent experiments. Statistical analysis was performed using an unpaired, 2-tailed Student’s t test. Mean ± SEM. n = 3 wells per group. *** P
    Rabbit Anti Mouse Active Cleaved Caspase 3 Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore anti caspase 3
    Expression patterns of cell-death-related proteins in the bvFTD iPSC-derived neurons in response to staurosporine (STS) treatment. ( A ) Immunoblot assay showing the expression of cell-death-related markers, including cleaved <t>caspase-3</t> (17 kDa), Bax (21 kDa), Bcl-2 (26 kDa), and cytochrome C (14 kDa). Note that samples were obtained from two different culture conditions in the presence or absence of STS treatment (100 nM). ( B ) Quantification of immunoblot assay showing that cleaved caspase-3 expression was significantly increased in the two bvFTD-iPSNs compared with the normal control. ( C ) Quantification of immunoblot assay by obtaining the ratio of Bax and Bcl-2 expression showing that significantly-increased patterns were observed in the two bvFTD-iPSNs compared with the normal control. ( D ) Quantification of immunoblot assay showing that cytochrome C expression was significantly increased in the two bvFTD-iPSNs compared with the normal control. Note that blot images indicated by dividing lines were chosen from different immunoblots due to the large size of samples. Whole blot images are provided in Supplementary Figure S3A–D . Protein quantifications were conducted under the same exposure time ( n = 3) (*: vs. normal control) * p
    Anti Caspase 3, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    The biological action of EA microprobe: ( a ). Experimental setup for in vitro cell viability (figure is not to scale), ( b ). Cell viability assay: The microprobe is effective as a DC power source (positive control) compared to negative controls (ultrasound only and no action). ( c ) Ex vivo experiment using mouse liver. ( d ) The expression of caspase3 was detected by immunofluorescence and immunohistochemistry. Positive caspase3 is counterstained with DAP in immunofluorescence and hematoxylin in immunohistochemistry. The control group (electrode insertion only) was compared with the experimental group. ( e ) Analysis of immunofluorescence: integrated density and corrected cell fluorescence were measured. Error bars represent SD; n ≥ 4; p-value was determined using a two-tailed t-test. *p

    Journal: Scientific Reports

    Article Title: An Ultrasonically Powered Implantable Microprobe for Electrolytic Ablation

    doi: 10.1038/s41598-020-58090-8

    Figure Lengend Snippet: The biological action of EA microprobe: ( a ). Experimental setup for in vitro cell viability (figure is not to scale), ( b ). Cell viability assay: The microprobe is effective as a DC power source (positive control) compared to negative controls (ultrasound only and no action). ( c ) Ex vivo experiment using mouse liver. ( d ) The expression of caspase3 was detected by immunofluorescence and immunohistochemistry. Positive caspase3 is counterstained with DAP in immunofluorescence and hematoxylin in immunohistochemistry. The control group (electrode insertion only) was compared with the experimental group. ( e ) Analysis of immunofluorescence: integrated density and corrected cell fluorescence were measured. Error bars represent SD; n ≥ 4; p-value was determined using a two-tailed t-test. *p

    Article Snippet: The anti-caspase3 antibody was incubated overnight at 4 °C (AB3623, Millipore, USA).

    Techniques: In Vitro, Viability Assay, Positive Control, Ex Vivo, Expressing, Immunofluorescence, Immunohistochemistry, Fluorescence, Two Tailed Test

    Anti-β3 antibody decreased AKT phosphorylation and increased apoptosis in HUVECs. ( A ) Human anti–HPA-1a IgG and murine anti-β3 sera significantly reduced AKT phosphorylation in HUVECs. ( B ) Human anti–HPA-1a IgG significantly increased caspase-3 activation. Results are pooled from 4 independent experiments. Statistical analysis was performed using an unpaired, 2-tailed Student’s t test. Mean ± SEM. n = 3 wells per group. *** P

