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  • 91
    Santa Cruz Biotechnology integrin α6
    <t>α6/β4-Integrin</t> signaling is essential for ΔNp63α expression A ECS cells display elevated α6/β4-integrin levels and elevated FAK/Src signaling. SCC-13 cells (40,000 per well) were grown in spheroid medium in attached (monolayer) or non-attached (spheroid, ECS cell). Cells were collected after 10 d and lysates were prepared for immunoblot. B SCC-13 cells spheroid were grown for 8 d and extracts were immunoprecipitated as indicated prior to immunoblot. C Integrin signaling is reduced in SCC13-TG2-shRNA2 cells. Cells were grown in spheroid medium in monolayer culture for 10 d prior to collection of lysates for immunoblot. D/E/F SCC-13 cells were double-electroporated with Control- or Integrin β4-, FAK-, or Src-siRNA and 48 h later extracts were prepared for immunoblot. G/H/I SCC-13 cells were double-electroporated with the indicated siRNA and 24 h later plated for growth as spheroids and for invasion and migration assays. J/K/L Cells were double-electroporated with indicated plasmid (EV, empty vector or ΔNp63α plasmid) and 24 h later plated for spheroid formation in the presence of the indicated inhibitor. Spheroids were grown for 5 d and then photographed and extracts prepared for immunoblot. The plotted values are mean ± SEM and asterisks indicate significant change compared to control, n = 3, p
    Integrin α6, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 193 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore α6 integrin
    Immunoblot of A. Integrin β1 B. Integrin α5 C. Integrin <t>α6</t> and D. β-actin used as loading control in MiaPaCa-2, Clone #3 and Clone #8 . E. Knockdown of integrin β1 in Clone #8 cells 48 hours post transfection (siRNAs ITGβ1 #1 and #2). F. Knockdown of integrin α5 in Clone #8 cells 48 hours post transfection (siRNAs ITGα5 #1, #2). G. Knockdown of integrin α6 in Clone #8 cells 48 hours post transfection (siRNAs ITGα6 #1 and #2). H. Beta-actin used as loading control.
    α6 Integrin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 313 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Abcam integrin α6
    <t>Integrin</t> <t>α6</t> subunit expression by Schlemm’s canal cells. A : Confocal immunofluorescence microscopy of outflow tissues including Schlemm’s canal (SC) from human donor eyes showing α6 integrin (INTG) levels. Shown is representative image from eye of individual human donor of 3 donor eyes that were examined. For comparison, a scleral vessel is indicated (*). B : western blot analysis of different human SC and trabecular meshwork (TM) cell strains checking for α6 integrin levels. Cell lysates were first subjected to immunoprecipition using integrin α6-specific IgGs, followed by SDS–PAGE and western blotting using IgGs that recognize both α3 and α6 INTG.
    Integrin α6, supplied by Abcam, used in various techniques. Bioz Stars score: 91/100, based on 120 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Becton Dickinson α6 integrin
    A , <t>integrin</t> endocytosis assay to examine the recycling <t>α6</t> integrin. BV2 and iPLA-KD cells were plated on LN-coated coverslips, and an integrin endocytosis assay was performed as described under “Experimental Procedures.” In untreated BV2 and iPLA-KD cells, endocytosed α6 integrin was found predominantly in a perinuclear vesicular structure. Following ADP treatment, α6 integrin localization changed to plasma membrane or vesicles in the periphery of BV2 cells, but this change is absent in iPLA-KD cells. Scale bar , 10 μm. The ratios of fluorescence intensities in the perinuclear area and cellular periphery from 10 cells were determined and are shown in the graph. Error bars represent S.E. **, p
    α6 Integrin, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 93/100, based on 155 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Becton Dickinson anti integrin α6
