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A Representative immunoblotting analysis ( n = 3 independent experiments) of phosphorylated EPHA2 and <t>FAK</t> (EPHA2 Y588 and FAK Y397) in A549 <t>(oe</t> <t>GLUD1</t> versus vector). B Representative immunoblotting analysis ( n = 3 independent experiments) of VE-Cadherin protein expression in whole-cell lysates (WCL) and membrane fractions of A549/DTX (si GLUD1 versus siNC; left) and A549 (oe GLUD1 versus vector; right). C Immunofluorescence staining of VE-Cadherin in A549/DTX (si GLUD1 versus siNC; top) and A549 (oe GLUD1 versus vector; bottom), with quantification shown in ( D ), n = 3 biologically independent samples. The average fluorescence intensity of VE-Cadherin on the cell membrane surface was calculated by manually selecting the area using FIJI. E Representative immunoblotting analysis ( n = 3 independent experiments) of VE-Cadherin and GLUD1 in A549 WCL following GLUD1 overexpression and subsequent CDH5 knockdown. F – K Representative images ( F – H ) and quantification ( I – K ) of adhesion ( F , I , n = 4 biologically independent samples), barrier-destruction ( G , J , n = 3 biologically independent samples) and transmigration ( H , K , n = 3 biologically independent samples) for siNC or si GLUD1 -treated A549 cells. Cells in ( F , H ) were counted using Fiji. G fluorescence was quantified using Fiji and normalized to the 30-min value within each experiment. L – O Immunofluorescence analysis of intravasation ( L ) and extravasation ( M ) in A549 cells following GLUD1 overexpression and subsequent CDH5 knockdown. Intravasation was quantified by tumor cells’ average fluorescence intensity in adjacent channels ( N , n = 4 biologically independent samples), while extravasation was measured by ECM-invading cells ( O , n = 3 biologically independent samples). All data were normalized to oe GLUD1 − /si CDH5 − group. All data are represented as mean ± SEM. P values were calculated using two-tailed unpaired Student’s t test D ; one-way ANOVA followed by Dunnett’s multiple-comparisons test ( I , K , N , O ); two-way ANOVA followed by Šídák multiple-comparisons test J . Scale bars: C , G , 20 μm; F , H , 1000 μm. Source data are provided as a Source Data file. For immunoblots, samples within each panel were derived from the same experiment, with separate gels processed in parallel where applicable; detailed gel assignments are provided in the Methods.
Fak, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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A Representative immunoblotting analysis ( n = 3 independent experiments) of phosphorylated EPHA2 and <t>FAK</t> (EPHA2 Y588 and FAK Y397) in A549 <t>(oe</t> <t>GLUD1</t> versus vector). B Representative immunoblotting analysis ( n = 3 independent experiments) of VE-Cadherin protein expression in whole-cell lysates (WCL) and membrane fractions of A549/DTX (si GLUD1 versus siNC; left) and A549 (oe GLUD1 versus vector; right). C Immunofluorescence staining of VE-Cadherin in A549/DTX (si GLUD1 versus siNC; top) and A549 (oe GLUD1 versus vector; bottom), with quantification shown in ( D ), n = 3 biologically independent samples. The average fluorescence intensity of VE-Cadherin on the cell membrane surface was calculated by manually selecting the area using FIJI. E Representative immunoblotting analysis ( n = 3 independent experiments) of VE-Cadherin and GLUD1 in A549 WCL following GLUD1 overexpression and subsequent CDH5 knockdown. F – K Representative images ( F – H ) and quantification ( I – K ) of adhesion ( F , I , n = 4 biologically independent samples), barrier-destruction ( G , J , n = 3 biologically independent samples) and transmigration ( H , K , n = 3 biologically independent samples) for siNC or si GLUD1 -treated A549 cells. Cells in ( F , H ) were counted using Fiji. G fluorescence was quantified using Fiji and normalized to the 30-min value within each experiment. L – O Immunofluorescence analysis of intravasation ( L ) and extravasation ( M ) in A549 cells following GLUD1 overexpression and subsequent CDH5 knockdown. Intravasation was quantified by tumor cells’ average fluorescence intensity in adjacent channels ( N , n = 4 biologically independent samples), while extravasation was measured by ECM-invading cells ( O , n = 3 biologically independent samples). All data were normalized to oe GLUD1 − /si CDH5 − group. All data are represented as mean ± SEM. P values were calculated using two-tailed unpaired Student’s t test D ; one-way ANOVA followed by Dunnett’s multiple-comparisons test ( I , K , N , O ); two-way ANOVA followed by Šídák multiple-comparisons test J . Scale bars: C , G , 20 μm; F , H , 1000 μm. Source data are provided as a Source Data file. For immunoblots, samples within each panel were derived from the same experiment, with separate gels processed in parallel where applicable; detailed gel assignments are provided in the Methods.
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A Representative immunoblotting analysis ( n = 3 independent experiments) of phosphorylated EPHA2 and <t>FAK</t> (EPHA2 Y588 and FAK Y397) in A549 <t>(oe</t> <t>GLUD1</t> versus vector). B Representative immunoblotting analysis ( n = 3 independent experiments) of VE-Cadherin protein expression in whole-cell lysates (WCL) and membrane fractions of A549/DTX (si GLUD1 versus siNC; left) and A549 (oe GLUD1 versus vector; right). C Immunofluorescence staining of VE-Cadherin in A549/DTX (si GLUD1 versus siNC; top) and A549 (oe GLUD1 versus vector; bottom), with quantification shown in ( D ), n = 3 biologically independent samples. The average fluorescence intensity of VE-Cadherin on the cell membrane surface was calculated by manually selecting the area using FIJI. E Representative immunoblotting analysis ( n = 3 independent experiments) of VE-Cadherin and GLUD1 in A549 WCL following GLUD1 overexpression and subsequent CDH5 knockdown. F – K Representative images ( F – H ) and quantification ( I – K ) of adhesion ( F , I , n = 4 biologically independent samples), barrier-destruction ( G , J , n = 3 