Journal: Scientific Reports

Article Title: Caveolin 1 and 2 enhance the proliferative capacity of BCAM-positive corneal progenitors

doi: 10.1038/s41598-024-81283-4

Figure Lengend Snippet: Evaluation of CAV1 and CAV2 expression in human limbus and cornea. Comparative analyses of CAV1 and CAV2 mRNA expression in BCAM-positive and BCAM-negative cells in the limbus ( a ) ( n = 8) and cornea ( b ) ( n = 3) (* p < 0.05, ** p < 0.01) ( c ) Representative immunostaining analyses of CAV1 (green), CAV2 (yellow) and BCAM (red) co-expression in the limbus and cornea. Sequential sections were used to illustrate BCAM and CAV1 co-expression since both antibodies were raised in rabbits. Nuclei are visualized with Hoechst 33342 (blue). n = 3. Scale bar, 50 μm. ( d ) Representative immunostaining analyses of CAV1 (green), CAV2 (yellow) and Laminin α5 (red) co-expression (top panels) and CAV1 (green), CAV2 (yellow) and Laminin α3 (red) (bottom panels) in the limbus and the cornea. Nuclei are visualized with Hoechst 33342 (blue). n = 3. Scale bar, 50 μm.

Article Snippet: Primary antibodies used in the current study were: rabbit anti-β-actin pAb (1:1000, Cell Signaling Technology), rabbit anti-CAV1 pAb (1:500, GeneTex), rabbit anti-CAV2 pAb (1:1000, GeneTex), rabbit anti-BCAM pAb (1:1000, ABClonal, Woburn, MA), rabbit anti-laminin α5 pAb (1:500, GeneTex), mouse anti-laminin α3 mAb (1:500, Atlas Antibodies) and rabbit anti-FGFR2 mAb (1:1000, Cell Signaling Technology).

Techniques: Expressing, Immunostaining

Journal: Scientific Reports

Article Title: Caveolin 1 and 2 enhance the proliferative capacity of BCAM-positive corneal progenitors

doi: 10.1038/s41598-024-81283-4

Figure Lengend Snippet: Regulation of CAV1 and CAV2 expression in limbal epithelial cells. ( a ) Left, western blot analysis of CAV1, CAV2 and BCAM expression in BCAM KD limbal epithelial cells. Right, bar graph depicts the quantitative analyses of CAV1 and CAV2 protein expression. Bottom, representative flow cytometry analysis of BCAM expression in BCAM KD limbal epithelial cells. n = 4, * p < 0.05, KD, knockdown. ( b ) Left, western blot analyses of CAV1, CAV2 and laminin α5 expression in LAMA5 KD limbal epithelial cells. Right, the bar graphs represent the quantitative analyses of CAV1 and CAV2 protein expression. n = 8, *** p < 0.001, **** p < 0.0001. ( c ) Left, Western blot analyses of CAV1, CAV2 and laminin α3 expression in control and LAMA3 KD limbal epithelial cells. Right, the bar graphs represent the quantitative analyses of CAV1 and CAV2 protein expression. n = 6, * p < 0.05, ** p < 0.01.

Article Snippet: Primary antibodies used in the current study were: rabbit anti-β-actin pAb (1:1000, Cell Signaling Technology), rabbit anti-CAV1 pAb (1:500, GeneTex), rabbit anti-CAV2 pAb (1:1000, GeneTex), rabbit anti-BCAM pAb (1:1000, ABClonal, Woburn, MA), rabbit anti-laminin α5 pAb (1:500, GeneTex), mouse anti-laminin α3 mAb (1:500, Atlas Antibodies) and rabbit anti-FGFR2 mAb (1:1000, Cell Signaling Technology).

Techniques: Expressing, Western Blot, Flow Cytometry, Knockdown, Control

Journal: Journal of Biological Chemistry

Article Title: Altered Cortical GABAA Receptor Composition, Physiology, and Endocytosis in a Mouse Model of a Human Genetic Absence Epilepsy Syndrome

