bapta am  (MedChemExpress)


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    MedChemExpress bapta am
    Calcium is responsible for zinc deficiency-induced STAT3 activation. <t>BAPTA-AM</t> (10 μM) (A,B) or <t>EGTA-AM</t> (10 μM) (C,D) was applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation ( n = 5). * p
    Bapta Am, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bapta am/product/MedChemExpress
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bapta am - by Bioz Stars, 2022-05
    94/100 stars

    Images

    1) Product Images from "Endoplasmic Reticulum Stress/Ca2+-Calmodulin-Dependent Protein Kinase/Signal Transducer and Activator of Transcription 3 Pathway Plays a Role in the Regulation of Cellular Zinc Deficiency in Myocardial Ischemia/Reperfusion Injury"

    Article Title: Endoplasmic Reticulum Stress/Ca2+-Calmodulin-Dependent Protein Kinase/Signal Transducer and Activator of Transcription 3 Pathway Plays a Role in the Regulation of Cellular Zinc Deficiency in Myocardial Ischemia/Reperfusion Injury

    Journal: Frontiers in Physiology

    doi: 10.3389/fphys.2021.736920

    Calcium is responsible for zinc deficiency-induced STAT3 activation. BAPTA-AM (10 μM) (A,B) or EGTA-AM (10 μM) (C,D) was applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation ( n = 5). * p
    Figure Legend Snippet: Calcium is responsible for zinc deficiency-induced STAT3 activation. BAPTA-AM (10 μM) (A,B) or EGTA-AM (10 μM) (C,D) was applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation ( n = 5). * p

    Techniques Used: Activation Assay

    P-CaMKII is involved in zinc deficiency-induced STAT3 activation. KN93, KN92 (A,B) , H89 (C), or BAPTA-AM (D) (10 μM, n = 5) were applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation. * p
    Figure Legend Snippet: P-CaMKII is involved in zinc deficiency-induced STAT3 activation. KN93, KN92 (A,B) , H89 (C), or BAPTA-AM (D) (10 μM, n = 5) were applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation. * p

    Techniques Used: Activation Assay

    ER Stress/CaMKII is involved in the regulation of ZIP9 by STAT3 (A,B) H89, KN93, or BAPTA-AM (10 μM, n = 5) were applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation. (C) Mouse hearts were ischemic for 30 min and then reperfused for 30 min. H89, KN93 or BAPTA-AM (10 mg/kg) were injected 5 min before reperfusion and continued for 30 min through the tail vein ( n = 7). (D) Zn 2+ levels were monitored with inductively coupled plasma optical emission spectroscopy (ICPOES, n = 5). * p
    Figure Legend Snippet: ER Stress/CaMKII is involved in the regulation of ZIP9 by STAT3 (A,B) H89, KN93, or BAPTA-AM (10 μM, n = 5) were applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation. (C) Mouse hearts were ischemic for 30 min and then reperfused for 30 min. H89, KN93 or BAPTA-AM (10 mg/kg) were injected 5 min before reperfusion and continued for 30 min through the tail vein ( n = 7). (D) Zn 2+ levels were monitored with inductively coupled plasma optical emission spectroscopy (ICPOES, n = 5). * p

    Techniques Used: Injection, Spectroscopy

    2) Product Images from "CaMKII/proteasome/cytosolic calcium/cathepsin B axis was present in tryspin activation induced by nicardipine"

    Article Title: CaMKII/proteasome/cytosolic calcium/cathepsin B axis was present in tryspin activation induced by nicardipine

    Journal: Bioscience Reports

    doi: 10.1042/BSR20190516

    Nicardipine-mediated increase in trypsinogen and cathepsin B activation depends on cytosolic calcium in primary pancreatic acinar cells Primary pancreatic acinar cells were incubated with 2.5 μM nicardipine for 1 h with or without calcium chelator BAPTA AM (10 μM). Cells were lysed and the cell lysates were subjected to trypsin ( A ) and cathepsin B ( B ) activity assay or were subjected to Western blotting analysis using anti-cathepsin B antibody, with actin as a loading control ( C ). Error bars for enzyme activity were presented as the standard deviation of triplicate samples. Error bars for graph of Western blot analysis represented the standard deviation between densitometry data from three unique experiments; * P
    Figure Legend Snippet: Nicardipine-mediated increase in trypsinogen and cathepsin B activation depends on cytosolic calcium in primary pancreatic acinar cells Primary pancreatic acinar cells were incubated with 2.5 μM nicardipine for 1 h with or without calcium chelator BAPTA AM (10 μM). Cells were lysed and the cell lysates were subjected to trypsin ( A ) and cathepsin B ( B ) activity assay or were subjected to Western blotting analysis using anti-cathepsin B antibody, with actin as a loading control ( C ). Error bars for enzyme activity were presented as the standard deviation of triplicate samples. Error bars for graph of Western blot analysis represented the standard deviation between densitometry data from three unique experiments; * P