biologically independent samples) and transmigration ( H , K , n = 3 biologically independent samples) for siNC or si GLUD1 -treated A549 cells. Cells in ( F , H ) were counted using Fiji. G fluorescence was quantified using Fiji and normalized to the 30-min value within each experiment. L – O Immunofluorescence analysis of intravasation ( L ) and extravasation ( M ) in A549 cells following GLUD1 overexpression and subsequent CDH5 knockdown. Intravasation was quantified by tumor cells’ average fluorescence intensity in adjacent channels ( N , n = 4 biologically independent samples), while extravasation was measured by ECM-invading cells ( O , n = 3 biologically independent samples). All data were normalized to oe GLUD1 − /si CDH5 − group. All data are represented as mean ± SEM. P values were calculated using two-tailed unpaired Student’s t test D ; one-way ANOVA followed by Dunnett’s multiple-comparisons test ( I , K , N , O ); two-way ANOVA followed by Šídák multiple-comparisons test J . Scale bars: C , G , 20 μm; F , H , 1000 μm. Source data are provided as a Source Data file. For immunoblots, samples within each panel were derived from the same experiment, with separate gels processed in parallel where applicable; detailed gel assignments are provided in the Methods.
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Immunofluorescence staining of focal adhesion-related markers and cytoskeleton in cells under control and mechanical stimulation conditions. Left (Control group): Immunofluorescence staining shows focal adhesion-associated proteins (green channels). These correspond to integrin β1(A), talin <t>(B),</t> <t>pFAK/FAK</t> (C), paxillin (D), YAP (E), and TAZ (F) in each row. F-actin and FAK are shown in the red channel. The rightmost column of each row displays merged images. These integrate focal adhesion marker signals (green), F-actin (red), and DAPI-stained nuclei (blue). Yellow indicates co-localization of focal adhesion markers and F-actin. Right (After mechanical stimulation group): Immunofluorescence staining displays the same set of focal adhesion-related proteins and F-actin in cells after mechanical stimulation. Merged images are presented in the same format as the control group.
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Immunofluorescence staining of focal adhesion-related markers and cytoskeleton in cells under control and mechanical stimulation conditions. Left (Control group): Immunofluorescence staining shows focal adhesion-associated proteins (green channels). These correspond to integrin β1(A), talin <t>(B),</t> <t>pFAK/FAK</t> (C), paxillin (D), YAP (E), and TAZ (F) in each row. F-actin and FAK are shown in the red channel. The rightmost column of each row displays merged images. These integrate focal adhesion marker signals (green), F-actin (red), and DAPI-stained nuclei (blue). Yellow indicates co-localization of focal adhesion markers and F-actin. Right (After mechanical stimulation group): Immunofluorescence staining displays the same set of focal adhesion-related proteins and F-actin in cells after mechanical stimulation. Merged images are presented in the same format as the control group.
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Immunofluorescence staining of focal adhesion-related markers and cytoskeleton in cells under control and mechanical stimulation conditions. Left (Control group): Immunofluorescence staining shows focal adhesion-associated proteins (green channels). These correspond to integrin β1(A), talin <t>(B),</t> <t>pFAK/FAK</t> (C), paxillin (D), YAP (E), and TAZ (F) in each row. F-actin and FAK are shown in the red channel. The rightmost column of each row displays merged images. These integrate focal adhesion marker signals (green), F-actin (red), and DAPI-stained nuclei (blue). Yellow indicates co-localization of focal adhesion markers and F-actin. Right (After mechanical stimulation group): Immunofluorescence staining displays the same set of focal adhesion-related proteins and F-actin in cells after mechanical stimulation. Merged images are presented in the same format as the control group.
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Immunofluorescence staining of focal adhesion-related markers and cytoskeleton in cells under control and mechanical stimulation conditions. Left (Control group): Immunofluorescence staining shows focal adhesion-associated proteins (green channels). These correspond to integrin β1(A), talin <t>(B),</t> <t>pFAK/FAK</t> (C), paxillin (D), YAP (E), and TAZ (F) in each row. F-actin and FAK are shown in the red channel. The rightmost column of each row displays merged images. These integrate focal adhesion marker signals (green), F-actin (red), and DAPI-stained nuclei (blue). Yellow indicates co-localization of focal adhesion markers and F-actin. Right (After mechanical stimulation group): Immunofluorescence staining displays the same set of focal adhesion-related proteins and F-actin in cells after mechanical stimulation. Merged images are presented in the same format as the control group.
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Immunofluorescence staining of focal adhesion-related markers and cytoskeleton in cells under control and mechanical stimulation conditions. Left (Control group): Immunofluorescence staining shows focal adhesion-associated proteins (green channels). These correspond to integrin β1(A), talin <t>(B),</t> <t>pFAK/FAK</t> (C), paxillin (D), YAP (E), and TAZ (F) in each row. F-actin and FAK are shown in the red channel. The rightmost column of each row displays merged images. These integrate focal adhesion marker signals (green), F-actin (red), and DAPI-stained nuclei (blue). Yellow indicates co-localization of focal adhesion markers and F-actin. Right (After mechanical stimulation group): Immunofluorescence staining displays the same set of focal adhesion-related proteins and F-actin in cells after mechanical stimulation. Merged images are presented in the same format as the control group.
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Image Search Results


