cardiomyocytes (Worthington Biochemical)

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Worthington Biochemical cardiomyocytes

SUMO-1 overexpression protects SERCA2a activity from oxidative stress. (A) <t>Cardiomyocytes</t> were infected with adenoviruses carrying SUMO-1 or β-gal genes for 24 h and then, the cells were exposed to 0.5 μ M of H 2 O 2 for 6 h. SERCA2a SUMOylation was determined by IP with anti-SUMO-1 followed by WB with anti-SERCA2a antibody. Tyrosine nitration of SERCA2a was measured by IP with anti-SERCA2a followed by WB with anti-3-nitrotyrosine antibody. The cell extracts were subjected to ATPase activity assay of SERCA2a. (B) Cardiac-specific Nox4 knockout mice were subjected to TAC operation for 4 weeks. The expression levels of SERCA2a, SUMO-1, and SUMOylated SERCA2a in cardiac tissues of Nox4 knockout mice are shown. Data indicate the mean±SD of three independent experiments. * p

Cardiomyocytes, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 86 stars, based on 1 article reviews
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cardiomyocytes - by Bioz Stars, 2022-05

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1) Product Images from "The Role of SUMO-1 in Cardiac Oxidative Stress and Hypertrophy"

Article Title: The Role of SUMO-1 in Cardiac Oxidative Stress and Hypertrophy

Journal: Antioxidants & Redox Signaling

doi: 10.1089/ars.2014.5983

SUMO-1 overexpression protects SERCA2a activity from oxidative stress. (A) Cardiomyocytes were infected with adenoviruses carrying SUMO-1 or β-gal genes for 24 h and then, the cells were exposed to 0.5 μ M of H 2 O 2 for 6 h. SERCA2a SUMOylation was determined by IP with anti-SUMO-1 followed by WB with anti-SERCA2a antibody. Tyrosine nitration of SERCA2a was measured by IP with anti-SERCA2a followed by WB with anti-3-nitrotyrosine antibody. The cell extracts were subjected to ATPase activity assay of SERCA2a. (B) Cardiac-specific Nox4 knockout mice were subjected to TAC operation for 4 weeks. The expression levels of SERCA2a, SUMO-1, and SUMOylated SERCA2a in cardiac tissues of Nox4 knockout mice are shown. Data indicate the mean±SD of three independent experiments. * p

Figure Legend Snippet: SUMO-1 overexpression protects SERCA2a activity from oxidative stress. (A) Cardiomyocytes were infected with adenoviruses carrying SUMO-1 or β-gal genes for 24 h and then, the cells were exposed to 0.5 μ M of H 2 O 2 for 6 h. SERCA2a SUMOylation was determined by IP with anti-SUMO-1 followed by WB with anti-SERCA2a antibody. Tyrosine nitration of SERCA2a was measured by IP with anti-SERCA2a followed by WB with anti-3-nitrotyrosine antibody. The cell extracts were subjected to ATPase activity assay of SERCA2a. (B) Cardiac-specific Nox4 knockout mice were subjected to TAC operation for 4 weeks. The expression levels of SERCA2a, SUMO-1, and SUMOylated SERCA2a in cardiac tissues of Nox4 knockout mice are shown. Data indicate the mean±SD of three independent experiments. * p

Techniques Used: Over Expression, Activity Assay, Infection, Western Blot, Nitration, Knock-Out, Mouse Assay, Expressing

SUMO-1 overexpression inhibits PE-induced hypertrophic response in cardiomyocytes. (A) The neonatal cardiomyocytes were infected with the indicated adenoviruses and further stimulated with PE (100 μ M ) for 24 h. The relative expression levels of hypertrophic association genes such as ANF, BNP, and myh7 were determined by semi-quantitative RT-PCR ( n =3). (B) The protein synthesis rates after PE stimulation were evaluated by measuring 3 H-leucine incorporation. Data indicate the mean value±SD of three independent experiments. (C) Cell size measurement. (D) MAPK activities after the stimulation of neonatal cardiomyocytes with PE. Cardiomyocytes were infected with indicated adenoviruses for 24 h and then treated with PE (100 μ M ) for 24 h. Cell extracts were examined for amounts of phosphorylated ERK, p38, JNK, and c-Jun using phospho-specific antibodies. Total protein levels of ERK, p38, JNK, and c-Jun were also analyzed. The relative intensity was quantitated using ImageJ software. Data indicate the mean±SD of three independent experiments. # p