doi: 10.1074/jbc.m112.444372

Figure Lengend Snippet: FIGURE4.Het1KOalteredtheassociationof1and3subunits.A,COS-7 cells were left untransfected or were transfected with 122 or 322 GABAAR (n 3). Cellular lysates were immunoprecipitated (IP) with either the 1 or 3 subunit, and the products were analyzed by Western blot. The blots were probed with the anti-1 subunit antibody (green) and the anti-3 sub- unit antibody (red). Neither the 1 nor 3 antibody immunoprecipitated pro- teins from untransfected cells. The 1 subunit antibody but not the anti-3 subunit antibody immunoprecipitated the 1 subunit protein from the cells expressing 122 receptors, and the 3 subunit antibody but not the 1 subunit antibody immunoprecipitated 3 subunit protein from the cells expressing 322 receptors. B, cortical lysates from wild type mice were immunoprecipitated with the mouse 1 subunit antibody (Ms 1), the rabbit 3 subunit antibody (Rb 3), or control immunoglobulin from nonimmu- nized mice (Ms cont) or rabbits (Rb cont). Immunoprecipitated material was analyzed by Western blot and stained for the 1 (green) or 3 (red) subunit. The anti-1 and anti-3 subunit antibodies coimmunoprecipitated 1 and 3 subunits, but neither the mouse nor rabbit control immunoglobulin immunoprecipitated either subunit. C–F, total protein from wild type and Het1KO cortices was immunoprecipitated with antibodies directed against the 1 or 3 subunits. Immunoprecipitated material (5, 10, and 20 l) was analyzedonWesternblot,whichwasstainedwithboththe1and3subunit antibodies (C and D). Immunoprecipitation using the anti-1 subunit anti- body (C and E) recovered 68 11% as much 1 subunit from Het1KO cortex as compared with wild type cortex (n 5, p 0.039), and, when normalized to recovered 1 subunit, co-immunoprecipitated 227 20% as much 3 subunit from Het1KO cortex as from wild type cortex (n 4, p 0.008). Immunoprecipitation using the anti-3 subunit antibody (D and F) recovered 173 19% as much 3 subunit from Het1KO as from wild type cortex (n 5, p 0.020) and co-immunoprecipitated 63 8% as much normalized 1 subunit from Het1KO as from wild type cortex (n 4, p 0.008). Error bars, S.E.

Article Snippet: The anti- 3 subunit antibody was from Alomone (AGA-003, 1:500).

Techniques: Transfection, Immunoprecipitation, Western Blot, Expressing, Control, Staining, Protein-Protein interactions, Tandem Mass Spectroscopy

Journal: Cell Journal (Yakhteh)

Article Title: The Effect of Endometrial Cell Culture on α3 and β1 integrin Genes and Protein Expression in Type 2 Diabetic Rats at The Time of Implantation

doi: 10.22074/cellj.2022.7445

Figure Lengend Snippet: Sequences of the real time‑polymerase chain reaction primer sets

Article Snippet: After electrophoresis, the separated proteins were blotted onto a nitrocellulose membrane (AR0135-02, Boster, USA) Incubation was then performed with a primary antibody solution against rabbit anti-rat α3 and β1 integrin antibody (Bs-1057R, Bioss, London) in appropriate dilution for 2 hours. at room temperature with gentle shaking.

Techniques: Real-time Polymerase Chain Reaction

Journal: Cell Journal (Yakhteh)

Article Title: The Effect of Endometrial Cell Culture on α3 and β1 integrin Genes and Protein Expression in Type 2 Diabetic Rats at The Time of Implantation

doi: 10.22074/cellj.2022.7445

Figure Lengend Snippet: The level of α3 integrin gene expression in the isolated endometrial cells on days 0 and 7 th after cell culture at the time of embryo implantation. *; P<0.05.

Article Snippet: After electrophoresis, the separated proteins were blotted onto a nitrocellulose membrane (AR0135-02, Boster, USA) Incubation was then performed with a primary antibody solution against rabbit anti-rat α3 and β1 integrin antibody (Bs-1057R, Bioss, London) in appropriate dilution for 2 hours. at room temperature with gentle shaking.

Techniques: Expressing, Isolation, Cell Culture

Journal: Cell Journal (Yakhteh)

Article Title: The Effect of Endometrial Cell Culture on α3 and β1 integrin Genes and Protein Expression in Type 2 Diabetic Rats at The Time of Implantation

doi: 10.22074/cellj.2022.7445

Figure Lengend Snippet: Comparison of α3 and β1 integrin protein levels in isolated endometrial cells on days 0 and 7 after cell culture at the time of embryo implantation. *; P<0.05.

Article Snippet: After electrophoresis, the separated proteins were blotted onto a nitrocellulose membrane (AR0135-02, Boster, USA) Incubation was then performed with a primary antibody solution against rabbit anti-rat α3 and β1 integrin antibody (Bs-1057R, Bioss, London) in appropriate dilution for 2 hours. at room temperature with gentle shaking.

Techniques: Isolation, Cell Culture