Review

mouse anti integrin β 1 mab (Santa Cruz Biotechnology)

Santa Cruz Biotechnology is a verified supplier

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

Santa Cruz Biotechnology mouse anti integrin β 1 mab

EVs from GT16 and CV3 were analyzed by MS. The abundance of proteins was compared after normalization based on the total peptide amount according to the human database of Discoverer 2.4. Perseus analysis was performed after focusing on Master Protein, removing contamination, and taking higher than PSMs 4. In the scatter plot, the X-axis represents the log2-transformed normalized abundance of CV3-derived EVs, while the Y-axis represents the log2-transformed normalized abundance of GT16-derived EVs. The plot includes fold change lines at ±2 log2 unit. These lines indicate a 4-fold increase (+2 log2 unit) or a 0.25-fold decrease (−2 log2 unit) in the expression level of GT16-derived EVs relative to CV3-derived EVs. <t>Integrin</t> binding proteins are marked by red circles based on the GO term. Integrin isoforms are marked by blue dots. Other identified proteins are indicated by gray circles.

Mouse Anti Integrin β 1 Mab, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 884 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+integrin+%CE%B2+1+mab/Integrin+%CE%B21+Antibody/pmc11641595-176-18-23
Average 96 stars, based on 884 article reviews

mouse anti integrin β 1 mab - by Bioz Stars, 2026-08

96/100 stars

Images

1) Product Images from "Action Mechanisms of Exosomes Derived from GD3/GD2-Positive Glioma Cells in the Regulation of Phenotypes and Intracellular Signaling: Roles of Integrins"

Article Title: Action Mechanisms of Exosomes Derived from GD3/GD2-Positive Glioma Cells in the Regulation of Phenotypes and Intracellular Signaling: Roles of Integrins

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms252312752

Figure Legend Snippet: EVs from GT16 and CV3 were analyzed by MS. The abundance of proteins was compared after normalization based on the total peptide amount according to the human database of Discoverer 2.4. Perseus analysis was performed after focusing on Master Protein, removing contamination, and taking higher than PSMs 4. In the scatter plot, the X-axis represents the log2-transformed normalized abundance of CV3-derived EVs, while the Y-axis represents the log2-transformed normalized abundance of GT16-derived EVs. The plot includes fold change lines at ±2 log2 unit. These lines indicate a 4-fold increase (+2 log2 unit) or a 0.25-fold decrease (−2 log2 unit) in the expression level of GT16-derived EVs relative to CV3-derived EVs. Integrin binding proteins are marked by red circles based on the GO term. Integrin isoforms are marked by blue dots. Other identified proteins are indicated by gray circles.

Techniques Used: Transformation Assay, Derivative Assay, Expressing, Binding Assay

The expression of integrins and gangliosides on/in cells and EVs. Cell surface expression of gangliosides, GD3 and GD2, and that of integrins, β 1, β 2, β 3, β 4, β 5, β 6, β 7, β 8, α 2, α 3, α 4, α 5, α 6, and α v , were analyzed by flow cytometry. Anti-GD3 mAb (R24), anti-GD2 mAb (220-51), anti-integrin β 1 ~β 8 Abs, anti-integrin α 2 ~α 6 Abs, or anti-integrin α v Ab were used as primary antibodies, and FITC-labeled secondary antibodies were used ( A ). The expression levels of integrin β 1, α 3, and α v were analyzed in both GD3/GD2(+) and (-) cell-derived EVs by Tim4-bead flow cytometry ( B ). Red lines are results with individual mAbs, and black lines are of negative controls. The expression of integrin β 1 and α 3 was observed in GT16 and CV2 cells and also in EVs derived from them by IB using lysates (1 μg) of both cells and EVs. Anti-integrin β 1 Ab and anti-integrin α 3 Ab were used as primary antibodies, and HRP-labelled secondary Ab was used ( Ci ). The intensity of the obtained bands in Ci was measured and plotted ( Cii,Ciii ). Representative results from repeated experiments (at least 3 times) are presented.