    <t>Integrin</t> α3β1 promotes CD cell adhesion, migration, and proliferation on LM-332 and LM-511. (A) Lysates from Itgα3 −/− and Itgα3 f/f CD cells (20 μg total protein/lane) were immunoblotted for integrin β1, α3, and <t>α6</t> subunits. β-actin served as a loading control. (B) Surface expression of integrin β1, α3, and α6 subunits was determined on Itgα3 −/− and Itgα3 f/f CD cells by flow cytometry using R-phycoerythrin (PE). (C) Lysates from Itgα3 −/− and Itgα3 f/f CD cells (100 μg total protein) were immunoprecipitated with anti-Itgα6 antibody or normal rabbit IgG and immunoblotted for integrin subunits β1 and β4. Adhesion (D and E), migration (F), and proliferation (G) of Itgα3 f/f and Itgα3 −/− CD cells on LM-332 and LM-511 were evaluated as described in Materials and Methods . Mean measurements ±SEM of four to six independent experiments are shown; *, p ≤ 0.05 between Itgα3 f/f and Itgα3 −/− CD cells. (H) Itgα3 f/f and Itgα3 −/− CD cells were treated with blocking anti-Itgα6 antibody and plated on LM-332. Adhesion was evaluated as described in Materials and Methods . Mean measurements ± SEM of three independent experiments are shown; *, p ≤ 0.05 between CD cells and CD cells treated with blocking anti-Itgα6 antibody.
    Anti Integrin α6, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 94/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Abcam anti integrin alpha 6 antibody epr18124
    <t>Integrin</t> α3β1 promotes CD cell adhesion, migration, and proliferation on LM-332 and LM-511. (A) Lysates from Itgα3 −/− and Itgα3 f/f CD cells (20 μg total protein/lane) were immunoblotted for integrin β1, α3, and <t>α6</t> subunits. β-actin served as a loading control. (B) Surface expression of integrin β1, α3, and α6 subunits was determined on Itgα3 −/− and Itgα3 f/f CD cells by flow cytometry using R-phycoerythrin (PE). (C) Lysates from Itgα3 −/− and Itgα3 f/f CD cells (100 μg total protein) were immunoprecipitated with anti-Itgα6 antibody or normal rabbit IgG and immunoblotted for integrin subunits β1 and β4. Adhesion (D and E), migration (F), and proliferation (G) of Itgα3 f/f and Itgα3 −/− CD cells on LM-332 and LM-511 were evaluated as described in Materials and Methods . Mean measurements ±SEM of four to six independent experiments are shown; *, p ≤ 0.05 between Itgα3 f/f and Itgα3 −/− CD cells. (H) Itgα3 f/f and Itgα3 −/− CD cells were treated with blocking anti-Itgα6 antibody and plated on LM-332. Adhesion was evaluated as described in Materials and Methods . Mean measurements ± SEM of three independent experiments are shown; *, p ≤ 0.05 between CD cells and CD cells treated with blocking anti-Itgα6 antibody.
    Anti Integrin Alpha 6 Antibody Epr18124, supplied by Abcam, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Cell Signaling Technology Inc integrin α6
    <t>Integrin</t> <t>α6</t> expression rescues KLF9-induced growth inhibition of glioma xenografts. GBM1b neurospheres were infected with lentivirus to express FLAG-KLF9, integrin α6, or both. A , immunofluorescence of neurosphere cells shows the expression
    Integrin α6, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Santa Cruz Biotechnology anti integrin α6
    Intravenous immunoglobulin (IVIg) prevents BP-IgG-induced type XVII collagen (COL17) depletion. DJM-1 cells (40% confluency) were treated with 1.0 mg/ml BP-IgG. Western blotting using total cell lysate was performed for anti-COL17. (A) DJM-1 cells were treated with IVIg (5–0.5–0.05–0.005 mg/ml) for 1 h followed by BP-IgG for 4 h (pretreatment). (B) DJM-1 cells were treated with BP-IgG for 4 h followed by IVIg for 1 h (posttreatment). (C) BP-IgG and IVIg were incubated in advance, and then added to the culture medium together (simultaneous). (D) DJM-1 cells were treated with appropriate controls. The amount of <t>integrin</t> <t>α6,</t> which is a transmembrane protein and a hemidesmosome component, was not changed. The representative Western blot is presented. Each experiment was performed at least three times, with p
    Anti Integrin α6, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher cd49f integrin alpha 6 monoclonal antibody
    Intravenous immunoglobulin (IVIg) prevents BP-IgG-induced type XVII collagen (COL17) depletion. DJM-1 cells (40% confluency) were treated with 1.0 mg/ml BP-IgG. Western blotting using total cell lysate was performed for anti-COL17. (A) DJM-1 cells were treated with IVIg (5–0.5–0.05–0.005 mg/ml) for 1 h followed by BP-IgG for 4 h (pretreatment). (B) DJM-1 cells were treated with BP-IgG for 4 h followed by IVIg for 1 h (posttreatment). (C) BP-IgG and IVIg were incubated in advance, and then added to the culture medium together (simultaneous). (D) DJM-1 cells were treated with appropriate controls. The amount of <t>integrin</t> <t>α6,</t> which is a transmembrane protein and a hemidesmosome component, was not changed. The representative Western blot is presented. Each experiment was performed at least three times, with p