    Techniques Used: Activation Assay, Incubation, Activity Assay, Western Blot, Standard Deviation

    Nicardipine-induced trypsinogen and cathepsin B activation depends on cytosolic calcium in AR42J cells AR42J cells were incubated with 2.5 μM nicardipine for indicated durations ( A ) or with nicardipine at indicated concentrations for 6 h ( B and C ). Cells were stained with calcium specific dye fluo-4AM (1 μM) at 37°C for 10 min, and then were subjected to calcium intensity assay by FACS after digestion (A and B) or were directly imaged with fluorescence microscopy (C). AR42J cells were incubated with 2.5 μM nicardipine for 6 h with or without calcium chelator BAPTA AM (10 μM). Cells were stained with calcium-specific dye fluo-4AM (1 μM) at 37°C for 10 min, and then were subjected to calcium intensity assay by FACS ( D ) or were directly imaged with fluorescence microscopy ( E ). After the indicated treatment, cells were lysed and the cell lysates were subjected to trypsin ( F ) and cathepsin B ( G ) activity assay or were subjected to Western blotting analysis using anti-cathepsin B antibody, with actin as the loading control ( H ). Error bars for enzyme activity or intensity of calcium specific staining were presented as the standard deviation of triplicate samples. Error bars for graph of Western blot analysis represent the standard deviation between densitometry data from three unique experiments; * P
    Figure Legend Snippet: Nicardipine-induced trypsinogen and cathepsin B activation depends on cytosolic calcium in AR42J cells AR42J cells were incubated with 2.5 μM nicardipine for indicated durations ( A ) or with nicardipine at indicated concentrations for 6 h ( B and C ). Cells were stained with calcium specific dye fluo-4AM (1 μM) at 37°C for 10 min, and then were subjected to calcium intensity assay by FACS after digestion (A and B) or were directly imaged with fluorescence microscopy (C). AR42J cells were incubated with 2.5 μM nicardipine for 6 h with or without calcium chelator BAPTA AM (10 μM). Cells were stained with calcium-specific dye fluo-4AM (1 μM) at 37°C for 10 min, and then were subjected to calcium intensity assay by FACS ( D ) or were directly imaged with fluorescence microscopy ( E ). After the indicated treatment, cells were lysed and the cell lysates were subjected to trypsin ( F ) and cathepsin B ( G ) activity assay or were subjected to Western blotting analysis using anti-cathepsin B antibody, with actin as the loading control ( H ). Error bars for enzyme activity or intensity of calcium specific staining were presented as the standard deviation of triplicate samples. Error bars for graph of Western blot analysis represent the standard deviation between densitometry data from three unique experiments; * P

    Techniques Used: Activation Assay, Incubation, Staining, FACS, Fluorescence, Microscopy, Activity Assay, Western Blot, Standard Deviation

    3) Product Images from "Inhibition of IP3R/Ca2+ Dysregulation Protects Mice From Ventilator-Induced Lung Injury via Endoplasmic Reticulum and Mitochondrial Pathways"

    Article Title: Inhibition of IP3R/Ca2+ Dysregulation Protects Mice From Ventilator-Induced Lung Injury via Endoplasmic Reticulum and Mitochondrial Pathways

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2021.729094

    Effects of carbachol, 2-APB and BAPTA-AM on HTV-induced pathological lung injury and inflammation. (A) H E staining the histology of lung tissues from group CON, HTV, HTV+Carbachol, HTV+2-APB mice, and the HTV-treated mice pretreated with Ca2+ chelator BAPTA-AM (HTV+BAPTA-AM group). Scale bar: 200μm. An inset picture was employed to show the indicated area at 4X magnification. (B) Pathological scores were assessed by results of H E staining. (C) Lung edema was assessed by determining the weight ratio between wet and dry lungs. (D) Total protein concentration in BALF. (E) Infiltrated cell counts in BALF. (F–H) Levels of IL-1β (F) , IL-6 (G) and TNF-α (H) in BALF. Data are expressed as means ± SD (n = 8 per group except for group HTV+ Carbachol (n=7), which has 1 mouse died unexpectedly and was removed from analysis). * P
    Figure Legend Snippet: Effects of carbachol, 2-APB and BAPTA-AM on HTV-induced pathological lung injury and inflammation. (A) H E staining the histology of lung tissues from group CON, HTV, HTV+Carbachol, HTV+2-APB mice, and the HTV-treated mice pretreated with Ca2+ chelator BAPTA-AM (HTV+BAPTA-AM group). Scale bar: 200μm. An inset picture was employed to show the indicated area at 4X magnification. (B) Pathological scores were assessed by results of H E staining. (C) Lung edema was assessed by determining the weight ratio between wet and dry lungs. (D) Total protein concentration in BALF. (E) Infiltrated cell counts in BALF. (F–H) Levels of IL-1β (F) , IL-6 (G) and TNF-α (H) in BALF. Data are expressed as means ± SD (n = 8 per group except for group HTV+ Carbachol (n=7), which has 1 mouse died unexpectedly and was removed from analysis). * P