Figure Legend Snippet: The expression of integrins and gangliosides on/in cells and EVs. Cell surface expression of gangliosides, GD3 and GD2, and that of integrins, β 1, β 2, β 3, β 4, β 5, β 6, β 7, β 8, α 2, α 3, α 4, α 5, α 6, and α v , were analyzed by flow cytometry. Anti-GD3 mAb (R24), anti-GD2 mAb (220-51), anti-integrin β 1 ~β 8 Abs, anti-integrin α 2 ~α 6 Abs, or anti-integrin α v Ab were used as primary antibodies, and FITC-labeled secondary antibodies were used ( A ). The expression levels of integrin β 1, α 3, and α v were analyzed in both GD3/GD2(+) and (-) cell-derived EVs by Tim4-bead flow cytometry ( B ). Red lines are results with individual mAbs, and black lines are of negative controls. The expression of integrin β 1 and α 3 was observed in GT16 and CV2 cells and also in EVs derived from them by IB using lysates (1 μg) of both cells and EVs. Anti-integrin β 1 Ab and anti-integrin α 3 Ab were used as primary antibodies, and HRP-labelled secondary Ab was used ( Ci ). The intensity of the obtained bands in Ci was measured and plotted ( Cii,Ciii ). Representative results from repeated experiments (at least 3 times) are presented.

Techniques Used: Expressing, Flow Cytometry, Labeling, Derivative Assay

Colocalization of GD3 and/or GD2 with integrin β 1 on the cell surface. GD3/GD2(+) GT16 and GD3/GD2(-) CV2 cells (2 × 10 4 ) were seeded on collagen-I-pre-coated glass-bottom dishes and fixed on the bottom of the dish with 4% paraformaldehyde at 70 to 80% confluency. The colocalization of GD3 and integrin β 1 was analyzed by staining with two kinds of primary antibodies, i.e., mouse anti-GD3 mAb (1:100) and rabbit anti-integrin β 1 Ab (1:100), and then by the individual secondary antibodies, Alexa 568-conjugated goat anti-mouse IgG Ab (red) (1:100) and Alexa 488-conjugated goat anti-rabbit IgG (H+L) Ab (1:100) (green), respectively, under a confocal microscope (FLUOVIEW FV10i, Olympus, Tokyo, Japan). ( A ). In the case of the colocalization of GD2 and integrin β 1 on the cell surface, mouse anti-GD2 mAb (1:100) was used with rabbit anti-integrin β 1 Ab (1:100) as primary Abs, and the secondary Abs were as mentioned above ( B ).

Figure Legend Snippet: Colocalization of GD3 and/or GD2 with integrin β 1 on the cell surface. GD3/GD2(+) GT16 and GD3/GD2(-) CV2 cells (2 × 10 4 ) were seeded on collagen-I-pre-coated glass-bottom dishes and fixed on the bottom of the dish with 4% paraformaldehyde at 70 to 80% confluency. The colocalization of GD3 and integrin β 1 was analyzed by staining with two kinds of primary antibodies, i.e., mouse anti-GD3 mAb (1:100) and rabbit anti-integrin β 1 Ab (1:100), and then by the individual secondary antibodies, Alexa 568-conjugated goat anti-mouse IgG Ab (red) (1:100) and Alexa 488-conjugated goat anti-rabbit IgG (H+L) Ab (1:100) (green), respectively, under a confocal microscope (FLUOVIEW FV10i, Olympus, Tokyo, Japan). ( A ). In the case of the colocalization of GD2 and integrin β 1 on the cell surface, mouse anti-GD2 mAb (1:100) was used with rabbit anti-integrin β 1 Ab (1:100) as primary Abs, and the secondary Abs were as mentioned above ( B ).

