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GenScript corporation coding sequences of grp protein (signal peptide removed)
Coding Sequences Of Grp Protein (Signal Peptide Removed), supplied by GenScript corporation, 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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GenScript corporation protein d gene with the n-terminal signal sequence removed
Protein D Gene With The N Terminal Signal Sequence Removed, supplied by GenScript corporation, 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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APURES Co Ltd porcine cadaver skin
Porcine Cadaver Skin, supplied by APURES Co Ltd, 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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Stoelting inc straight long pt ground electrode with of its insulation coating removed
Straight Long Pt Ground Electrode With Of Its Insulation Coating Removed, supplied by Stoelting inc, 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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Hamamatsu removed tissue
Removed Tissue, supplied by Hamamatsu, 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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Healthwise Incorporated ovarian cancer: should i have my ovaries removed to prevent ovarian cancer?
Table 2 Basic decision aid data.
Ovarian Cancer: Should I Have My Ovaries Removed To Prevent Ovarian Cancer?, supplied by Healthwise Incorporated, 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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Lifesource Medical Inc human blood with leucocytes removed
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Human Blood With Leucocytes Removed, supplied by Lifesource Medical Inc, 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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Scf Removed, supplied by SeraCare Life Sciences, 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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Merck KGaA aptt reagent filtrates (with contact activators and phospholipids removed)
Effects of <t>activated</t> <t>partial</t> <t>thromboplastin</t> time ( <t>APTT</t> ) reagents, APTT reagent filtrates and contact activators on the activation of nonacog beta pegol (N9‐ GP ) and factor IX ( FIX ) (N9) during the clotting phase of a OS FIX clotting assay. The bars represent relative generation of activated factor IX ( FIX a) activity in the presence of mere buffer (black), APTT reagent (red), APTT reagent filtrate (green), or isolated contact activator (purple). Striped and solid bars show the results obtained with N9 and N9‐ GP , respectively. For each APTT reagent, the generation of FIX a activity was compared to that obtained using N9 in the presence of mere buffer (arbitrarily assigned the value 100%). The APTT reagents are indicated below the graph
Aptt Reagent Filtrates (With Contact Activators And Phospholipids Removed), supplied by Merck KGaA, 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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GenScript corporation paraffin blocks containing lymph node metastases surgically removed from mice 31 days after orthotopic implantation of 2 × 10 6 pc-3m-luc cells
Effects of <t>activated</t> <t>partial</t> <t>thromboplastin</t> time ( <t>APTT</t> ) reagents, APTT reagent filtrates and contact activators on the activation of nonacog beta pegol (N9‐ GP ) and factor IX ( FIX ) (N9) during the clotting phase of a OS FIX clotting assay. The bars represent relative generation of activated factor IX ( FIX a) activity in the presence of mere buffer (black), APTT reagent (red), APTT reagent filtrate (green), or isolated contact activator (purple). Striped and solid bars show the results obtained with N9 and N9‐ GP , respectively. For each APTT reagent, the generation of FIX a activity was compared to that obtained using N9 in the presence of mere buffer (arbitrarily assigned the value 100%). The APTT reagents are indicated below the graph
Paraffin Blocks Containing Lymph Node Metastases Surgically Removed From Mice 31 Days After Orthotopic Implantation Of 2 × 10 6 Pc 3m Luc Cells, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/paraffin blocks containing lymph node metastases surgically removed from mice 31 days after orthotopic implantation of 2 × 10 6 pc-3m-luc cells/product/GenScript corporation
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Hamamatsu surgically removed tumors
Effects of <t>activated</t> <t>partial</t> <t>thromboplastin</t> time ( <t>APTT</t> ) reagents, APTT reagent filtrates and contact activators on the activation of nonacog beta pegol (N9‐ GP ) and factor IX ( FIX ) (N9) during the clotting phase of a OS FIX clotting assay. The bars represent relative generation of activated factor IX ( FIX a) activity in the presence of mere buffer (black), APTT reagent (red), APTT reagent filtrate (green), or isolated contact activator (purple). Striped and solid bars show the results obtained with N9 and N9‐ GP , respectively. For each APTT reagent, the generation of FIX a activity was compared to that obtained using N9 in the presence of mere buffer (arbitrarily assigned the value 100%). The APTT reagents are indicated below the graph
Surgically Removed Tumors, supplied by Hamamatsu, 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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Promega immobilized vitronectin (2 µg/ml, incubated 1 h and then removed
Identification of β3-integrin (ITβ3) as a potential mediator of rapamycin-independent component of mammalian target of rapamycin (Rictor) activation in aged Marfan syndrome (MFS) mice. A: protein-level data for α5-integrin (ITα5), β1-integrin (ITβ1), and αv-integrin (ITαv) identified from the original proteomic analysis along with a targeted reanalysis of data-independent acquisition mass spectrometry files to identify and quantify ITβ3. *mapDIA false discovery rate (FDR) of <1% from the original proteomic analysis; #independent-samples two-tailed t-test, P < 0.05 for Skyline quantification. B: Western blot confirmation of ITβ1 [n = 4, wild-type (WT) and MFS] and ITβ3 (n = 3, WT and MFS) expression in the aorta of aged mice, with integrin signals normalized to β-tubulin to account for loading differences. #Independent-samples two-tailed t-test, P < 0.05; n.s., not significant. C: quantification of fibronectin and <t>vitronectin</t> expression from original proteomics analysis. Statistics were performed in mapDIA software. *FDR < 1%. D: immunofluorescence analysis of vitronectin and fibronectin expression and localization in ×20 magnification images of the aorta of aged WT (n = 3) and MFS (n = 4) mice [blue, DAPI cell nuclei; red, vitronectin (Vn); green, fibronectin (Fn)]. Quantification of mean intensity for each marker is shown at the right. Independent-samples t-test P values are given on each comparison panel.
Immobilized Vitronectin (2 µg/Ml, Incubated 1 H And Then Removed, supplied by Promega, 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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Image Search Results