Figure Legend Snippet: SUMO-1 overexpression inhibits PE-induced hypertrophic response in cardiomyocytes. (A) The neonatal cardiomyocytes were infected with the indicated adenoviruses and further stimulated with PE (100 μ M ) for 24 h. The relative expression levels of hypertrophic association genes such as ANF, BNP, and myh7 were determined by semi-quantitative RT-PCR ( n =3). (B) The protein synthesis rates after PE stimulation were evaluated by measuring 3 H-leucine incorporation. Data indicate the mean value±SD of three independent experiments. (C) Cell size measurement. (D) MAPK activities after the stimulation of neonatal cardiomyocytes with PE. Cardiomyocytes were infected with indicated adenoviruses for 24 h and then treated with PE (100 μ M ) for 24 h. Cell extracts were examined for amounts of phosphorylated ERK, p38, JNK, and c-Jun using phospho-specific antibodies. Total protein levels of ERK, p38, JNK, and c-Jun were also analyzed. The relative intensity was quantitated using ImageJ software. Data indicate the mean±SD of three independent experiments. # p

Techniques Used: Over Expression, Infection, Expressing, Quantitative RT-PCR, Software

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Fluorescent Activated Cell Sorting Neurospheres, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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α amylase inhibitory activity (Worthington Biochemical)

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<t>α‐Amylase</t> inhibitory activities of butternut squash residues (seed and skin extract). Values are means of duplicate determinations

α Amylase Inhibitory Activity, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Neurosphere differentiation and composition. ( A and B ) 10 days-post ES cell differentiation neurospheres were dissociated and cell composition was quantified using FACS. Plots of V3, V2a, and V1 interneurons and motor neurons from Sim1:Cre;R26/C:LSL:Tomato, Chx10:Cre;R26/C:LSL:Tomato, En1:Cre;R26/C:LSL:Tomato, and Hb9:GFP ES cell reporter lines, respectively are shown after differentiation with ( A ) 1000 nM and ( B ) 5 nM SAG. ( C ) Two Chx:10:Cre;R26/C:LSL:Tomato ES cell lines were differentiated 10 days under a range of SAG concentrations. Tomato+V2a neuron number was quantified using FACS. ( D ) Chx:10:Cre;R26/C:LSL:Tomato lines #1 and #2 were differentiated with 15 nM and 40 nM SAG, respectively. 5 μM DAPT was applied days 6–10. Standardized tomato + V2a neurons relative to no DAPT control. DOI: http://dx.doi.org/10.7554/eLife.21540.004

Journal: eLife

Article Title: Speed and segmentation control mechanisms characterized in rhythmically-active circuits created from spinal neurons produced from genetically-tagged embryonic stem cells

doi: 10.7554/eLife.21540

Figure Lengend Snippet: Neurosphere differentiation and composition. ( A and B ) 10 days-post ES cell differentiation neurospheres were dissociated and cell composition was quantified using FACS. Plots of V3, V2a, and V1 interneurons and motor neurons from Sim1:Cre;R26/C:LSL:Tomato, Chx10:Cre;R26/C:LSL:Tomato, En1:Cre;R26/C:LSL:Tomato, and Hb9:GFP ES cell reporter lines, respectively are shown after differentiation with ( A ) 1000 nM and ( B ) 5 nM SAG. ( C ) Two Chx:10:Cre;R26/C:LSL:Tomato ES cell lines were differentiated 10 days under a range of SAG concentrations. Tomato+V2a neuron number was quantified using FACS. ( D ) Chx:10:Cre;R26/C:LSL:Tomato lines #1 and #2 were differentiated with 15 nM and 40 nM SAG, respectively. 5 μM DAPT was applied days 6–10. Standardized tomato + V2a neurons relative to no DAPT control. DOI: http://dx.doi.org/10.7554/eLife.21540.004

Article Snippet: Fluorescent-activated cell sorting Neurospheres, 6–11 days from ES cells, were dissociated (Papain, Worthington), and then counted with a BD FACScan to determine the percentage of neurons composing neurospheres at different SAG concentrations.