    Cd49f Integrin Alpha 6 Monoclonal Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 101 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Abcam anti integrin α6
    FKBP10 promotes adhesion of GC cells (A) FKBP10 protein expression in gastric cancer cell line and GES-1. ( B ) and ( C ) FKBP10 mRNA and protein expression levels were tested by qRT-PCR and Western blot analysis in HGC-27 and MKN-7 cells after transfected with siFKBP10 for 48 hours. ( D ) Adhesion assay was used to detect changes in adhesion ability of HGC-27 and MKN-7 cells after transfected with siFKBP10 for 48 hours. ( E ) Quantifications of cells are shown as proportions of the number of control cells. Original magnification, 200×. Scale bar: 100 µM. ( F ) and ( G ) <t>Integrin</t> α1, integrin α2, integrin α5, integrin αV, integrin <t>α6,</t> AKT, P-AKT 308, P-AKT 473 proteins were detected by Western blot analysis in HGC-27 and MKN-7 cells after transfected with siFKBP10 for 48 hours. β-actin was used as a loading control in Western blot.(*P
    Anti Integrin α6, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Merck KGaA anti α6 integrin
    Effect of laminin isoforms on limbal progenitor cell adhesion and migration. ( A ) The effect of laminin (LN) isoforms on cell adhesion was tested by seeding limbal epithelial progenitor cells (LEPC) at a density of 50,000 cells/cm 2 and spectrophotometric measurement of adherent cells 30 and 60 minutes after seeding. Data are expressed as means ± SEM (n = 4). ( B ) Phase contrast images of LEPC cultured on LN isoforms; magnification ×100. ( C ) Flow cytometry analyses of cultured LEPC showing expression of <t>integrin</t> α3 (ITGA3), integrin <t>α6</t> (ITGA6), integrin β1 (ITGB1), and integrin β4 (ITGB4) on their surface. Percentages (%) of positive cells are expressed as means ± SEM percentage (%) (n = 3). ( D ) Functional blocking of integrin-mediated LEPC adhesion to LN-521, -511, -511-E8 and -332 was tested using neutralizing antibodies against integrin α3β1 and α6β1 60 minutes seeding. Data are expressed as means ± SEM (n = 4). ( E ) The effect of LN isoforms on LEPC migration was analyzed in two well-culture inserts with a defined cell-free gap and measurement of gap closure 3 and 6 hours after removal of the culture inserts. Data are expressed as means ± SEM (n = 3); *p
    Anti α6 Integrin, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 89/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher anti α6 integrin
    Genetic signature of TPA treated and expanded epidermis. a , Representative FACS plots showing the strategy used to isolate basal cells. Single living cells were gated by debris exclusion (P1), DAPI exclusion (P2), doublet elimination (P3) and basal IFE <t>Integrin-α6</t> high CD34 neg cell were sorted (P4). n=10 independent experiments. b, c , mRNA expression of genes that were upregulated in basal cells at EXP D4 (n = 3) and in cells treated with TPA (n = 2). These genes are related to a generic stress signature (b) , regulating ECM remodeling and cytoskeleton, important for cell survival and cell cycle (c). Bars are mean with s.e.m. d , Representative images of Paxillin immunostaining color-coded for the signal intensity with ImageJ. Protein expression is visualized as a color gradient going from black to yellow with black as indicator of no expression and yellow as indicator of maximal expression. Scale bar, 10 μm e , Quantification of the average integrated density signal for Paxillin as in d. Each data point is the average of 3 sections per mouse (n = 3 mice per condition). f , Geometric mean fluorescence intensity for the indicated integrin in CTRL (grey, n = 4 mice) and EXP D4 (red, n = 6 mice) from FACS analysis of basal IFE Integrin-α6 high CD34 neg cells. g-k , ATAC-seq profiles showing increasing accessibility of chromatin regions that are specifically remodeled during mechanical expansion (CTRL in grey and EXP D2 in orange). l , Quantification of the number of cells FOSL1+ in the basal layer related to . m , Immunostaining on skin sections for c-JUN (white) in