Table 2 Basic decision aid data.

Journal: Geburtshilfe und Frauenheilkunde

Article Title: Decision Aids for Preventive Treatment Alternatives for BRCA1/2 Mutation Carriers: a Systematic Review

doi: 10.1055/a-1326-1792

Figure Lengend Snippet: Table 2 Basic decision aid data.

Article Snippet: Ovarian Cancer: Should I Have My Ovaries Removed to Prevent Ovarian Cancer? , Healthwise , 2019 , USA , webbasiert , Frauen mit erhöhtem EK-Risiko (BRCA1/2-Mutationsträgerinnen, familiäre Häufung von EK, Lynch-Syndrom) , EK-F (CA-125-Testung, vaginale Sonografie), RR-O, Nutzung oraler Kontrazeptiva.

Techniques: Mutagenesis, Activity Assay, Ligation

Tab. 2 Basisdaten der Entscheidungshilfen.

Journal: Geburtshilfe und Frauenheilkunde

Article Title: Decision Aids for Preventive Treatment Alternatives for BRCA1/2 Mutation Carriers: a Systematic Review

doi: 10.1055/a-1326-1792

Figure Lengend Snippet: Tab. 2 Basisdaten der Entscheidungshilfen.

Article Snippet: Ovarian Cancer: Should I Have My Ovaries Removed to Prevent Ovarian Cancer? , Healthwise , 2019 , USA , webbasiert , Frauen mit erhöhtem EK-Risiko (BRCA1/2-Mutationsträgerinnen, familiäre Häufung von EK, Lynch-Syndrom) , EK-F (CA-125-Testung, vaginale Sonografie), RR-O, Nutzung oraler Kontrazeptiva.

Techniques: Mutagenesis

Effects of activated partial thromboplastin time ( APTT ) reagents, APTT reagent filtrates and contact activators on the activation of nonacog beta pegol (N9‐ GP ) and factor IX ( FIX ) (N9) during the clotting phase of a OS FIX clotting assay. The bars represent relative generation of activated factor IX ( FIX a) activity in the presence of mere buffer (black), APTT reagent (red), APTT reagent filtrate (green), or isolated contact activator (purple). Striped and solid bars show the results obtained with N9 and N9‐ GP , respectively. For each APTT reagent, the generation of FIX a activity was compared to that obtained using N9 in the presence of mere buffer (arbitrarily assigned the value 100%). The APTT reagents are indicated below the graph