A Representative immunoblotting analysis ( n = 3 independent experiments) of phosphorylated EPHA2 and FAK (EPHA2 Y588 and FAK Y397) in A549 (oe GLUD1 versus vector). B Representative immunoblotting analysis ( n = 3 independent experiments) of VE-Cadherin protein expression in whole-cell lysates (WCL) and membrane fractions of A549/DTX (si GLUD1 versus siNC; left) and A549 (oe GLUD1 versus vector; right). C Immunofluorescence staining of VE-Cadherin in A549/DTX (si GLUD1 versus siNC; top) and A549 (oe GLUD1 versus vector; bottom), with quantification shown in ( D ), n = 3 biologically independent samples. The average fluorescence intensity of VE-Cadherin on the cell membrane surface was calculated by manually selecting the area using FIJI. E Representative immunoblotting analysis ( n = 3 independent experiments) of VE-Cadherin and GLUD1 in A549 WCL following GLUD1 overexpression and subsequent CDH5 knockdown. F – K Representative images ( F – H ) and quantification ( I – K ) of adhesion ( F , I , n = 4 biologically independent samples), barrier-destruction ( G , J , n = 3 biologically independent samples) and transmigration ( H , K , n = 3 biologically independent samples) for siNC or si GLUD1 -treated A549 cells. Cells in ( F , H ) were counted using Fiji. G fluorescence was quantified using Fiji and normalized to the 30-min value within each experiment. L – O Immunofluorescence analysis of intravasation ( L ) and extravasation ( M ) in A549 cells following GLUD1 overexpression and subsequent CDH5 knockdown. Intravasation was quantified by tumor cells’ average fluorescence intensity in adjacent channels ( N , n = 4 biologically independent samples), while extravasation was measured by ECM-invading cells ( O , n = 3 biologically independent samples). All data were normalized to oe GLUD1 − /si CDH5 − group. All data are represented as mean ± SEM. P values were calculated using two-tailed unpaired Student’s t test D ; one-way ANOVA followed by Dunnett’s multiple-comparisons test ( I , K , N , O ); two-way ANOVA followed by Šídák multiple-comparisons test J . Scale bars: C , G , 20 μm; F , H , 1000 μm. Source data are provided as a Source Data file. For immunoblots, samples within each panel were derived from the same experiment, with separate gels processed in parallel where applicable; detailed gel assignments are provided in the Methods.