control and EXP D4. n , Quantification of the number of cells c-JUN+ in the basal layer related to m. o . p . q , Immunohistochemistry on paraffin sections for c-FOS in control and EXPD4. Scale bar, 20 μm. r , Quantification of the number of cells c-FOSL+ in the basal layer related to q. s , Immunofluorescence on tissue sections for pSTAT3 in green and K14 (red) to identified the epidermis. Scale bar, 20 μm. t , Quantification of the number of cells positive for pSTAT3 in the basal layer related to s. l, n, o, p, r, t , 3 sections quantified per n = number of mice and total number of cells indicated in parentheses d, m, q, s , Dashed lines delineate the basal lamina. e, f, l, n, o, p, r, t , Two-tailed Mann–Whitney test, Mean + s.e.m. Fig. 3d
    Anti α6 Integrin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher integrin α6
    NF B cells express laminin α5 binding integrins and show some colocalization with laminin α5 in the MZ. ( A ) Representative flow cytometry for cell surface <t>integrin</t> expression on NF B cells with antibody isotype controls shown in gray. ( B ) In vitro adhesion of MZ, FO, and NF B cells to VCAM-1, laminin 511/521, the RGD-containing laminin α5 domain IVa, agrin, fibronectin (all 30 μM), or BSA. Adhesion of NF B cells to VCAM-1, laminin 511/521, or fibronectin was measured in the presence or absence of function blocking antibodies to integrins β1 (Ha2/5), <t>α6</t> (GoH3), or α4 (PS/2). Data shown are mean values ± SEM from three separate experiments with n = 6 for each treatment in each experiment. ( C ) Immunofluorescence staining shows the presence of IgM + CD21 low and ( D ) IgM + AA4.1 + B cells in the MZ of mature mice (arrowheads). Magnification, 100× ( D , Left ), 200× ( C , Upper ), 400× ( C, Lower , and D, Right ). ( E ) In vivo localization of ex vivo TAMRA-labeled NF B cells or FO B cells (isolated from day 10 mouse spleens) at 16 h after i.v injection into mature mice in the presence or absence of GoH3. Immunofluorescent staining for laminin α5 reveals localization of NF B cells in the MZ (double arrows), follicle, and RP, whereas FO B cells home predominantly to the follicle. Coinjection with GoH3 reduced TAMRA + NF B-cell localization to the MZ only. Magnification: 100×. Bar graph shows quantification of the ratio of MZ/FO localized TAMRA + cells; data are means ± SEM from two experiments with four mice in each category. * P
    Integrin α6, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 82 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore α6
    NF B cells express laminin α5 binding integrins and show some colocalization with laminin α5 in the MZ. ( A ) Representative flow cytometry for cell surface <t>integrin</t> expression on NF B cells with antibody isotype controls shown in gray. ( B ) In vitro adhesion of MZ, FO, and NF B cells to VCAM-1, laminin 511/521, the RGD-containing laminin α5 domain IVa, agrin, fibronectin (all 30 μM), or BSA. Adhesion of NF B cells to VCAM-1, laminin 511/521, or fibronectin was measured in the presence or absence of function blocking antibodies to integrins β1 (Ha2/5), <t>α6</t> (GoH3), or α4 (PS/2). Data shown are mean values ± SEM from three separate experiments with n = 6 for each treatment in each experiment. ( C ) Immunofluorescence staining shows the presence of IgM + CD21 low and ( D ) IgM + AA4.1 + B cells in the MZ of mature mice (arrowheads). Magnification, 100× ( D , Left ), 200× ( C , Upper ), 400× ( C, Lower , and D, Right ). ( E ) In vivo localization of ex vivo TAMRA-labeled NF B cells or FO B cells (isolated from day 10 mouse spleens) at 16 h after i.v injection into mature mice in the presence or absence of GoH3. Immunofluorescent staining for laminin α5 reveals localization of NF B cells in the MZ (double arrows), follicle, and RP, whereas FO B cells home predominantly to the follicle. Coinjection with GoH3 reduced TAMRA + NF B-cell localization to the MZ only. Magnification: 100×. Bar graph shows quantification of the ratio of MZ/FO localized TAMRA + cells; data are means ± SEM from two experiments with four mice in each category. * P
    α6, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 106 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Hitachi aloka prosound α6