Techniques Used: Staining, Microscopy

The close localization of GD3 and/or GD2 with integrin β 1 on EVs as analyzed by double immunostaining. Fresh exosomes (3 μg/200 μL) were added on Tim4-Fc-coated glass-bottom dishes for 30 min at RT. After washing, the bound exosomes were fixed on the bottom of the dish with 4% paraformaldehyde. Fixed exosomes were incubated with primary antibodies (mouse anti-GD3 mAb (1:100) and rabbit anti-integrin β 1 Ab (1:100)) and secondary Abs (Alexa 568-conjugated goat anti-mouse IgG Abs (red) (1:100) and/or Alexa 488-conjugated goat anti-rabbit IgG (H+L) Abs (green) (1:100)) and finally analyzed with a confocal microscope, where the yellow color of the overlapping image indicates the close localization of GD3 and integrin β 1 on GT16-derived EVs ( A upper ) but not on CV2-derived EVs ( A lower ). Colocalization between GD2 and integrin β 1 was examined on EVs using primary antibodies, mouse anti-GD2 mAbs (1:100) and rabbit anti-integrin β 1 Abs (1:100), and the proper secondary Abs as mentioned above. The yellow color of the confocal imaging means close localization between GD2 and integrin β 1 on GT16 cell-derived EVs ( B upper ), but not on CV2-derived EVs ( B lower ).

Figure Legend Snippet: The close localization of GD3 and/or GD2 with integrin β 1 on EVs as analyzed by double immunostaining. Fresh exosomes (3 μg/200 μL) were added on Tim4-Fc-coated glass-bottom dishes for 30 min at RT. After washing, the bound exosomes were fixed on the bottom of the dish with 4% paraformaldehyde. Fixed exosomes were incubated with primary antibodies (mouse anti-GD3 mAb (1:100) and rabbit anti-integrin β 1 Ab (1:100)) and secondary Abs (Alexa 568-conjugated goat anti-mouse IgG Abs (red) (1:100) and/or Alexa 488-conjugated goat anti-rabbit IgG (H+L) Abs (green) (1:100)) and finally analyzed with a confocal microscope, where the yellow color of the overlapping image indicates the close localization of GD3 and integrin β 1 on GT16-derived EVs ( A upper ) but not on CV2-derived EVs ( A lower ). Colocalization between GD2 and integrin β 1 was examined on EVs using primary antibodies, mouse anti-GD2 mAbs (1:100) and rabbit anti-integrin β 1 Abs (1:100), and the proper secondary Abs as mentioned above. The yellow color of the confocal imaging means close localization between GD2 and integrin β 1 on GT16 cell-derived EVs ( B upper ), but not on CV2-derived EVs ( B lower ).

Techniques Used: Double Immunostaining, Incubation, Microscopy, Derivative Assay, Imaging

Molecular clustering of gangliosides and integrin β 1 . ( A ) The association of GD3 and integrin β 1 and that of GD2 and integrin β 1 on cells was analyzed by IP with anti-integrin β 1 Ab and subsequent IB with anti-GD3 mAb or anti-GD2 mAb as well as anti-integrin β 1 Ab. ( B ) The molecular clustering between GD3 and integrin β 1 and between GD2 and integrin β 1 in EVs derived from them was examined by IP followed by IB as mentioned above.

Figure Legend Snippet: Molecular clustering of gangliosides and integrin β 1 . ( A ) The association of GD3 and integrin β 1 and that of GD2 and integrin β 1 on cells was analyzed by IP with anti-integrin β 1 Ab and subsequent IB with anti-GD3 mAb or anti-GD2 mAb as well as anti-integrin β 1 Ab. ( B ) The molecular clustering between GD3 and integrin β 1 and between GD2 and integrin β 1 in EVs derived from them was examined by IP followed by IB as mentioned above.

Techniques Used: Derivative Assay

Effects of anti-integrin Abs and anti-GD3/GD2 mAbs on EV function. ( A ) The adhesion activity of GD3/GD2(-) cells to collagen-I examined by RT-CES. Cells (1 × 10 4 ) were cultured in collagen-I-precoated wells containing 100 μL of culture medium and incubated. The data after 24 h ( A ) and 9 h ( B ) of cell incubation are shown. GT16 cell-derived EVs enhanced the adhesion activity of CV2 cells ( A , B ), but anti-integrin β 1 Ab remarkably suppressed the adhesion activity of CV2 cells ( A ). Anti-GD3 mAb and/or anti-GD2 mAb also significantly suppressed the action of EVs to the adhesion of CV2 cells when either one of these anti-ganglioside mAbs was added to CV2 cells together with GD3/GD2(+) cell-derived EVs ( B ). The data until 24 h of incubation ( A ) and until 9 h of incubation ( B ) were analyzed with an unpaired Student’s two-tailed t test. Not significant (NS) p > 0.05, and *** p < 0.001. The mean values ± SD (n = 3) were plotted for each time point.