Journal: Nature Communications

Article Title: α-KG conformationally stabilizes nuclear GLUD1-SNAIL complex to fuel trans-endothelial migration in metastasis

doi: 10.1038/s41467-026-77149-0

Figure Lengend Snippet: A Representative immunoblotting analysis ( n = 3 independent experiments) of phosphorylated EPHA2 and FAK (EPHA2 Y588 and FAK Y397) in A549 (oe GLUD1 versus vector). B Representative immunoblotting analysis ( n = 3 independent experiments) of VE-Cadherin protein expression in whole-cell lysates (WCL) and membrane fractions of A549/DTX (si GLUD1 versus siNC; left) and A549 (oe GLUD1 versus vector; right). C Immunofluorescence staining of VE-Cadherin in A549/DTX (si GLUD1 versus siNC; top) and A549 (oe GLUD1 versus vector; bottom), with quantification shown in ( D ), n = 3 biologically independent samples. The average fluorescence intensity of VE-Cadherin on the cell membrane surface was calculated by manually selecting the area using FIJI. E Representative immunoblotting analysis ( n = 3 independent experiments) of VE-Cadherin and GLUD1 in A549 WCL following GLUD1 overexpression and subsequent CDH5 knockdown. F – K Representative images ( F – H ) and quantification ( I – K ) of adhesion ( F , I , n = 4 biologically independent samples), barrier-destruction ( G , J , n = 3 biologically independent samples) and transmigration ( H , K , n = 3 biologically independent samples) for siNC or si GLUD1 -treated A549 cells. Cells in ( F , H ) were counted using Fiji. G fluorescence was quantified using Fiji and normalized to the 30-min value within each experiment. L – O Immunofluorescence analysis of intravasation ( L ) and extravasation ( M ) in A549 cells following GLUD1 overexpression and subsequent CDH5 knockdown. Intravasation was quantified by tumor cells’ average fluorescence intensity in adjacent channels ( N , n = 4 biologically independent samples), while extravasation was measured by ECM-invading cells ( O , n = 3 biologically independent samples). All data were normalized to oe GLUD1 − /si CDH5 − group. All data are represented as mean ± SEM. P values were calculated using two-tailed unpaired Student’s t test D ; one-way ANOVA followed by Dunnett’s multiple-comparisons test ( I , K , N , O ); two-way ANOVA followed by Šídák multiple-comparisons test J . Scale bars: C , G , 20 μm; F , H , 1000 μm. Source data are provided as a Source Data file. For immunoblots, samples within each panel were derived from the same experiment, with separate gels processed in parallel where applicable; detailed gel assignments are provided in the Methods.