    NF B cells express laminin α5 binding integrins and show some colocalization with laminin α5 in the MZ. ( A ) Representative flow cytometry for cell surface <t>integrin</t> expression on NF B cells with antibody isotype controls shown in gray. ( B ) In vitro adhesion of MZ, FO, and NF B cells to VCAM-1, laminin 511/521, the RGD-containing laminin α5 domain IVa, agrin, fibronectin (all 30 μM), or BSA. Adhesion of NF B cells to VCAM-1, laminin 511/521, or fibronectin was measured in the presence or absence of function blocking antibodies to integrins β1 (Ha2/5), <t>α6</t> (GoH3), or α4 (PS/2). Data shown are mean values ± SEM from three separate experiments with n = 6 for each treatment in each experiment. ( C ) Immunofluorescence staining shows the presence of IgM + CD21 low and ( D ) IgM + AA4.1 + B cells in the MZ of mature mice (arrowheads). Magnification, 100× ( D , Left ), 200× ( C , Upper ), 400× ( C, Lower , and D, Right ). ( E ) In vivo localization of ex vivo TAMRA-labeled NF B cells or FO B cells (isolated from day 10 mouse spleens) at 16 h after i.v injection into mature mice in the presence or absence of GoH3. Immunofluorescent staining for laminin α5 reveals localization of NF B cells in the MZ (double arrows), follicle, and RP, whereas FO B cells home predominantly to the follicle. Coinjection with GoH3 reduced TAMRA + NF B-cell localization to the MZ only. Magnification: 100×. Bar graph shows quantification of the ratio of MZ/FO localized TAMRA + cells; data are means ± SEM from two experiments with four mice in each category. * P
    Aloka Prosound α6, supplied by Hitachi, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Biomol GmbH anti 20s subunit α6
    NF B cells express laminin α5 binding integrins and show some colocalization with laminin α5 in the MZ. ( A ) Representative flow cytometry for cell surface <t>integrin</t> expression on NF B cells with antibody isotype controls shown in gray. ( B ) In vitro adhesion of MZ, FO, and NF B cells to VCAM-1, laminin 511/521, the RGD-containing laminin α5 domain IVa, agrin, fibronectin (all 30 μM), or BSA. Adhesion of NF B cells to VCAM-1, laminin 511/521, or fibronectin was measured in the presence or absence of function blocking antibodies to integrins β1 (Ha2/5), <t>α6</t> (GoH3), or α4 (PS/2). Data shown are mean values ± SEM from three separate experiments with n = 6 for each treatment in each experiment. ( C ) Immunofluorescence staining shows the presence of IgM + CD21 low and ( D ) IgM + AA4.1 + B cells in the MZ of mature mice (arrowheads). Magnification, 100× ( D , Left ), 200× ( C , Upper ), 400× ( C, Lower , and D, Right ). ( E ) In vivo localization of ex vivo TAMRA-labeled NF B cells or FO B cells (isolated from day 10 mouse spleens) at 16 h after i.v injection into mature mice in the presence or absence of GoH3. Immunofluorescent staining for laminin α5 reveals localization of NF B cells in the MZ (double arrows), follicle, and RP, whereas FO B cells home predominantly to the follicle. Coinjection with GoH3 reduced TAMRA + NF B-cell localization to the MZ only. Magnification: 100×. Bar graph shows quantification of the ratio of MZ/FO localized TAMRA + cells; data are means ± SEM from two experiments with four mice in each category. * P
    Anti 20s Subunit α6, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 85/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    N/A
    CRISPR Cas9 KO Plasmids consists of IFN α6 specific 20 nt guide RNA sequences derived from the GeCKO v2 library For CRISPR gene knockout gRNA sequences direct the Cas9 protein
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    N/A
    Target species human Gene Silencers generally consist of pools of three to five target specific 19 25 nucleotide sequences in length For independent verification of IFN α6 gene silencing results
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    N/A
    CRISPR Cas9 KO Plasmids consists of IFN α6 specific 20 nt guide RNA sequences derived from the GeCKO v2 library For CRISPR gene knockout gRNA sequences direct the Cas9 protein
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    N/A
    CRISPR Cas9 KO Plasmids consists of IFN α6 specific 20 nt guide RNA sequences derived from the GeCKO v2 library For CRISPR gene knockout gRNA sequences direct the Cas9 protein
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    Image Search Results