Figure Legend Snippet: Effects of anti-integrin Abs and anti-GD3/GD2 mAbs on EV function. ( A ) The adhesion activity of GD3/GD2(-) cells to collagen-I examined by RT-CES. Cells (1 × 10 4 ) were cultured in collagen-I-precoated wells containing 100 μL of culture medium and incubated. The data after 24 h ( A ) and 9 h ( B ) of cell incubation are shown. GT16 cell-derived EVs enhanced the adhesion activity of CV2 cells ( A , B ), but anti-integrin β 1 Ab remarkably suppressed the adhesion activity of CV2 cells ( A ). Anti-GD3 mAb and/or anti-GD2 mAb also significantly suppressed the action of EVs to the adhesion of CV2 cells when either one of these anti-ganglioside mAbs was added to CV2 cells together with GD3/GD2(+) cell-derived EVs ( B ). The data until 24 h of incubation ( A ) and until 9 h of incubation ( B ) were analyzed with an unpaired Student’s two-tailed t test. Not significant (NS) p > 0.05, and *** p < 0.001. The mean values ± SD (n = 3) were plotted for each time point.

Techniques Used: Activity Assay, Cell Culture, Incubation, Derivative Assay, Two Tailed Test

Image Search Results

Journal: International Journal of Molecular Sciences

Article Title: Action Mechanisms of Exosomes Derived from GD3/GD2-Positive Glioma Cells in the Regulation of Phenotypes and Intracellular Signaling: Roles of Integrins

doi: 10.3390/ijms252312752

Figure Lengend Snippet: EVs from GT16 and CV3 were analyzed by MS. The abundance of proteins was compared after normalization based on the total peptide amount according to the human database of Discoverer 2.4. Perseus analysis was performed after focusing on Master Protein, removing contamination, and taking higher than PSMs 4. In the scatter plot, the X-axis represents the log2-transformed normalized abundance of CV3-derived EVs, while the Y-axis represents the log2-transformed normalized abundance of GT16-derived EVs. The plot includes fold change lines at ±2 log2 unit. These lines indicate a 4-fold increase (+2 log2 unit) or a 0.25-fold decrease (−2 log2 unit) in the expression level of GT16-derived EVs relative to CV3-derived EVs. Integrin binding proteins are marked by red circles based on the GO term. Integrin isoforms are marked by blue dots. Other identified proteins are indicated by gray circles.

Article Snippet: After removing the insoluble cell debris through repeated centrifugation, the supernatants (cell lysates) were used for immunoprecipitation with mouse anti-integrin β 1 mAb (Santa Cruz Biotechnology) at 4 °C overnight with rotation.

Techniques: Transformation Assay, Derivative Assay, Expressing, Binding Assay

Journal: International Journal of Molecular Sciences

Article Title: Action Mechanisms of Exosomes Derived from GD3/GD2-Positive Glioma Cells in the Regulation of Phenotypes and Intracellular Signaling: Roles of Integrins

doi: 10.3390/ijms252312752

Figure Lengend Snippet: The expression of integrins and gangliosides on/in cells and EVs. Cell surface expression of gangliosides, GD3 and GD2, and that of integrins, β 1, β 2, β 3, β 4, β 5, β 6, β 7, β 8, α 2, α 3, α 4, α 5, α 6, and α v , were analyzed by flow cytometry. Anti-GD3 mAb (R24), anti-GD2 mAb (220-51), anti-integrin β 1 ~β 8 Abs, anti-integrin α 2 ~α 6 Abs, or anti-integrin α v Ab were used as primary antibodies, and FITC-labeled secondary antibodies were used ( A ). The expression levels of integrin β 1, α 3, and α v were analyzed in both GD3/GD2(+) and (-) cell-derived EVs by Tim4-bead flow cytometry ( B ). Red lines are results with individual mAbs, and black lines are of negative controls. The expression of integrin β 1 and α 3 was observed in GT16 and CV2 cells and also in EVs derived from them by IB using lysates (1 μg) of both cells and EVs. Anti-integrin β 1 Ab and anti-integrin α 3 Ab were used as primary antibodies, and HRP-labelled secondary Ab was used ( Ci ). The intensity of the obtained bands in Ci was measured and plotted ( Cii,Ciii ). Representative results from repeated experiments (at least 3 times) are presented.