Techniques: Cell Differentiation, FACS

α‐Amylase inhibitory activities of butternut squash residues (seed and skin extract). Values are means of duplicate determinations

Journal: Food Science & Nutrition

Article Title: Evaluation of bioactivity of butternut squash (Cucurbita moschata D.) seeds and skin. Evaluation of bioactivity of butternut squash (Cucurbita moschata D.) seeds and skin

doi: 10.1002/fsn3.1602

Figure Lengend Snippet: α‐Amylase inhibitory activities of butternut squash residues (seed and skin extract). Values are means of duplicate determinations

Article Snippet: The α‐amylase inhibitory activity was expressed as percentage inhibition (Worthington, Weddell, & Neilson, ).

Techniques:

In vitro antioxidants and anti-hypoglycemic effects of AESTL. Bar graphs of dose vs inhibition showing the effect of AESTL and standard drugs on ( A ) DPPH, ( B ) ABTS, ( C ) α-amylase and, ( D ) α-glucosidase activities. Values are mean ± SEM (n = 6).

Journal: Journal of Inflammation Research

Article Title: Sterculia tragacantha Lindl Leaf Extract Ameliorates STZ-Induced Diabetes, Oxidative Stress, Inflammation and Neuronal Impairment

doi: 10.2147/JIR.S319673

Figure Lengend Snippet: In vitro antioxidants and anti-hypoglycemic effects of AESTL. Bar graphs of dose vs inhibition showing the effect of AESTL and standard drugs on ( A ) DPPH, ( B ) ABTS, ( C ) α-amylase and, ( D ) α-glucosidase activities. Values are mean ± SEM (n = 6).

Article Snippet: The α-amylase inhibitory activity of the extract was assayed following the protocol of Worthington.

Techniques: In Vitro, Inhibition

Journal: Journal of Inflammation Research

Article Title: Sterculia tragacantha Lindl Leaf Extract Ameliorates STZ-Induced Diabetes, Oxidative Stress, Inflammation and Neuronal Impairment

doi: 10.2147/JIR.S319673

Figure Lengend Snippet: Molecular docking profile of epicatechin and procyanidin B2 with carbohydrate metabolizing enzymes. Two-dimensional (2 D) representations of the interaction occurring between epicatechin and procyanidin B2 and ( A ) α-amylase and ( B ) α-glucosidase.

Article Snippet: The α-amylase inhibitory activity of the extract was assayed following the protocol of Worthington.

Techniques:

$Activity of Nuc/Nuc2 chimeric proteins. Chimeras consisting of combinations of Nuc and Nuc2 N- and C-terminal protein domains were constructed. Each chimera was constructed to include a His 6 -tag on the C-terminal protein domain. A . Schematic showing the Nuc/Nuc2 chimeric proteins constructed, with Nuc domains colored in teal and Nuc2 domains colored in purple (see Fig. 1A for additional description of domains and processing sites). Chimeras constructed include, from the top down: Nuc control (pMK12), Nuc2 control (pMK13), Nuc signal sequence fused to the Nuc2 active domain (pMK8), Nuc signal sequence and NucB leader fused to the Nuc2 active domain (pMK9), Nuc2 membrane anchor fused to NucA (pMK10) and Nuc2 membrane anchor fused to NucB (pMK11). Each construct was expressed in a S. aureus nuc mutant (strain AH1680) for 15 hr, and culture supernatant was saved and membranes purified. Anti-His immunoblots were performed to detect the presence of C-terminal His 6 -tag on chimeric proteins in culture supernatants ( B ) or membrane ( C ) fractions. FRET activity assays were performed to detect nuclease activity in culture supernatants ( D ) and membrane ( E) fractions. The nuc mutant strain was included as a negative control (called “no plasmid”).$