    α6/β4-Integrin signaling is essential for ΔNp63α expression A ECS cells display elevated α6/β4-integrin levels and elevated FAK/Src signaling. SCC-13 cells (40,000 per well) were grown in spheroid medium in attached (monolayer) or non-attached (spheroid, ECS cell). Cells were collected after 10 d and lysates were prepared for immunoblot. B SCC-13 cells spheroid were grown for 8 d and extracts were immunoprecipitated as indicated prior to immunoblot. C Integrin signaling is reduced in SCC13-TG2-shRNA2 cells. Cells were grown in spheroid medium in monolayer culture for 10 d prior to collection of lysates for immunoblot. D/E/F SCC-13 cells were double-electroporated with Control- or Integrin β4-, FAK-, or Src-siRNA and 48 h later extracts were prepared for immunoblot. G/H/I SCC-13 cells were double-electroporated with the indicated siRNA and 24 h later plated for growth as spheroids and for invasion and migration assays. J/K/L Cells were double-electroporated with indicated plasmid (EV, empty vector or ΔNp63α plasmid) and 24 h later plated for spheroid formation in the presence of the indicated inhibitor. Spheroids were grown for 5 d and then photographed and extracts prepared for immunoblot. The plotted values are mean ± SEM and asterisks indicate significant change compared to control, n = 3, p