Techniques: Expressing, Flow Cytometry, Labeling, Derivative Assay

Journal: International Journal of Molecular Sciences

Article Title: Action Mechanisms of Exosomes Derived from GD3/GD2-Positive Glioma Cells in the Regulation of Phenotypes and Intracellular Signaling: Roles of Integrins

doi: 10.3390/ijms252312752

Figure Lengend Snippet: Colocalization of GD3 and/or GD2 with integrin β 1 on the cell surface. GD3/GD2(+) GT16 and GD3/GD2(-) CV2 cells (2 × 10 4 ) were seeded on collagen-I-pre-coated glass-bottom dishes and fixed on the bottom of the dish with 4% paraformaldehyde at 70 to 80% confluency. The colocalization of GD3 and integrin β 1 was analyzed by staining with two kinds of primary antibodies, i.e., mouse anti-GD3 mAb (1:100) and rabbit anti-integrin β 1 Ab (1:100), and then by the individual secondary antibodies, Alexa 568-conjugated goat anti-mouse IgG Ab (red) (1:100) and Alexa 488-conjugated goat anti-rabbit IgG (H+L) Ab (1:100) (green), respectively, under a confocal microscope (FLUOVIEW FV10i, Olympus, Tokyo, Japan). ( A ). In the case of the colocalization of GD2 and integrin β 1 on the cell surface, mouse anti-GD2 mAb (1:100) was used with rabbit anti-integrin β 1 Ab (1:100) as primary Abs, and the secondary Abs were as mentioned above ( B ).

Techniques: Staining, Microscopy

Journal: International Journal of Molecular Sciences

Article Title: Action Mechanisms of Exosomes Derived from GD3/GD2-Positive Glioma Cells in the Regulation of Phenotypes and Intracellular Signaling: Roles of Integrins

doi: 10.3390/ijms252312752

Figure Lengend Snippet: The close localization of GD3 and/or GD2 with integrin β 1 on EVs as analyzed by double immunostaining. Fresh exosomes (3 μg/200 μL) were added on Tim4-Fc-coated glass-bottom dishes for 30 min at RT. After washing, the bound exosomes were fixed on the bottom of the dish with 4% paraformaldehyde. Fixed exosomes were incubated with primary antibodies (mouse anti-GD3 mAb (1:100) and rabbit anti-integrin β 1 Ab (1:100)) and secondary Abs (Alexa 568-conjugated goat anti-mouse IgG Abs (red) (1:100) and/or Alexa 488-conjugated goat anti-rabbit IgG (H+L) Abs (green) (1:100)) and finally analyzed with a confocal microscope, where the yellow color of the overlapping image indicates the close localization of GD3 and integrin β 1 on GT16-derived EVs ( A upper ) but not on CV2-derived EVs ( A lower ). Colocalization between GD2 and integrin β 1 was examined on EVs using primary antibodies, mouse anti-GD2 mAbs (1:100) and rabbit anti-integrin β 1 Abs (1:100), and the proper secondary Abs as mentioned above. The yellow color of the confocal imaging means close localization between GD2 and integrin β 1 on GT16 cell-derived EVs ( B upper ), but not on CV2-derived EVs ( B lower ).

Techniques: Double Immunostaining, Incubation, Microscopy, Derivative Assay, Imaging

Journal: International Journal of Molecular Sciences

Article Title: Action Mechanisms of Exosomes Derived from GD3/GD2-Positive Glioma Cells in the Regulation of Phenotypes and Intracellular Signaling: Roles of Integrins

doi: 10.3390/ijms252312752

Figure Lengend Snippet: Molecular clustering of gangliosides and integrin β 1 . ( A ) The association of GD3 and integrin β 1 and that of GD2 and integrin β 1 on cells was analyzed by IP with anti-integrin β 1 Ab and subsequent IB with anti-GD3 mAb or anti-GD2 mAb as well as anti-integrin β 1 Ab. ( B ) The molecular clustering between GD3 and integrin β 1 and between GD2 and integrin β 1 in EVs derived from them was examined by IP followed by IB as mentioned above.