    Techniques Used: Staining, Mouse Assay, Protein Concentration

    4) Product Images from "TGR5 Activation Ameliorates Mitochondrial Homeostasis via Regulating the PKCδ/Drp1-HK2 Signaling in Diabetic Retinopathy"

    Article Title: TGR5 Activation Ameliorates Mitochondrial Homeostasis via Regulating the PKCδ/Drp1-HK2 Signaling in Diabetic Retinopathy

    Journal: Frontiers in Cell and Developmental Biology

    doi: 10.3389/fcell.2021.759421

    TGR5 decreases the Drp1 phosphorylation by inhibiting the Ca 2+ -PKCδ pathway. (A, B) RMECs were pretreated with INT-777 (30 μM) for 2 h and exposed with or without HG (33 mM) for 3 days. RMECs were transduced with TGR5 siRNA for 48 h and then incubated with BAPTA-AM (10 μM) for 2 h followed by HG (33 mM) for (C) three or (D) 5 days. (E, F) RMECs were transduced with TGR5 siRNA or PKCδ siRNA for 48 h and then incubated with HG (33 mM) for 3 days. (A) PKCδ phosphorylation level was detected by Western blotting. (B) Intracellular Ca 2+ levels were detected by Fluo 4-AM (2 μM, 30 min) and mitochondria were stained with MitoBright LT Red (200 nM, 30 min). Colocalization of intracellular Ca 2+ and mitochondria was detected by confocal microscopy. Scale bar = 25 μm. Intracellular Ca 2+ levels were detected by Fluo 4-AM (2 μ M, 30 min; scale bar = 25 μ m) . (C) Western blotting was conducted to determine the phosphorylation level of PKCδ. (D) Mitochondria were stained with MitoBright LT Red (200 nM, 30 min) and detected by confocal microscopy (63X_bar, 10 μm). Quantification of cells with different forms of mitochondrial morphology is shown in the bar chart. (E) PKCδ transfection efficiency was evaluated by Western blotting. (F) Drp1 phosphorylation levels were detected in different groups by Western blot. All data were presented as mean ± SD and analysed by RM ANOVA with Tukey’s HSD test. # p
    Figure Legend Snippet: TGR5 decreases the Drp1 phosphorylation by inhibiting the Ca 2+ -PKCδ pathway. (A, B) RMECs were pretreated with INT-777 (30 μM) for 2 h and exposed with or without HG (33 mM) for 3 days. RMECs were transduced with TGR5 siRNA for 48 h and then incubated with BAPTA-AM (10 μM) for 2 h followed by HG (33 mM) for (C) three or (D) 5 days. (E, F) RMECs were transduced with TGR5 siRNA or PKCδ siRNA for 48 h and then incubated with HG (33 mM) for 3 days. (A) PKCδ phosphorylation level was detected by Western blotting. (B) Intracellular Ca 2+ levels were detected by Fluo 4-AM (2 μM, 30 min) and mitochondria were stained with MitoBright LT Red (200 nM, 30 min). Colocalization of intracellular Ca 2+ and mitochondria was detected by confocal microscopy. Scale bar = 25 μm. Intracellular Ca 2+ levels were detected by Fluo 4-AM (2 μ M, 30 min; scale bar = 25 μ m) . (C) Western blotting was conducted to determine the phosphorylation level of PKCδ. (D) Mitochondria were stained with MitoBright LT Red (200 nM, 30 min) and detected by confocal microscopy (63X_bar, 10 μm). Quantification of cells with different forms of mitochondrial morphology is shown in the bar chart. (E) PKCδ transfection efficiency was evaluated by Western blotting. (F) Drp1 phosphorylation levels were detected in different groups by Western blot. All data were presented as mean ± SD and analysed by RM ANOVA with Tukey’s HSD test. # p

    Techniques Used: Transduction, Incubation, Western Blot, Staining, Confocal Microscopy, Transfection

    5) Product Images from "Ginsenoside Rk1 inhibits cell proliferation and promotes apoptosis in lung squamous cell carcinoma by calcium signaling pathway"

    Article Title: Ginsenoside Rk1 inhibits cell proliferation and promotes apoptosis in lung squamous cell carcinoma by calcium signaling pathway

    Journal: RSC Advances

    doi: 10.1039/c9ra05037j

    Rk1 increased intracellular calcium levels to activate calpain-induced apoptosis in SK-MES-1 and H226 cells. (A) Cells were treated with the indicated concentrations of Rk1 for 24 h. The levels of calpain, cleaved caspase 12, 7 and cleaved PARP were determined via Western blotting. (B) BAPTA-AM pretreated cells using the above methods, and calpain, cleaved caspase 12, 7, 3, cleaved PARP and Bax were analyzed by Western blotting. (C) Calpeptin pretreated cells using the above methods, and calpain, cleaved caspase -12, -7, -3 and cleaved PARP were analyzed by Western blotting. Values are presented as the means ± SD, n = 3, * p
    Figure Legend Snippet: Rk1 increased intracellular calcium levels to activate calpain-induced apoptosis in SK-MES-1 and H226 cells. (A) Cells were treated with the indicated concentrations of Rk1 for 24 h. The levels of calpain, cleaved caspase 12, 7 and cleaved PARP were determined via Western blotting. (B) BAPTA-AM pretreated cells using the above methods, and calpain, cleaved caspase 12, 7, 3, cleaved PARP and Bax were analyzed by Western blotting. (C) Calpeptin pretreated cells using the above methods, and calpain, cleaved caspase -12, -7, -3 and cleaved PARP were analyzed by Western blotting. Values are presented as the means ± SD, n = 3, * p