Journal: Research and Practice in Thrombosis and Haemostasis

Article Title: Underestimation of N‐glyco PEG ylated factor IX one‐stage clotting activity owing to contact activator‐impaired activation

doi: 10.1002/rth2.12046

Figure Lengend Snippet: Effects of activated partial thromboplastin time ( APTT ) reagents, APTT reagent filtrates and contact activators on the activation of nonacog beta pegol (N9‐ GP ) and factor IX ( FIX ) (N9) during the clotting phase of a OS FIX clotting assay. The bars represent relative generation of activated factor IX ( FIX a) activity in the presence of mere buffer (black), APTT reagent (red), APTT reagent filtrate (green), or isolated contact activator (purple). Striped and solid bars show the results obtained with N9 and N9‐ GP , respectively. For each APTT reagent, the generation of FIX a activity was compared to that obtained using N9 in the presence of mere buffer (arbitrarily assigned the value 100%). The APTT reagents are indicated below the graph

Article Snippet: APTT reagent filtrates (with contact activators and phospholipids removed) were prepared by passage through centrifugal filters (Amicon Ultra, Ultracel) from Merck Millipore (Carrigtwohill, Ireland) with a molecular mass cut‐off of 10 or 100 kDa at 14 000 × g for 15 minutes.

Techniques: Activation Assay, Coagulation, Activity Assay, Isolation

Effects of activated partial thromboplastin time ( APTT ) reagents, APTT reagent filtrates and contact activators on activated factor XI ( FXI a) amidolytic activity. Each bar triplet represents relative FXI a activity in the presence of APTT reagent (gray), APTT reagent filtrate (white) or isolated contact activator (black), with the FXI a activity when instead using assay buffer arbitrarily set to 100% (outer left bar). The APTT reagents are indicated below the graph

Journal: Research and Practice in Thrombosis and Haemostasis

Article Title: Underestimation of N‐glyco PEG ylated factor IX one‐stage clotting activity owing to contact activator‐impaired activation

doi: 10.1002/rth2.12046

Figure Lengend Snippet: Effects of activated partial thromboplastin time ( APTT ) reagents, APTT reagent filtrates and contact activators on activated factor XI ( FXI a) amidolytic activity. Each bar triplet represents relative FXI a activity in the presence of APTT reagent (gray), APTT reagent filtrate (white) or isolated contact activator (black), with the FXI a activity when instead using assay buffer arbitrarily set to 100% (outer left bar). The APTT reagents are indicated below the graph

Article Snippet: APTT reagent filtrates (with contact activators and phospholipids removed) were prepared by passage through centrifugal filters (Amicon Ultra, Ultracel) from Merck Millipore (Carrigtwohill, Ireland) with a molecular mass cut‐off of 10 or 100 kDa at 14 000 × g for 15 minutes.

Techniques: Activity Assay, Isolation

Identification of β3-integrin (ITβ3) as a potential mediator of rapamycin-independent component of mammalian target of rapamycin (Rictor) activation in aged Marfan syndrome (MFS) mice. A: protein-level data for α5-integrin (ITα5), β1-integrin (ITβ1), and αv-integrin (ITαv) identified from the original proteomic analysis along with a targeted reanalysis of data-independent acquisition mass spectrometry files to identify and quantify ITβ3. *mapDIA false discovery rate (FDR) of <1% from the original proteomic analysis; #independent-samples two-tailed t-test, P < 0.05 for Skyline quantification. B: Western blot confirmation of ITβ1 [n = 4, wild-type (WT) and MFS] and ITβ3 (n = 3, WT and MFS) expression in the aorta of aged mice, with integrin signals normalized to β-tubulin to account for loading differences. #Independent-samples two-tailed t-test, P < 0.05; n.s., not significant. C: quantification of fibronectin and vitronectin expression from original proteomics analysis. Statistics were performed in mapDIA software. *FDR < 1%. D: immunofluorescence analysis of vitronectin and fibronectin expression and localization in ×20 magnification images of the aorta of aged WT (n = 3) and MFS (n = 4) mice [blue, DAPI cell nuclei; red, vitronectin (Vn); green, fibronectin (Fn)]. Quantification of mean intensity for each marker is shown at the right. Independent-samples t-test P values are given on each comparison panel.