    Journal: Cancer research

    Article Title: Transglutaminase interaction with α6/β4-integrin stimulates YAP1-dependent ΔNp63α stabilization and leads to enhanced cancer stem cell survival and tumor formation

    doi: 10.1158/0008-5472.CAN-16-2032

    Figure Lengend Snippet: α6/β4-Integrin signaling is essential for ΔNp63α expression A ECS cells display elevated α6/β4-integrin levels and elevated FAK/Src signaling. SCC-13 cells (40,000 per well) were grown in spheroid medium in attached (monolayer) or non-attached (spheroid, ECS cell). Cells were collected after 10 d and lysates were prepared for immunoblot. B SCC-13 cells spheroid were grown for 8 d and extracts were immunoprecipitated as indicated prior to immunoblot. C Integrin signaling is reduced in SCC13-TG2-shRNA2 cells. Cells were grown in spheroid medium in monolayer culture for 10 d prior to collection of lysates for immunoblot. D/E/F SCC-13 cells were double-electroporated with Control- or Integrin β4-, FAK-, or Src-siRNA and 48 h later extracts were prepared for immunoblot. G/H/I SCC-13 cells were double-electroporated with the indicated siRNA and 24 h later plated for growth as spheroids and for invasion and migration assays. J/K/L Cells were double-electroporated with indicated plasmid (EV, empty vector or ΔNp63α plasmid) and 24 h later plated for spheroid formation in the presence of the indicated inhibitor. Spheroids were grown for 5 d and then photographed and extracts prepared for immunoblot. The plotted values are mean ± SEM and asterisks indicate significant change compared to control, n = 3, p

    Article Snippet: TG2- (sc-37514), p63- (sc-36161), FAK- (sc-29310), integrin α6- (sc-43129), integrin β4- (sc-35678) and control-siRNA (sc-37007) were from Santa Cruz (Dallas, TX).

    Techniques: Expressing, Immunoprecipitation, Migration, Plasmid Preparation

    Immunoblot of A. Integrin β1 B. Integrin α5 C. Integrin α6 and D. β-actin used as loading control in MiaPaCa-2, Clone #3 and Clone #8 . E. Knockdown of integrin β1 in Clone #8 cells 48 hours post transfection (siRNAs ITGβ1 #1 and #2). F. Knockdown of integrin α5 in Clone #8 cells 48 hours post transfection (siRNAs ITGα5 #1, #2). G. Knockdown of integrin α6 in Clone #8 cells 48 hours post transfection (siRNAs ITGα6 #1 and #2). H. Beta-actin used as loading control.

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Alterations in integrin expression modulates invasion of pancreatic cancer cells

    doi: 10.1186/1756-9966-28-140

    Figure Lengend Snippet: Immunoblot of A. Integrin β1 B. Integrin α5 C. Integrin α6 and D. β-actin used as loading control in MiaPaCa-2, Clone #3 and Clone #8 . E. Knockdown of integrin β1 in Clone #8 cells 48 hours post transfection (siRNAs ITGβ1 #1 and #2). F. Knockdown of integrin α5 in Clone #8 cells 48 hours post transfection (siRNAs ITGα5 #1, #2). G. Knockdown of integrin α6 in Clone #8 cells 48 hours post transfection (siRNAs ITGα6 #1 and #2). H. Beta-actin used as loading control.

    Article Snippet: Anti-β1 (MAB1951Z-20), anti-α5 (AB1949) and anti-α6 (MAB1982) were obtained from Chemicon (Millipore, Europe).