    Techniques Used: Western Blot

    Rk1 induced endoplasmic reticulum stress to release calcium ions in SK-MES-1 and H226 cells. (A) Cells were treated with the indicated concentrations of Rk1 for 24 h. The levels of GRP78, ATF-6, IRE1α and CHOP were determined via Western blot. (B) Intracellular calcium levels were analyzed via flow cytometry after Fluo-3/AM staining. (C) SK-MES-1 cells were pretreated with 100 μM 2-APB (IP3Rs channel inhibitor), 40 μM BAPTA-AM (intracellular Ca 2+ chelating agent) or 50 μM calpeptin (calpain inhibitor) for 2 h and then treated with 100 μM Rk1 for 24 h. Cell inhibition was determined via MTT. Values are presented as the means ± SD, n = 3; * p
    Figure Legend Snippet: Rk1 induced endoplasmic reticulum stress to release calcium ions in SK-MES-1 and H226 cells. (A) Cells were treated with the indicated concentrations of Rk1 for 24 h. The levels of GRP78, ATF-6, IRE1α and CHOP were determined via Western blot. (B) Intracellular calcium levels were analyzed via flow cytometry after Fluo-3/AM staining. (C) SK-MES-1 cells were pretreated with 100 μM 2-APB (IP3Rs channel inhibitor), 40 μM BAPTA-AM (intracellular Ca 2+ chelating agent) or 50 μM calpeptin (calpain inhibitor) for 2 h and then treated with 100 μM Rk1 for 24 h. Cell inhibition was determined via MTT. Values are presented as the means ± SD, n = 3; * p

    Techniques Used: Western Blot, Flow Cytometry, Staining, Inhibition, MTT Assay

    6) Product Images from "Sacubitril Ameliorates Cardiac Fibrosis Through Inhibiting TRPM7 Channel"

    Article Title: Sacubitril Ameliorates Cardiac Fibrosis Through Inhibiting TRPM7 Channel

    Journal: Frontiers in Cell and Developmental Biology

    doi: 10.3389/fcell.2021.760035

    LBQ657 reduced hypoxia-induced necrosis by inhibiting TRPM7-mediated Ca 2+ influx in cardiomyocytes. (A) Comparison of TRPM7 protein levels in MEF and H 9 C 2 cells. (B) Fluorescence intensity of Fluo-4-AM fluorescent dye in 488 nm excitation light of normoxic H 9 C 2 , hypoxic H 9 C 2 and hypoxic H 9 C 2 pre-treated with LBQ657. (C) Protein levels of caspase3, cleaved caspase3, LC3B-I and LC3B-II in hypoxic H 9 C 2 and hypoxic H 9 C 2 pre-treated with LBQ657. (D) Protein levels of RIPK1/RIPK3/MLKL/p-MLKL in hypoxic H 9 C 2 and hypoxic H 9 C 2 pre-treated with LBQ657. (E) Protein levels of RIPK1/RIPK3/MLKL/p-MLKL in normoxic H 9 C 2 and normoxic H 9 C 2 treated with LBQ657. (F) Protein levels of RIPK1/RIPK3/MLKL/p-MLKL in hypoxic H 9 C 2 and hypoxic H 9 C 2 pre-treated with BAPTA-AM. The data presented are mean ± SD. Each group contained the results of three independent repeated trials. β-actin was used as the internal reference protein for normalization and statistical analysis. ∗∗∗∗ P
    Figure Legend Snippet: LBQ657 reduced hypoxia-induced necrosis by inhibiting TRPM7-mediated Ca 2+ influx in cardiomyocytes. (A) Comparison of TRPM7 protein levels in MEF and H 9 C 2 cells. (B) Fluorescence intensity of Fluo-4-AM fluorescent dye in 488 nm excitation light of normoxic H 9 C 2 , hypoxic H 9 C 2 and hypoxic H 9 C 2 pre-treated with LBQ657. (C) Protein levels of caspase3, cleaved caspase3, LC3B-I and LC3B-II in hypoxic H 9 C 2 and hypoxic H 9 C 2 pre-treated with LBQ657. (D) Protein levels of RIPK1/RIPK3/MLKL/p-MLKL in hypoxic H 9 C 2 and hypoxic H 9 C 2 pre-treated with LBQ657. (E) Protein levels of RIPK1/RIPK3/MLKL/p-MLKL in normoxic H 9 C 2 and normoxic H 9 C 2 treated with LBQ657. (F) Protein levels of RIPK1/RIPK3/MLKL/p-MLKL in hypoxic H 9 C 2 and hypoxic H 9 C 2 pre-treated with BAPTA-AM. The data presented are mean ± SD. Each group contained the results of three independent repeated trials. β-actin was used as the internal reference protein for normalization and statistical analysis. ∗∗∗∗ P