Journal: American Journal of Physiology - Heart and Circulatory Physiology

Article Title: Proteomics reveals Rictor as a noncanonical TGF-β signaling target during aneurysm progression in Marfan mice

doi: 10.1152/ajpheart.00089.2018

Figure Lengend Snippet: Identification of β3-integrin (ITβ3) as a potential mediator of rapamycin-independent component of mammalian target of rapamycin (Rictor) activation in aged Marfan syndrome (MFS) mice. A: protein-level data for α5-integrin (ITα5), β1-integrin (ITβ1), and αv-integrin (ITαv) identified from the original proteomic analysis along with a targeted reanalysis of data-independent acquisition mass spectrometry files to identify and quantify ITβ3. *mapDIA false discovery rate (FDR) of <1% from the original proteomic analysis; #independent-samples two-tailed t-test, P < 0.05 for Skyline quantification. B: Western blot confirmation of ITβ1 [n = 4, wild-type (WT) and MFS] and ITβ3 (n = 3, WT and MFS) expression in the aorta of aged mice, with integrin signals normalized to β-tubulin to account for loading differences. #Independent-samples two-tailed t-test, P < 0.05; n.s., not significant. C: quantification of fibronectin and vitronectin expression from original proteomics analysis. Statistics were performed in mapDIA software. *FDR < 1%. D: immunofluorescence analysis of vitronectin and fibronectin expression and localization in ×20 magnification images of the aorta of aged WT (n = 3) and MFS (n = 4) mice [blue, DAPI cell nuclei; red, vitronectin (Vn); green, fibronectin (Fn)]. Quantification of mean intensity for each marker is shown at the right. Independent-samples t-test P values are given on each comparison panel.

Article Snippet: Cells were plated on immobilized vitronectin (2 µg/ml, incubated 1 h and then removed, Promega, Madison, WI)-coated six-well plates at a density of 10 6 cells/well in complete DMEM (5% FBS).

Techniques: Activation Assay, Mass Spectrometry, Two Tailed Test, Western Blot, Expressing, Software, Immunofluorescence, Marker

Roles of vitronectin and β3-integrin (ITβ3) in mediating transforming growth factor (TGF)-β-induced rapamycin-independent component of mammalian target of rapamycin (Rictor) activation. A: confirmation of functional ITβ3 overexpression (ITβ3-OE) in vascular smooth muscle cells (VSMCs). Blots at the top and middle demonstrate ITβ3-green fluorescent protein (GFP) fusion protein expression (125 kDa) as well as light native ITβ3 expression (100 kDa) that was only detectable with higher exposure of blot membrane. The blot at the bottom shows β-tubulin loading control. The image on the right shows GFP-ITβ3 expression localized to the perinuclear region and focal adhesions as expected. B–D: Western blot analysis of in vitro effect of TGF-β1 stimulation on Rictor (B), Akt (C), and SMAD2 (D) phosphorylation in VSMCs (n = 5 per group) with or without the ITβ3 inhibitor SB-273005 (100 nM) or ITβ3-OE plated on regular plastic or vitronectin-coated cell culture dishes. Representative blots are shown for the ITβ3 inhibitor (left) and ITβ3-OE (right) data separately. Quantitative data for phospho-Rictor (pRictor) and pAkt are presented as the fold changes of TGF-β-stimulated (Stim) versus unstimulated (Unstim) intensity for each condition after normalization to total Rictor or total Akt protein. Data for pSMAD2 are presented as the ratio of pSMAD2 to total SMAD2 for the TGF-β-stimulated condition only. Phos, phosphorylated; WT, wild type. Groups were compared via one-way ANOVA followed by two-tailed, independent-samples pairwise post hoc t-tests. F-test P values are shown on each plot. *Post hoc comparison P < 0.05.

Journal: American Journal of Physiology - Heart and Circulatory Physiology

Article Title: Proteomics reveals Rictor as a noncanonical TGF-β signaling target during aneurysm progression in Marfan mice