    Journal: The Journal of Clinical Investigation

    Article Title: Maternal anti-platelet β3 integrins impair angiogenesis and cause intracranial hemorrhage

    doi: 10.1172/JCI77820

    Figure Lengend Snippet: Anti-β3 antibody decreased AKT phosphorylation and increased apoptosis in HUVECs. ( A ) Human anti–HPA-1a IgG and murine anti-β3 sera significantly reduced AKT phosphorylation in HUVECs. ( B ) Human anti–HPA-1a IgG significantly increased caspase-3 activation. Results are pooled from 4 independent experiments. Statistical analysis was performed using an unpaired, 2-tailed Student’s t test. Mean ± SEM. n = 3 wells per group. *** P

    Article Snippet: Rabbit anti-human (crossreacts with mouse) vWF (catalog AB7356), rabbit anti-mouse collagen IV (catalog AB2031), and rabbit anti-mouse active (cleaved) caspase-3 antibodies (catalog PC679) were purchased from Millipore.

    Techniques: Activation Assay

    Expression patterns of cell-death-related proteins in the bvFTD iPSC-derived neurons in response to staurosporine (STS) treatment. ( A ) Immunoblot assay showing the expression of cell-death-related markers, including cleaved caspase-3 (17 kDa), Bax (21 kDa), Bcl-2 (26 kDa), and cytochrome C (14 kDa). Note that samples were obtained from two different culture conditions in the presence or absence of STS treatment (100 nM). ( B ) Quantification of immunoblot assay showing that cleaved caspase-3 expression was significantly increased in the two bvFTD-iPSNs compared with the normal control. ( C ) Quantification of immunoblot assay by obtaining the ratio of Bax and Bcl-2 expression showing that significantly-increased patterns were observed in the two bvFTD-iPSNs compared with the normal control. ( D ) Quantification of immunoblot assay showing that cytochrome C expression was significantly increased in the two bvFTD-iPSNs compared with the normal control. Note that blot images indicated by dividing lines were chosen from different immunoblots due to the large size of samples. Whole blot images are provided in Supplementary Figure S3A–D . Protein quantifications were conducted under the same exposure time ( n = 3) (*: vs. normal control) * p

    Journal: International Journal of Molecular Sciences

    Article Title: Modeling of Frontotemporal Dementia Using iPSC Technology

    doi: 10.3390/ijms21155319

    Figure Lengend Snippet: Expression patterns of cell-death-related proteins in the bvFTD iPSC-derived neurons in response to staurosporine (STS) treatment. ( A ) Immunoblot assay showing the expression of cell-death-related markers, including cleaved caspase-3 (17 kDa), Bax (21 kDa), Bcl-2 (26 kDa), and cytochrome C (14 kDa). Note that samples were obtained from two different culture conditions in the presence or absence of STS treatment (100 nM). ( B ) Quantification of immunoblot assay showing that cleaved caspase-3 expression was significantly increased in the two bvFTD-iPSNs compared with the normal control. ( C ) Quantification of immunoblot assay by obtaining the ratio of Bax and Bcl-2 expression showing that significantly-increased patterns were observed in the two bvFTD-iPSNs compared with the normal control. ( D ) Quantification of immunoblot assay showing that cytochrome C expression was significantly increased in the two bvFTD-iPSNs compared with the normal control. Note that blot images indicated by dividing lines were chosen from different immunoblots due to the large size of samples. Whole blot images are provided in Supplementary Figure S3A–D . Protein quantifications were conducted under the same exposure time ( n = 3) (*: vs. normal control) * p

    Article Snippet: The following primary antibodies were used—anti-TDP43 (1:200, Proteintech), anti-FUS/TLS (1:200, Santa Cruz Biotechnology), Tau5 anti-tau (1:1000, Thermo Fisher Scientific), AT8 anti-p-tau (1:1000, Thermo Fisher Scientific), and anti-caspase-3 (1:200, Millipore).