    Techniques Used: Fluorescence

    7) Product Images from "Neuroinflammation is induced by tongue-instilled ZnO nanoparticles via the Ca2+-dependent NF-κB and MAPK pathways"

    Article Title: Neuroinflammation is induced by tongue-instilled ZnO nanoparticles via the Ca2+-dependent NF-κB and MAPK pathways

    Journal: Particle and Fibre Toxicology

    doi: 10.1186/s12989-018-0274-0

    ZnO NPs-induced inflammation is mediated by calcium-dependent pathways in BV2 cells. BV2 cells were preincubated for 1 h with A839977 (200 nM) and BAPTA-AM (20 μM) before ZnO NPs treatment. After the cells were treated with ZnO NPs at a dose of 30 μg/ml for 6 h. Summary of cell viability ( a ), TNF-α ( b ) and IL-1β ( c ) release and the expression of proinflammatory genes ( f ). The concentration of Ca 2+ in BV2 cells, cells were stained with Ca 2+ indicator Fluo4-AM (green) and DAPI (blue) ( d ). Scale bar represents 200 μm. Compare the mean fluorescence intensity of Ca 2+ measured in BV2 cells ( g ). Total proteins of BV2 cells were extracted, and the levels of P 2 X 7 , NF-κB, ERK and p38 signaling pathway molecules were analyzed via Western Blot ( e ). The gray value was semiquantitative as shown in histogram ( h ). The 30 μg/mL ZnO NPs-induced cytotoxicity, increase in proinflammatory cytokine release and NF-κB, ERK and p38 phosphorylation was significantly inhibited by BAPTA-AM. Results shown as means ± SD from three independent experiments, compare with control group, * P
    Figure Legend Snippet: ZnO NPs-induced inflammation is mediated by calcium-dependent pathways in BV2 cells. BV2 cells were preincubated for 1 h with A839977 (200 nM) and BAPTA-AM (20 μM) before ZnO NPs treatment. After the cells were treated with ZnO NPs at a dose of 30 μg/ml for 6 h. Summary of cell viability ( a ), TNF-α ( b ) and IL-1β ( c ) release and the expression of proinflammatory genes ( f ). The concentration of Ca 2+ in BV2 cells, cells were stained with Ca 2+ indicator Fluo4-AM (green) and DAPI (blue) ( d ). Scale bar represents 200 μm. Compare the mean fluorescence intensity of Ca 2+ measured in BV2 cells ( g ). Total proteins of BV2 cells were extracted, and the levels of P 2 X 7 , NF-κB, ERK and p38 signaling pathway molecules were analyzed via Western Blot ( e ). The gray value was semiquantitative as shown in histogram ( h ). The 30 μg/mL ZnO NPs-induced cytotoxicity, increase in proinflammatory cytokine release and NF-κB, ERK and p38 phosphorylation was significantly inhibited by BAPTA-AM. Results shown as means ± SD from three independent experiments, compare with control group, * P

    Techniques Used: Expressing, Concentration Assay, Staining, Fluorescence, Western Blot

    8) Product Images from "Porcine deltacoronavirus (PDCoV) modulates calcium influx to favor viral replication"

    Article Title: Porcine deltacoronavirus (PDCoV) modulates calcium influx to favor viral replication

    Journal: Virology

    doi: 10.1016/j.virol.2019.10.011

    Ca 2+ channel blockers inhibit PDCoV production. IPI-2I cells were treated with diltiazem hydrochloride (DTZ, 200 μM), bepridil hydrochloride (BP, 20 μM), 2-APB (50 μM) and BAPTA-AM (25 μM) for 1 h, and then infected with PDCoV (MOI = 0.5). At 6 or 12 hpi, the infected cells were collected to detect the expression of PDCoV mRNA and the N protein (A). Viral titers were determined by the PFU assay (B).
    Figure Legend Snippet: Ca 2+ channel blockers inhibit PDCoV production. IPI-2I cells were treated with diltiazem hydrochloride (DTZ, 200 μM), bepridil hydrochloride (BP, 20 μM), 2-APB (50 μM) and BAPTA-AM (25 μM) for 1 h, and then infected with PDCoV (MOI = 0.5). At 6 or 12 hpi, the infected cells were collected to detect the expression of PDCoV mRNA and the N protein (A). Viral titers were determined by the PFU assay (B).