Journal: PLoS ONE

Article Title: Staphylococcus aureus Nuc2 Is a Functional, Surface-Attached Extracellular Nuclease

doi: 10.1371/journal.pone.0095574

Figure Lengend Snippet: Activity of Nuc/Nuc2 chimeric proteins. Chimeras consisting of combinations of Nuc and Nuc2 N- and C-terminal protein domains were constructed. Each chimera was constructed to include a His 6 -tag on the C-terminal protein domain. A . Schematic showing the Nuc/Nuc2 chimeric proteins constructed, with Nuc domains colored in teal and Nuc2 domains colored in purple (see Fig. 1A for additional description of domains and processing sites). Chimeras constructed include, from the top down: Nuc control (pMK12), Nuc2 control (pMK13), Nuc signal sequence fused to the Nuc2 active domain (pMK8), Nuc signal sequence and NucB leader fused to the Nuc2 active domain (pMK9), Nuc2 membrane anchor fused to NucA (pMK10) and Nuc2 membrane anchor fused to NucB (pMK11). Each construct was expressed in a S. aureus nuc mutant (strain AH1680) for 15 hr, and culture supernatant was saved and membranes purified. Anti-His immunoblots were performed to detect the presence of C-terminal His 6 -tag on chimeric proteins in culture supernatants ( B ) or membrane ( C ) fractions. FRET activity assays were performed to detect nuclease activity in culture supernatants ( D ) and membrane ( E) fractions. The nuc mutant strain was included as a negative control (called “no plasmid”).

Article Snippet: FRET activity assays Nuc enzyme was purchased from Worthington Biochemical (Lakewood, NJ).

Techniques: Activity Assay, Construct, Sequencing, Mutagenesis, Purification, Western Blot, Negative Control, Plasmid Preparation

Nuc2 is expressed at low levels during growth. A . Monitoring changes in fluorescence of a P nuc2 -sGFP transcriptional reporter over time (open circles) in comparison to growth (black squares). Dotted line indicates level of background fluorescence of growth media. B . Changes in surface Nuc2 activity (open circles) present in a S. aureus USA300 LAC nuc mutant over time as measured by whole-cell FRET assay.

Journal: PLoS ONE

Article Title: Staphylococcus aureus Nuc2 Is a Functional, Surface-Attached Extracellular Nuclease

doi: 10.1371/journal.pone.0095574

Figure Lengend Snippet: Nuc2 is expressed at low levels during growth. A . Monitoring changes in fluorescence of a P nuc2 -sGFP transcriptional reporter over time (open circles) in comparison to growth (black squares). Dotted line indicates level of background fluorescence of growth media. B . Changes in surface Nuc2 activity (open circles) present in a S. aureus USA300 LAC nuc mutant over time as measured by whole-cell FRET assay.

Article Snippet: FRET activity assays Nuc enzyme was purchased from Worthington Biochemical (Lakewood, NJ).

Techniques: Fluorescence, Activity Assay, Mutagenesis

Nuc2 activity can be measured at the cell surface. A . Whole-cell FRET activity assay measuring Nuc2 surface function with UAMS-1 WT, nuc2 , nuc and nuc nuc2 double mutants. B . Cell surface nuclease activity in USA300 strain LAC WT, nuc2 , nuc and nuc nuc2 double mutants. Statistical significance (*p

Journal: PLoS ONE

Article Title: Staphylococcus aureus Nuc2 Is a Functional, Surface-Attached Extracellular Nuclease

doi: 10.1371/journal.pone.0095574

Figure Lengend Snippet: Nuc2 activity can be measured at the cell surface. A . Whole-cell FRET activity assay measuring Nuc2 surface function with UAMS-1 WT, nuc2 , nuc and nuc nuc2 double mutants. B . Cell surface nuclease activity in USA300 strain LAC WT, nuc2 , nuc and nuc nuc2 double mutants. Statistical significance (*p

Article Snippet: FRET activity assays Nuc enzyme was purchased from Worthington Biochemical (Lakewood, NJ).

Techniques: Activity Assay