Techniques: Derivative Assay

Journal: International Journal of Molecular Sciences

Article Title: Action Mechanisms of Exosomes Derived from GD3/GD2-Positive Glioma Cells in the Regulation of Phenotypes and Intracellular Signaling: Roles of Integrins

doi: 10.3390/ijms252312752

Figure Lengend Snippet: Effects of anti-integrin Abs and anti-GD3/GD2 mAbs on EV function. ( A ) The adhesion activity of GD3/GD2(-) cells to collagen-I examined by RT-CES. Cells (1 × 10 4 ) were cultured in collagen-I-precoated wells containing 100 μL of culture medium and incubated. The data after 24 h ( A ) and 9 h ( B ) of cell incubation are shown. GT16 cell-derived EVs enhanced the adhesion activity of CV2 cells ( A , B ), but anti-integrin β 1 Ab remarkably suppressed the adhesion activity of CV2 cells ( A ). Anti-GD3 mAb and/or anti-GD2 mAb also significantly suppressed the action of EVs to the adhesion of CV2 cells when either one of these anti-ganglioside mAbs was added to CV2 cells together with GD3/GD2(+) cell-derived EVs ( B ). The data until 24 h of incubation ( A ) and until 9 h of incubation ( B ) were analyzed with an unpaired Student’s two-tailed t test. Not significant (NS) p > 0.05, and *** p < 0.001. The mean values ± SD (n = 3) were plotted for each time point.

Techniques: Activity Assay, Cell Culture, Incubation, Derivative Assay, Two Tailed Test

Comparative study on protein extractions from T47D cells using 5-different lysis buffers (M1–M5). A) Five sets of cancer cells were cultured for extraction of proteins using different lysis buffers. Phase-contrast microscopic images showing the confluency of cells at different days. Images were taken for d 0 and 2. Original scale bars, 50 µm. B, C) Coomassie blue (B) and (C) silver staining after running the SDS-PAGE gel electrophoresis. D, E) Immunoblot result (D) of protein lysates against GAPDH antibody and their relative intensity (E) of protein bands. F, G) Immunoblot result (F) of protein lysates against integrin β-1 antibody and their relative intensity (G) of protein bands.

Journal: Journal of Biomolecular Techniques : JBT

Article Title: Cytosolic and Transmembrane Protein Extraction Methods of Breast and Ovarian Cancer Cells: A Comparative Study

doi: 10.7171/jbt.18-2903-002

Figure Lengend Snippet: Comparative study on protein extractions from T47D cells using 5-different lysis buffers (M1–M5). A) Five sets of cancer cells were cultured for extraction of proteins using different lysis buffers. Phase-contrast microscopic images showing the confluency of cells at different days. Images were taken for d 0 and 2. Original scale bars, 50 µm. B, C) Coomassie blue (B) and (C) silver staining after running the SDS-PAGE gel electrophoresis. D, E) Immunoblot result (D) of protein lysates against GAPDH antibody and their relative intensity (E) of protein bands. F, G) Immunoblot result (F) of protein lysates against integrin β-1 antibody and their relative intensity (G) of protein bands.

Article Snippet: GAPDH (D4C6R) and integrin β-1 (D2E5) primary antibodies were purchased from Cell Signaling Technology (Danvers, MA, USA).

Techniques: Lysis, Cell Culture, Extraction, Silver Staining, SDS Page, Nucleic Acid Electrophoresis, Western Blot

Comparative study on protein extractions from MDA-MB-231 cells using 5-different lysis buffers (M1–M5). A) Five sets of cancer cells were cultured for extraction of proteins using different lysis buffers. Phase-contrast microscopic images showing the confluency of cells at different days. Images were taken for d 0 and 2. Original scale bars, 50 µm. B, C) Coomassie blue (B) and silver (C) staining after running the SDS-PAGE gel electrophoresis. D, E) Immunoblot result of protein lysates against GAPDH antibody and their relative intensity of protein bands. F, G) Immunoblot result of protein lysates against integrin β-1 antibody and their relative intensity of protein bands.

