function-blocking antibody to integrin αvβ3 Search Results


function-blocking antibody to integrin αvβ3  (Merck KGaA)
90
Merck KGaA function-blocking antibody to integrin αvβ3
Function Blocking Antibody To Integrin αvβ3, 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
https://www.bioz.com/result/function-blocking antibody to integrin αvβ3/product/Merck KGaA
Average 90 stars, based on 1 article reviews
function-blocking antibody to integrin αvβ3 - by Bioz Stars, 2026-03
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functional blocking integrin-αvβ3 23c6  (Millipore)
90
Millipore functional blocking integrin-αvβ3 23c6
(A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and <t>integrin-αVβ3</t> (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.
Functional Blocking Integrin αvβ3 23c6, 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
https://www.bioz.com/result/functional blocking integrin-αvβ3 23c6/product/Millipore
Average 90 stars, based on 1 article reviews
functional blocking integrin-αvβ3 23c6 - by Bioz Stars, 2026-03
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function-blocking antibody specific for αvβ3 integrin lm609  (Millipore)
90
Millipore function-blocking antibody specific for αvβ3 integrin lm609
(A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and <t>integrin-αVβ3</t> (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.
Function Blocking Antibody Specific For αvβ3 Integrin Lm609, 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
https://www.bioz.com/result/function-blocking antibody specific for αvβ3 integrin lm609/product/Millipore
Average 90 stars, based on 1 article reviews
function-blocking antibody specific for αvβ3 integrin lm609 - by Bioz Stars, 2026-03
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function blocking antibodies α5 (mab1956, p1d6  (Millipore)
90
Millipore function blocking antibodies α5 (mab1956, p1d6
(A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and <t>integrin-αVβ3</t> (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.
Function Blocking Antibodies α5 (Mab1956, P1d6, 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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Average 90 stars, based on 1 article reviews
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mouse β3 function-blocking antibody 2c9.g2  (Becton Dickinson)
90
Becton Dickinson mouse β3 function-blocking antibody 2c9.g2
(A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and <t>integrin-αVβ3</t> (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.
Mouse β3 Function Blocking Antibody 2c9.G2, supplied by Becton Dickinson, 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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rat αvβ3 function-blocking β3 antibody f11  (Becton Dickinson)
90
Becton Dickinson rat αvβ3 function-blocking β3 antibody f11
(A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and <t>integrin-αVβ3</t> (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.
Rat αvβ3 Function Blocking β3 Antibody F11, supplied by Becton Dickinson, 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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Average 90 stars, based on 1 article reviews
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function-blocking antibodies against β1 integrin  (Millipore)
90
Millipore function-blocking antibodies against β1 integrin
(A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and <t>integrin-αVβ3</t> (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.
Function Blocking Antibodies Against β1 Integrin, 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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function-blocking antibodies against β1 integrin - by Bioz Stars, 2026-03
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p4c10 (anti-β1  (R&D Systems)
90
R&D Systems p4c10 (anti-β1
(A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and <t>integrin-αVβ3</t> (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.
P4c10 (Anti β1, supplied by R&D Systems, 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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non-function-blocking antibody to αv  (Biacore)
90
Biacore non-function-blocking antibody to αv
(A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and <t>integrin-αVβ3</t> (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.
Non Function Blocking Antibody To αv, supplied by Biacore, 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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lm609 (anti-αvβ3  (R&D Systems)
90
R&D Systems lm609 (anti-αvβ3
(A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and <t>integrin-αVβ3</t> (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.
Lm609 (Anti αvβ3, supplied by R&D Systems, 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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αvβ3 (mab1976  (Millipore)
90
Millipore αvβ3 (mab1976
(A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and <t>integrin-αVβ3</t> (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.
αvβ3 (Mab1976, 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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antibodies against kcc1  (Millipore)
90
Millipore antibodies against kcc1
(A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and <t>integrin-αVβ3</t> (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.
Antibodies Against Kcc1, 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
https://www.bioz.com/result/antibodies against kcc1/product/Millipore
Average 90 stars, based on 1 article reviews
antibodies against kcc1 - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier

Image Search Results


(A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and integrin-αVβ3 (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.