    Techniques: Expressing, Derivative Assay, Western Blot

    Biological consequences of miR-210, miR-147a and miR-147b overexpression on A549 cells proliferation and viability. A549 cells were transfected with 10 nM pre-miR-210, pre-miR-147a, pre-miR-147b or pre-miR-Neg and analyzed for several proliferation (A-E) and viability (F-G) parameters. A) Confluent cell monolayer was wound and filmed for 55h under light time laps microscope. Curves represent wound beds closure quantified by measuring the wound bed surface at the indicated times after injury using the Image J software. Values are expressed in percentage of the initial surface and correspond to the mean ± SD of 3 microscope fields. B) Effect of miR-210 and miR-147 family on A549 cell proliferation. Exponentially growing A549 cells were transfected and counted each day during 4 days with blue Trypan. Data show mean ± SD values of trypan blue negative (left panel) and trypan-blue positive cell number (right panel) from 2 independent experiments performed in triplicate. C) Cells were stained with propidium iodide and analyzed by flow cytometry. The G0/G1 (1), S (2) and G2/M (3) fractions were quantified in each condition. D) Quantification of each of these 3 fractions (G0/G1, S and G2/M) from 3 independent experiments. E) Expression of Cyclin D, Cyclin A, Cyclin E, CDK4, CDK6, pRB (6 molecules involved in G1 phase progression), p27Kip1 (inhibitor of G1 phase progression) and Cyclin B (involved in G2/M phase) were assessed by Western blot. Hsp60 corresponds to the loading control. F) Caspase 3/7 assay was performed at 3, 4 and 5 days after transfection. Data are mean ± SD values of 3 independent experiments performed in triplicate. See also Figure S4A . G) Expression of active caspase-3 (cleaved) and PARP, a substrate of caspase-3 was analyzed by Western blot. HSP60 corresponds to the loading control. Normalized densitometric quantification are shown for each lane. See also Figure S4C and Figure S4D (* p

    Journal: PLoS ONE

    Article Title: "Seed-Milarity" Confers to hsa-miR-210 and hsa-miR-147b Similar Functional Activity

    doi: 10.1371/journal.pone.0044919

    Figure Lengend Snippet: Biological consequences of miR-210, miR-147a and miR-147b overexpression on A549 cells proliferation and viability. A549 cells were transfected with 10 nM pre-miR-210, pre-miR-147a, pre-miR-147b or pre-miR-Neg and analyzed for several proliferation (A-E) and viability (F-G) parameters. A) Confluent cell monolayer was wound and filmed for 55h under light time laps microscope. Curves represent wound beds closure quantified by measuring the wound bed surface at the indicated times after injury using the Image J software. Values are expressed in percentage of the initial surface and correspond to the mean ± SD of 3 microscope fields. B) Effect of miR-210 and miR-147 family on A549 cell proliferation. Exponentially growing A549 cells were transfected and counted each day during 4 days with blue Trypan. Data show mean ± SD values of trypan blue negative (left panel) and trypan-blue positive cell number (right panel) from 2 independent experiments performed in triplicate. C) Cells were stained with propidium iodide and analyzed by flow cytometry. The G0/G1 (1), S (2) and G2/M (3) fractions were quantified in each condition. D) Quantification of each of these 3 fractions (G0/G1, S and G2/M) from 3 independent experiments. E) Expression of Cyclin D, Cyclin A, Cyclin E, CDK4, CDK6, pRB (6 molecules involved in G1 phase progression), p27Kip1 (inhibitor of G1 phase progression) and Cyclin B (involved in G2/M phase) were assessed by Western blot. Hsp60 corresponds to the loading control. F) Caspase 3/7 assay was performed at 3, 4 and 5 days after transfection. Data are mean ± SD values of 3 independent experiments performed in triplicate. See also Figure S4A . G) Expression of active caspase-3 (cleaved) and PARP, a substrate of caspase-3 was analyzed by Western blot. HSP60 corresponds to the loading control. Normalized densitometric quantification are shown for each lane. See also Figure S4C and Figure S4D (* p

    Article Snippet: Anti-RB (MAB3186) mouse mAb and anti-caspase-3 (total and cleaved) were from Millipore and Cell Signaling, respectively.

    Techniques: Over Expression, Transfection, Microscopy, Software, Staining, Flow Cytometry, Cytometry, Expressing, Western Blot