Article Snippet: The antibodies used were shown as followed: VE-Cadherin (ab33168; 1:1000, Abcam), Lamin B (ab16048; 1:5000, Abcam), Sodium/Potassium ATPase alpha 1 (ab308329; 1:1000, Abcam), FLAG (ab205606; 1:10,000, Abcam), ACTIN (ab8226, 1:2000, Abcam), GLUD1 (14299-1-AP; 1:1000, Proteintech), FAK (12636-1-AP; 1:1000, Proteintech), EPHA2 (25749-1-AP; 1:1000, Proteintech), SNAIL (13099-1-AP; 1:1000, Proteintech), β-Tubulin (80713-1-RR; 1:1000, Proteintech), Phospho-FAK (83933-1-RR, 1:1000, Proteintech), Phospho-EPHA2 (25749-1-AP, 1:1000, Proteintech), SOX2 (11064-1-AP, 1:500, Proteintech), SLUG (12129-1-AP, 1:500, Proteintech), ZEB1 (21544-1-AP, 1:500, Proteintech).

Techniques: Western Blot, Analysis, Plasmid Preparation, Expressing, Membrane, Immunofluorescence, Staining, Fluorescence, Over Expression, Knockdown, Transmigration Assay, Two Tailed Test, Derivative Assay

Immunofluorescence staining of focal adhesion-related markers and cytoskeleton in cells under control and mechanical stimulation conditions. Left (Control group): Immunofluorescence staining shows focal adhesion-associated proteins (green channels). These correspond to integrin β1(A), talin (B), pFAK/FAK (C), paxillin (D), YAP (E), and TAZ (F) in each row. F-actin and FAK are shown in the red channel. The rightmost column of each row displays merged images. These integrate focal adhesion marker signals (green), F-actin (red), and DAPI-stained nuclei (blue). Yellow indicates co-localization of focal adhesion markers and F-actin. Right (After mechanical stimulation group): Immunofluorescence staining displays the same set of focal adhesion-related proteins and F-actin in cells after mechanical stimulation. Merged images are presented in the same format as the control group.

Journal: Bioactive Materials

Article Title: Pre-priming cell sheet therapy enabled by dynamic wrinkled electroactive substrate for muscle reconstruction

doi: 10.1016/j.bioactmat.2026.01.046

Figure Lengend Snippet: Immunofluorescence staining of focal adhesion-related markers and cytoskeleton in cells under control and mechanical stimulation conditions. Left (Control group): Immunofluorescence staining shows focal adhesion-associated proteins (green channels). These correspond to integrin β1(A), talin (B), pFAK/FAK (C), paxillin (D), YAP (E), and TAZ (F) in each row. F-actin and FAK are shown in the red channel. The rightmost column of each row displays merged images. These integrate focal adhesion marker signals (green), F-actin (red), and DAPI-stained nuclei (blue). Yellow indicates co-localization of focal adhesion markers and F-actin. Right (After mechanical stimulation group): Immunofluorescence staining displays the same set of focal adhesion-related proteins and F-actin in cells after mechanical stimulation. Merged images are presented in the same format as the control group.

Article Snippet: FAK Antibody (sc-271126), pFAK(Y3978556s), talin (sc: 4021s), paxillin (sc: 365379), integrin β1 (sc: 374429), and YAP (cst: 14074s), TAZ (cst: 83669s) were ordered from Santa Cruz Biotechnology.

Techniques: Immunofluorescence, Staining, Control, Marker