    Techniques Used: Infection, Expressing

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    MedChemExpress bapta am
    Calcium is responsible for zinc deficiency-induced STAT3 activation. <t>BAPTA-AM</t> (10 μM) (A,B) or <t>EGTA-AM</t> (10 μM) (C,D) was applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation ( n = 5). * p
    Bapta Am, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bapta am/product/MedChemExpress
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bapta am - by Bioz Stars, 2022-05
    94/100 stars
      Buy from Supplier

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    Calcium is responsible for zinc deficiency-induced STAT3 activation. BAPTA-AM (10 μM) (A,B) or EGTA-AM (10 μM) (C,D) was applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation ( n = 5). * p

    Journal: Frontiers in Physiology

    Article Title: Endoplasmic Reticulum Stress/Ca2+-Calmodulin-Dependent Protein Kinase/Signal Transducer and Activator of Transcription 3 Pathway Plays a Role in the Regulation of Cellular Zinc Deficiency in Myocardial Ischemia/Reperfusion Injury

    doi: 10.3389/fphys.2021.736920

    Figure Lengend Snippet: Calcium is responsible for zinc deficiency-induced STAT3 activation. BAPTA-AM (10 μM) (A,B) or EGTA-AM (10 μM) (C,D) was applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation ( n = 5). * p

    Article Snippet: BAPTA-AM, EGTA-AM, H89, 2APB, and stattic were purchased from MCE (NJ, United States).

    Techniques: Activation Assay

    P-CaMKII is involved in zinc deficiency-induced STAT3 activation. KN93, KN92 (A,B) , H89 (C), or BAPTA-AM (D) (10 μM, n = 5) were applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation. * p

    Journal: Frontiers in Physiology

    Article Title: Endoplasmic Reticulum Stress/Ca2+-Calmodulin-Dependent Protein Kinase/Signal Transducer and Activator of Transcription 3 Pathway Plays a Role in the Regulation of Cellular Zinc Deficiency in Myocardial Ischemia/Reperfusion Injury

    doi: 10.3389/fphys.2021.736920

    Figure Lengend Snippet: P-CaMKII is involved in zinc deficiency-induced STAT3 activation. KN93, KN92 (A,B) , H89 (C), or BAPTA-AM (D) (10 μM, n = 5) were applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation. * p

    Article Snippet: BAPTA-AM, EGTA-AM, H89, 2APB, and stattic were purchased from MCE (NJ, United States).

    Techniques: Activation Assay

    ER Stress/CaMKII is involved in the regulation of ZIP9 by STAT3 (A,B) H89, KN93, or BAPTA-AM (10 μM, n = 5) were applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation. (C) Mouse hearts were ischemic for 30 min and then reperfused for 30 min. H89, KN93 or BAPTA-AM (10 mg/kg) were injected 5 min before reperfusion and continued for 30 min through the tail vein ( n = 7). (D) Zn 2+ levels were monitored with inductively coupled plasma optical emission spectroscopy (ICPOES, n = 5). * p

    Journal: Frontiers in Physiology

    Article Title: Endoplasmic Reticulum Stress/Ca2+-Calmodulin-Dependent Protein Kinase/Signal Transducer and Activator of Transcription 3 Pathway Plays a Role in the Regulation of Cellular Zinc Deficiency in Myocardial Ischemia/Reperfusion Injury

    doi: 10.3389/fphys.2021.736920

    Figure Lengend Snippet: ER Stress/CaMKII is involved in the regulation of ZIP9 by STAT3 (A,B) H89, KN93, or BAPTA-AM (10 μM, n = 5) were applied 2 h before exposure to TPEN for 2 h or 30 min before the onset of reoxygenation. (C) Mouse hearts were ischemic for 30 min and then reperfused for 30 min. H89, KN93 or BAPTA-AM (10 mg/kg) were injected 5 min before reperfusion and continued for 30 min through the tail vein ( n = 7). (D) Zn 2+ levels were monitored with inductively coupled plasma optical emission spectroscopy (ICPOES, n = 5). * p

    Article Snippet: BAPTA-AM, EGTA-AM, H89, 2APB, and stattic were purchased from MCE (NJ, United States).

    Techniques: Injection, Spectroscopy

    Nicardipine-mediated increase in trypsinogen and cathepsin B activation depends on cytosolic calcium in primary pancreatic acinar cells Primary pancreatic acinar cells were incubated with 2.5 μM nicardipine for 1 h with or without calcium chelator BAPTA AM (10 μM). Cells were lysed and the cell lysates were subjected to trypsin ( A ) and cathepsin B ( B ) activity assay or were subjected to Western blotting analysis using anti-cathepsin B antibody, with actin as a loading control ( C ). Error bars for enzyme activity were presented as the standard deviation of triplicate samples. Error bars for graph of Western blot analysis represented the standard deviation between densitometry data from three unique experiments; * P

    Journal: Bioscience Reports

    Article Title: CaMKII/proteasome/cytosolic calcium/cathepsin B axis was present in tryspin activation induced by nicardipine

    doi: 10.1042/BSR20190516

    Figure Lengend Snippet: Nicardipine-mediated increase in trypsinogen and cathepsin B activation depends on cytosolic calcium in primary pancreatic acinar cells Primary pancreatic acinar cells were incubated with 2.5 μM nicardipine for 1 h with or without calcium chelator BAPTA AM (10 μM). Cells were lysed and the cell lysates were subjected to trypsin ( A ) and cathepsin B ( B ) activity assay or were subjected to Western blotting analysis using anti-cathepsin B antibody, with actin as a loading control ( C ). Error bars for enzyme activity were presented as the standard deviation of triplicate samples. Error bars for graph of Western blot analysis represented the standard deviation between densitometry data from three unique experiments; * P

    Article Snippet: Cerulein, nicardipine, CA074me, and BAPTA AM were obtained from MCE.