Journal: Journal of Biomolecular Techniques : JBT

Article Title: Cytosolic and Transmembrane Protein Extraction Methods of Breast and Ovarian Cancer Cells: A Comparative Study

doi: 10.7171/jbt.18-2903-002

Figure Lengend Snippet: Comparative study on protein extractions from MDA-MB-231 cells using 5-different lysis buffers (M1–M5). A) Five sets of cancer cells were cultured for extraction of proteins using different lysis buffers. Phase-contrast microscopic images showing the confluency of cells at different days. Images were taken for d 0 and 2. Original scale bars, 50 µm. B, C) Coomassie blue (B) and silver (C) staining after running the SDS-PAGE gel electrophoresis. D, E) Immunoblot result of protein lysates against GAPDH antibody and their relative intensity of protein bands. F, G) Immunoblot result of protein lysates against integrin β-1 antibody and their relative intensity of protein bands.

Article Snippet: GAPDH (D4C6R) and integrin β-1 (D2E5) primary antibodies were purchased from Cell Signaling Technology (Danvers, MA, USA).

Techniques: Lysis, Cell Culture, Extraction, Staining, SDS Page, Nucleic Acid Electrophoresis, Western Blot

Comparative study on protein extractions from PA-1 cells using 5-different lysis buffers (M1–M5). A) Five sets of cancer cells were cultured for extraction of proteins using different lysis buffers. Phase-contrast microscopic images showing the confluency of cells at different days. Images were taken for d 0 and 2. Original scale bars, 50 µm. B, C) Coomassie blue (B) and silver (C) staining after running the SDS-PAGE gel electrophoresis. D, E) Immunoblot result (D) of protein lysates against GAPDH antibody and their relative intensity (E) of protein bands. F, G) Immunoblot result (F) of protein lysates against integrin β-1 antibody and their relative intensity (G) of protein bands.

Journal: Journal of Biomolecular Techniques : JBT

Article Title: Cytosolic and Transmembrane Protein Extraction Methods of Breast and Ovarian Cancer Cells: A Comparative Study

doi: 10.7171/jbt.18-2903-002

Figure Lengend Snippet: Comparative study on protein extractions from PA-1 cells using 5-different lysis buffers (M1–M5). A) Five sets of cancer cells were cultured for extraction of proteins using different lysis buffers. Phase-contrast microscopic images showing the confluency of cells at different days. Images were taken for d 0 and 2. Original scale bars, 50 µm. B, C) Coomassie blue (B) and silver (C) staining after running the SDS-PAGE gel electrophoresis. D, E) Immunoblot result (D) of protein lysates against GAPDH antibody and their relative intensity (E) of protein bands. F, G) Immunoblot result (F) of protein lysates against integrin β-1 antibody and their relative intensity (G) of protein bands.

Article Snippet: GAPDH (D4C6R) and integrin β-1 (D2E5) primary antibodies were purchased from Cell Signaling Technology (Danvers, MA, USA).

Techniques: Lysis, Cell Culture, Extraction, Staining, SDS Page, Nucleic Acid Electrophoresis, Western Blot

Expression of β1-integrin in various cancer cell lines. (A) Reverse transcription-polymerase chain reaction for β1-integrin mRNA expression. (B) Western blot analysis of β1-integrin expression. (C) Adhesion of MDA-MB-231 and MGC803 cells to FN and PLL. FN, fibronectin; PLL, poly-L-lysine.

Journal: Oncology Letters

Article Title: Anti-metastatic effect of jolkinolide B and the mechanism of activity in breast cancer MDA-MB-231 cells

doi: 10.3892/ol.2015.3310

Figure Lengend Snippet: Expression of β1-integrin in various cancer cell lines. (A) Reverse transcription-polymerase chain reaction for β1-integrin mRNA expression. (B) Western blot analysis of β1-integrin expression. (C) Adhesion of MDA-MB-231 and MGC803 cells to FN and PLL. FN, fibronectin; PLL, poly-L-lysine.