doi: 10.1152/ajpheart.00089.2018

Figure Lengend Snippet: Roles of vitronectin and β3-integrin (ITβ3) in mediating transforming growth factor (TGF)-β-induced rapamycin-independent component of mammalian target of rapamycin (Rictor) activation. A: confirmation of functional ITβ3 overexpression (ITβ3-OE) in vascular smooth muscle cells (VSMCs). Blots at the top and middle demonstrate ITβ3-green fluorescent protein (GFP) fusion protein expression (125 kDa) as well as light native ITβ3 expression (100 kDa) that was only detectable with higher exposure of blot membrane. The blot at the bottom shows β-tubulin loading control. The image on the right shows GFP-ITβ3 expression localized to the perinuclear region and focal adhesions as expected. B–D: Western blot analysis of in vitro effect of TGF-β1 stimulation on Rictor (B), Akt (C), and SMAD2 (D) phosphorylation in VSMCs (n = 5 per group) with or without the ITβ3 inhibitor SB-273005 (100 nM) or ITβ3-OE plated on regular plastic or vitronectin-coated cell culture dishes. Representative blots are shown for the ITβ3 inhibitor (left) and ITβ3-OE (right) data separately. Quantitative data for phospho-Rictor (pRictor) and pAkt are presented as the fold changes of TGF-β-stimulated (Stim) versus unstimulated (Unstim) intensity for each condition after normalization to total Rictor or total Akt protein. Data for pSMAD2 are presented as the ratio of pSMAD2 to total SMAD2 for the TGF-β-stimulated condition only. Phos, phosphorylated; WT, wild type. Groups were compared via one-way ANOVA followed by two-tailed, independent-samples pairwise post hoc t-tests. F-test P values are shown on each plot. *Post hoc comparison P < 0.05.

Article Snippet: Cells were plated on immobilized vitronectin (2 µg/ml, incubated 1 h and then removed, Promega, Madison, WI)-coated six-well plates at a density of 10 6 cells/well in complete DMEM (5% FBS).

Techniques: Activation Assay, Functional Assay, Over Expression, Expressing, Western Blot, In Vitro, Cell Culture, Two Tailed Test

Effect of β3-integrin (ITβ3) and vitronectin on metabolic and migration-proliferation vascular smooth muscle cell (VSMC) physiology. A: assessment of in vitro proliferation and migration by scratch assay of VSMCs under wild-type (WT), ITβ3-overexpressing (ITβ3-OE), and ITβ3 inhibition (Inhib) conditions (n = 3 per group). Quantification is reported as the percent cell-occupied area in scratch at 16 h relative to the cell-occupied area at 0-h transforming growth factor (TGF)-β stimulation. T, time. B: quantification of mitochondrial respiration in vitro in WT (line graph on the top left and box plots on the left side of each panel below) and ITβ3-OE (line graph on the top right and box plots on the right side of each panel below) VSMCs after 48 h of serum starvation in the presence or absence of TGF-β1 (5 ng/ml). The overall oxygen consumption rate (OCR) was measured using the Seahorse assay. Antimy./roten., antimycin-rotenone; ns, not significant. Groups were compared using two-tailed, independent-samples t-test. *P < 0.05; ^P < 0.05 relative to the WT-unstimulated condition; #P < 0.05 relative to the WT-TGF-β-stimulated condition.

Journal: American Journal of Physiology - Heart and Circulatory Physiology

Article Title: Proteomics reveals Rictor as a noncanonical TGF-β signaling target during aneurysm progression in Marfan mice

doi: 10.1152/ajpheart.00089.2018

Figure Lengend Snippet: Effect of β3-integrin (ITβ3) and vitronectin on metabolic and migration-proliferation vascular smooth muscle cell (VSMC) physiology. A: assessment of in vitro proliferation and migration by scratch assay of VSMCs under wild-type (WT), ITβ3-overexpressing (ITβ3-OE), and ITβ3 inhibition (Inhib) conditions (n = 3 per group). Quantification is reported as the percent cell-occupied area in scratch at 16 h relative to the cell-occupied area at 0-h transforming growth factor (TGF)-β stimulation. T, time. B: quantification of mitochondrial respiration in vitro in WT (line graph on the top left and box plots on the left side of each panel below) and ITβ3-OE (line graph on the top right and box plots on the right side of each panel below) VSMCs after 48 h of serum starvation in the presence or absence of TGF-β1 (5 ng/ml). The overall oxygen consumption rate (OCR) was measured using the Seahorse assay. Antimy./roten., antimycin-rotenone; ns, not significant. Groups were compared using two-tailed, independent-samples t-test. *P < 0.05; ^P < 0.05 relative to the WT-unstimulated condition; #P < 0.05 relative to the WT-TGF-β-stimulated condition.

Article Snippet: Cells were plated on immobilized vitronectin (2 µg/ml, incubated 1 h and then removed, Promega, Madison, WI)-coated six-well plates at a density of 10 6 cells/well in complete DMEM (5% FBS).

Techniques: Migration, In Vitro, Wound Healing Assay, Inhibition, Two Tailed Test