    Techniques: Activation Assay, Incubation, Activity Assay, Western Blot, Standard Deviation

    Nicardipine-induced trypsinogen and cathepsin B activation depends on cytosolic calcium in AR42J cells AR42J cells were incubated with 2.5 μM nicardipine for indicated durations ( A ) or with nicardipine at indicated concentrations for 6 h ( B and C ). Cells were stained with calcium specific dye fluo-4AM (1 μM) at 37°C for 10 min, and then were subjected to calcium intensity assay by FACS after digestion (A and B) or were directly imaged with fluorescence microscopy (C). AR42J cells were incubated with 2.5 μM nicardipine for 6 h with or without calcium chelator BAPTA AM (10 μM). Cells were stained with calcium-specific dye fluo-4AM (1 μM) at 37°C for 10 min, and then were subjected to calcium intensity assay by FACS ( D ) or were directly imaged with fluorescence microscopy ( E ). After the indicated treatment, cells were lysed and the cell lysates were subjected to trypsin ( F ) and cathepsin B ( G ) activity assay or were subjected to Western blotting analysis using anti-cathepsin B antibody, with actin as the loading control ( H ). Error bars for enzyme activity or intensity of calcium specific staining were presented as the standard deviation of triplicate samples. Error bars for graph of Western blot analysis represent the standard deviation between densitometry data from three unique experiments; * P

    Journal: Bioscience Reports

    Article Title: CaMKII/proteasome/cytosolic calcium/cathepsin B axis was present in tryspin activation induced by nicardipine

    doi: 10.1042/BSR20190516

    Figure Lengend Snippet: Nicardipine-induced trypsinogen and cathepsin B activation depends on cytosolic calcium in AR42J cells AR42J cells were incubated with 2.5 μM nicardipine for indicated durations ( A ) or with nicardipine at indicated concentrations for 6 h ( B and C ). Cells were stained with calcium specific dye fluo-4AM (1 μM) at 37°C for 10 min, and then were subjected to calcium intensity assay by FACS after digestion (A and B) or were directly imaged with fluorescence microscopy (C). AR42J cells were incubated with 2.5 μM nicardipine for 6 h with or without calcium chelator BAPTA AM (10 μM). Cells were stained with calcium-specific dye fluo-4AM (1 μM) at 37°C for 10 min, and then were subjected to calcium intensity assay by FACS ( D ) or were directly imaged with fluorescence microscopy ( E ). After the indicated treatment, cells were lysed and the cell lysates were subjected to trypsin ( F ) and cathepsin B ( G ) activity assay or were subjected to Western blotting analysis using anti-cathepsin B antibody, with actin as the loading control ( H ). Error bars for enzyme activity or intensity of calcium specific staining were presented as the standard deviation of triplicate samples. Error bars for graph of Western blot analysis represent the standard deviation between densitometry data from three unique experiments; * P

    Article Snippet: Cerulein, nicardipine, CA074me, and BAPTA AM were obtained from MCE.

    Techniques: Activation Assay, Incubation, Staining, FACS, Fluorescence, Microscopy, Activity Assay, Western Blot, Standard Deviation

    Effects of carbachol, 2-APB and BAPTA-AM on HTV-induced pathological lung injury and inflammation. (A) H E staining the histology of lung tissues from group CON, HTV, HTV+Carbachol, HTV+2-APB mice, and the HTV-treated mice pretreated with Ca2+ chelator BAPTA-AM (HTV+BAPTA-AM group). Scale bar: 200μm. An inset picture was employed to show the indicated area at 4X magnification. (B) Pathological scores were assessed by results of H E staining. (C) Lung edema was assessed by determining the weight ratio between wet and dry lungs. (D) Total protein concentration in BALF. (E) Infiltrated cell counts in BALF. (F–H) Levels of IL-1β (F) , IL-6 (G) and TNF-α (H) in BALF. Data are expressed as means ± SD (n = 8 per group except for group HTV+ Carbachol (n=7), which has 1 mouse died unexpectedly and was removed from analysis). * P