Article Snippet: The membrane was blocked with a solution of 5% nonfat dry milk for 2 h at room temperature, followed by incubation overnight at 4°C with the following primary antibodies: monoclonal mouse anti-human β 1 -integrin (dilution, 1:500; cat. no. 9699S), monoclonal rabbit anti-human FAK (dilution, 1:1,000; cat. no. 13009), monoclonal rabbit anti-human phosphorylated FAK (dilution, 1:1,000; cat. no. 8556), monoclonal rabbit anti-human ERK (dilution, 1:1,000; cat. no. 8201S), monoclonal rabbit anti-human phosphorylated ERK (dilution, 1:1,000; cat. no. 8201S), monoclonal rabbit anti-human Akt (dilution, 1:1,000; cat. no. 8200S), monoclonal rabbit anti-human phosphorylated Akt (p-Akt; dilution, 1:1,000; cat. no. 8200S) and monoclonal rabbit anti-human GAPDH antibody (dilution, 1:5,000; cat. no. 2118S; all purchased from Cell Signaling Technology, Beverly, MA, USA).

Techniques: Expressing, Reverse Transcription, Polymerase Chain Reaction, Western Blot

Effect of jolkinolide B on protein expressions of the β1-integrin/FAK and ERK signaling proteins. (A and B) Effect of jolkinolide B on the expression of the proteins of the β1-integrin/FAK signaling pathway. Cells were treated with 0, 1 and 2 µM jolkinolide B. (A) Proteins were extracted, and the expression of β1-integrin, FAK and p-FAK was then determined by western blot analysis. (B) Densitometric values of protein bands were normalized to those of GAPDH. The data represent the mean ± SD of three independent determinations. *P<0.05 vs. untreated cells. (C and D) The effect of jolkinolide B on the expression of ERK signaling proteins. (C) Expression of the ERK signaling proteins in MDA-MB-231 cells was confirmed by western blot analysis. (D) Quantitated results are presented relative to the control. Densitometric analysis of western blotting was obtained from three independent experiments and is expressed as the mean ± SD. *P<0.05 vs. untreated cells. SD, standard deviation; FAK, focal adhesion kinase; p-FAK, phosphorylated FAK; ERK, extracellular signal-regulated kinase; p-ERK, phosphorylated ERK; p-Akt, phosphorylated Akt.

Journal: Oncology Letters

Article Title: Anti-metastatic effect of jolkinolide B and the mechanism of activity in breast cancer MDA-MB-231 cells

doi: 10.3892/ol.2015.3310

Figure Lengend Snippet: Effect of jolkinolide B on protein expressions of the β1-integrin/FAK and ERK signaling proteins. (A and B) Effect of jolkinolide B on the expression of the proteins of the β1-integrin/FAK signaling pathway. Cells were treated with 0, 1 and 2 µM jolkinolide B. (A) Proteins were extracted, and the expression of β1-integrin, FAK and p-FAK was then determined by western blot analysis. (B) Densitometric values of protein bands were normalized to those of GAPDH. The data represent the mean ± SD of three independent determinations. *P<0.05 vs. untreated cells. (C and D) The effect of jolkinolide B on the expression of ERK signaling proteins. (C) Expression of the ERK signaling proteins in MDA-MB-231 cells was confirmed by western blot analysis. (D) Quantitated results are presented relative to the control. Densitometric analysis of western blotting was obtained from three independent experiments and is expressed as the mean ± SD. *P<0.05 vs. untreated cells. SD, standard deviation; FAK, focal adhesion kinase; p-FAK, phosphorylated FAK; ERK, extracellular signal-regulated kinase; p-ERK, phosphorylated ERK; p-Akt, phosphorylated Akt.

Techniques: Expressing, Western Blot, Control, Standard Deviation

Review

Structured Review

Images

1) Product Images from "Action Mechanisms of Exosomes Derived from GD3/GD2-Positive Glioma Cells in the Regulation of Phenotypes and Intracellular Signaling: Roles of Integrins"

Similar Products

Image Search Results