Journal:

Article Title: MMP-2 Alters VEGF Expression via ?V?3 Integrin-Mediated PI3K/AKT Signaling in A549 Lung Cancer Cells

doi: 10.1002/ijc.25134

Figure Lengend Snippet: (A) A549 cells were plated in 8-well chamber slides and infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h. Immunocytochemistry was performed for co-localization (yellow) of MMP-2 (green) and integrin-αVβ3 (Red) using specific antibodies. (B) A549 cells were infected with mock or 100 MOI of either Ad-SV or Ad-MMP-2-Si for 48 h, and proteins were immunoprecipitated with an anti-integrin-αVβ3 antibody. Western blot analysis was performed for MMP-2 using immunoprecipitated proteins. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control. (C) After 36 h of Ad-MMP-2-Si infection, A549 cells were incubated with a MMP-2 specific inhibitor (ARP-100; at a concentration of 50 and 100 μM) for 12 h. Proteins were immunoprecipitated with anti-integrin-αVβ3 antibody and performed gelatin zymography and western blot for MMP-2. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV/solvent control. (D) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL) for 24 h. Gelatin zymography and western blot analysis was performed for MMP-2 from immunoprecipitated protein samples with an anti-integrin-αVβ3 antibody. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of MMP-2 protein were normalized to protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV control; **p<0.01 significant difference from Ad-MMP-2-Si infection. (E) After 24 h of Ad-MMP-2-Si infection, A549 cells were incubated with rhMMP-2 (25 ng/mL), non-specific IgG and/or anti-integrin-αVβ3 antibodies for another 24 h. We then performed western blot analyses for PI3K, phosphorylation of AKT and VEGF levels using total lysates. GAPDH served as a loading control. Protein band intensities were quantified by densitometric analysis using ImageJ software (National Institutes of Health). The levels of PI3K, phospho-AKT (Ser-473) and VEGF proteins were normalized to respective protein level in mock infected A549 cells. Columns: mean of triplicate experiments; *p<0.01, significant difference from Ad-SV infected control; **p<0.05 significant difference from Ad-SV plus integrin-αVβ3 blocking antibody treatment.

Article Snippet: We used antibodies specific for MMP-2, VEGF (VEGF-A), VEGFR-2, HIF-1α, GAPDH, integrin-αVβ3 (Clone 23C6), MT1MMP, (Santa Cruz Biotechnology, Santa Cruz, CA), PI3K, AKT, phospho-AKT (Ser-473) (Cell Signal Technology, Boston, MA), functional blocking integrin-αVβ3 (Clone 23C6; Cat# CBL544; Millipore Corporation, Temecula, CA) and anti-Human Von-Willebrand Factor (Factor-VIII; Dako North America, Inc, CA), and HRP/Alexa Fluor ® conjugated secondary antibodies (Santa Cruz Biotechnology, Santa Cruz, CA).

Techniques: Infection, Immunocytochemistry, Immunoprecipitation, Western Blot, Software, Incubation, Concentration Assay, Zymography, Blocking Assay

H&E staining was performed as per standard protocol and representative pictures (400 X magnifications) of tumor sections from mock, Ad-SV and Ad-MMP-2-Si-treated mice were shown. Immunohistochemistry was performed for expression and co-localization (yellow) of MMP-2 (green) and integrin-αVβ3 (Red) using specific antibodies. Also showed immunohistochemical analysis for anti-Human Von-Willebrand Factor (Factor-VIII) and VEGF expression using specific antibodies. Data shown are representative fields (400 X magnifications). Also shown is the negative control where the primary antibody was replaced by non-immune serum (inserts).

Journal:

Article Title: MMP-2 Alters VEGF Expression via ?V?3 Integrin-Mediated PI3K/AKT Signaling in A549 Lung Cancer Cells

doi: 10.1002/ijc.25134

Figure Lengend Snippet: H&E staining was performed as per standard protocol and representative pictures (400 X magnifications) of tumor sections from mock, Ad-SV and Ad-MMP-2-Si-treated mice were shown. Immunohistochemistry was performed for expression and co-localization (yellow) of MMP-2 (green) and integrin-αVβ3 (Red) using specific antibodies. Also showed immunohistochemical analysis for anti-Human Von-Willebrand Factor (Factor-VIII) and VEGF expression using specific antibodies. Data shown are representative fields (400 X magnifications). Also shown is the negative control where the primary antibody was replaced by non-immune serum (inserts).

Article Snippet: We used antibodies specific for MMP-2, VEGF (VEGF-A), VEGFR-2, HIF-1α, GAPDH, integrin-αVβ3 (Clone 23C6), MT1MMP, (Santa Cruz Biotechnology, Santa Cruz, CA), PI3K, AKT, phospho-AKT (Ser-473) (Cell Signal Technology, Boston, MA), functional blocking integrin-αVβ3 (Clone 23C6; Cat# CBL544; Millipore Corporation, Temecula, CA) and anti-Human Von-Willebrand Factor (Factor-VIII; Dako North America, Inc, CA), and HRP/Alexa Fluor ® conjugated secondary antibodies (Santa Cruz Biotechnology, Santa Cruz, CA).

Techniques: Staining, Immunohistochemistry, Expressing, Immunohistochemical staining, Negative Control