    Journal: Frontiers in Immunology

    Article Title: Inhibition of IP3R/Ca2+ Dysregulation Protects Mice From Ventilator-Induced Lung Injury via Endoplasmic Reticulum and Mitochondrial Pathways

    doi: 10.3389/fimmu.2021.729094

    Figure Lengend Snippet: Effects of carbachol, 2-APB and BAPTA-AM on HTV-induced pathological lung injury and inflammation. (A) H E staining the histology of lung tissues from group CON, HTV, HTV+Carbachol, HTV+2-APB mice, and the HTV-treated mice pretreated with Ca2+ chelator BAPTA-AM (HTV+BAPTA-AM group). Scale bar: 200μm. An inset picture was employed to show the indicated area at 4X magnification. (B) Pathological scores were assessed by results of H E staining. (C) Lung edema was assessed by determining the weight ratio between wet and dry lungs. (D) Total protein concentration in BALF. (E) Infiltrated cell counts in BALF. (F–H) Levels of IL-1β (F) , IL-6 (G) and TNF-α (H) in BALF. Data are expressed as means ± SD (n = 8 per group except for group HTV+ Carbachol (n=7), which has 1 mouse died unexpectedly and was removed from analysis). * P

    Article Snippet: Reagents used in this study included IP3R agonist carbachol (Abmole Bioscience, USA), IP3R inhibitor 2-aminoethoxydiphenyl borate (2-APB, Tocris Biosciences, UK), and Ca2+ chelator BAPTA-AM (MedChemExpress, USA).

    Techniques: Staining, Mouse Assay, Protein Concentration

    TGR5 decreases the Drp1 phosphorylation by inhibiting the Ca 2+ -PKCδ pathway. (A, B) RMECs were pretreated with INT-777 (30 μM) for 2 h and exposed with or without HG (33 mM) for 3 days. RMECs were transduced with TGR5 siRNA for 48 h and then incubated with BAPTA-AM (10 μM) for 2 h followed by HG (33 mM) for (C) three or (D) 5 days. (E, F) RMECs were transduced with TGR5 siRNA or PKCδ siRNA for 48 h and then incubated with HG (33 mM) for 3 days. (A) PKCδ phosphorylation level was detected by Western blotting. (B) Intracellular Ca 2+ levels were detected by Fluo 4-AM (2 μM, 30 min) and mitochondria were stained with MitoBright LT Red (200 nM, 30 min). Colocalization of intracellular Ca 2+ and mitochondria was detected by confocal microscopy. Scale bar = 25 μm. Intracellular Ca 2+ levels were detected by Fluo 4-AM (2 μ M, 30 min; scale bar = 25 μ m) . (C) Western blotting was conducted to determine the phosphorylation level of PKCδ. (D) Mitochondria were stained with MitoBright LT Red (200 nM, 30 min) and detected by confocal microscopy (63X_bar, 10 μm). Quantification of cells with different forms of mitochondrial morphology is shown in the bar chart. (E) PKCδ transfection efficiency was evaluated by Western blotting. (F) Drp1 phosphorylation levels were detected in different groups by Western blot. All data were presented as mean ± SD and analysed by RM ANOVA with Tukey’s HSD test. # p

    Journal: Frontiers in Cell and Developmental Biology

    Article Title: TGR5 Activation Ameliorates Mitochondrial Homeostasis via Regulating the PKCδ/Drp1-HK2 Signaling in Diabetic Retinopathy

    doi: 10.3389/fcell.2021.759421

    Figure Lengend Snippet: TGR5 decreases the Drp1 phosphorylation by inhibiting the Ca 2+ -PKCδ pathway. (A, B) RMECs were pretreated with INT-777 (30 μM) for 2 h and exposed with or without HG (33 mM) for 3 days. RMECs were transduced with TGR5 siRNA for 48 h and then incubated with BAPTA-AM (10 μM) for 2 h followed by HG (33 mM) for (C) three or (D) 5 days. (E, F) RMECs were transduced with TGR5 siRNA or PKCδ siRNA for 48 h and then incubated with HG (33 mM) for 3 days. (A) PKCδ phosphorylation level was detected by Western blotting. (B) Intracellular Ca 2+ levels were detected by Fluo 4-AM (2 μM, 30 min) and mitochondria were stained with MitoBright LT Red (200 nM, 30 min). Colocalization of intracellular Ca 2+ and mitochondria was detected by confocal microscopy. Scale bar = 25 μm. Intracellular Ca 2+ levels were detected by Fluo 4-AM (2 μ M, 30 min; scale bar = 25 μ m) . (C) Western blotting was conducted to determine the phosphorylation level of PKCδ. (D) Mitochondria were stained with MitoBright LT Red (200 nM, 30 min) and detected by confocal microscopy (63X_bar, 10 μm). Quantification of cells with different forms of mitochondrial morphology is shown in the bar chart. (E) PKCδ transfection efficiency was evaluated by Western blotting. (F) Drp1 phosphorylation levels were detected in different groups by Western blot. All data were presented as mean ± SD and analysed by RM ANOVA with Tukey’s HSD test. # p

    Article Snippet: Mdivi-1, 3-bromopyruvic acid, INT-777, 3-methyladenine, Rapamycin, BAPTA-AM, and Z-VAD (OMe)-FMK were procured from MedChemExpress (NJ, United States).

    Techniques: Transduction, Incubation, Western Blot, Staining, Confocal Microscopy, Transfection