    Techniques: Transfection

    A vascularized mammary duct platform models native 3D tissue architectures and morphogenesis. Tissues are at one week of co-culture unless otherwise indicated. a Organotypic microfluidic device consisting of an engineered 3D endothelial vessel (green) and mammary epithelial duct (cyan) in physiologic ECM (magenta), enabling long-term culture and paracrine signaling. Inset: 3D reconstruction of endothelial vessel (green—VE-cadherin) and epithelial duct (cyan—phalloidin). b Left: Composite stitched maximum intensity projection micrograph of tissue base to medial section of a mammary epithelial duct (cyan, phalloidin) and proximal vasculature (green, phalloidin); Alexa Fluor-labeled collagen I (magenta), DAPI (blue). Top right: Representative maximum intensity micrographs of mature endothelial vessels immunostained for VE-cadherin, ZO-1, actin, and Ki67, as indicated. Bottom right: Individual confocal slice micrographs from 3D epithelial duct midsections immunostained for GM130, Ki67, α6 integrin, E-cadherin, actin, and DAPI, as is indicated in each panel. c Quantification of golgi localization as measured by the nuclear-GM130 axis ( n = 52 cells examined from three independent ducts). 0 corresponds to a nuclear-GM130 axis apically oriented toward the lumen, while 180 corresponds to a basal orientation. d Cartoon depicting morphogen gradients established by perfusing growth factors through an acellular vascular channel. Immunographs of quiescent MCF10A ducts exposed to vehicle (DMSO), FGF2 (3 nM), or TGFβ1 (5 ng/ml) gradients for three days. Inset: high magnification slice micrograph of duct terminus immunostained with phalloidin (cyan), DAPI (blue) and Ki67 (magenta). e Quantification of percentage of Ki67 positive nuclei in ducts treated with each morphogen gradient ( n = 4, 3, 3 ducts examined across three independent experiments; one-way ANOVA with Bonferroni post test Vehicle vs FGF2 ** p = 0.0036, FGF2 vs TGFβ1 ** p = 0.002, mean ± s.e.m). All images are representative of at least three independent experiments. Source Data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Uncovering mutation-specific morphogenic phenotypes and paracrine-mediated vessel dysfunction in a biomimetic vascularized mammary duct platform

    doi: 10.1038/s41467-020-17102-x

    Figure Lengend Snippet: A vascularized mammary duct platform models native 3D tissue architectures and morphogenesis. Tissues are at one week of co-culture unless otherwise indicated. a Organotypic microfluidic device consisting of an engineered 3D endothelial vessel (green) and mammary epithelial duct (cyan) in physiologic ECM (magenta), enabling long-term culture and paracrine signaling. Inset: 3D reconstruction of endothelial vessel (green—VE-cadherin) and epithelial duct (cyan—phalloidin). b Left: Composite stitched maximum intensity projection micrograph of tissue base to medial section of a mammary epithelial duct (cyan, phalloidin) and proximal vasculature (green, phalloidin); Alexa Fluor-labeled collagen I (magenta), DAPI (blue). Top right: Representative maximum intensity micrographs of mature endothelial vessels immunostained for VE-cadherin, ZO-1, actin, and Ki67, as indicated. Bottom right: Individual confocal slice micrographs from 3D epithelial duct midsections immunostained for GM130, Ki67, α6 integrin, E-cadherin, actin, and DAPI, as is indicated in each panel. c Quantification of golgi localization as measured by the nuclear-GM130 axis ( n = 52 cells examined from three independent ducts). 0 corresponds to a nuclear-GM130 axis apically oriented toward the lumen, while 180 corresponds to a basal orientation. d Cartoon depicting morphogen gradients established by perfusing growth factors through an acellular vascular channel. Immunographs of quiescent MCF10A ducts exposed to vehicle (DMSO), FGF2 (3 nM), or TGFβ1 (5 ng/ml) gradients for three days. Inset: high magnification slice micrograph of duct terminus immunostained with phalloidin (cyan), DAPI (blue) and Ki67 (magenta). e Quantification of percentage of Ki67 positive nuclei in ducts treated with each morphogen gradient ( n = 4, 3, 3 ducts examined across three independent experiments; one-way ANOVA with Bonferroni post test Vehicle vs FGF2 ** p = 0.0036, FGF2 vs TGFβ1 ** p = 0.002, mean ± s.e.m). All images are representative of at least three independent experiments. Source Data are provided as a Source Data file.

    Article Snippet: Anti-α6 integrin (MA6, 1 µg/ml) was from Millipore.

    Techniques: Co-Culture Assay, Labeling

    The post-mitotic midbody infers apical specificity to basal membranes. (A) Representative confocal images of midbodies purified from synchronized cells (+ nocodazole) spinned down over poly-l-lysine coverslips and stained with Cep-55 (magenta), MKLP-1 (green) and γ-tubulin (red) antibodies. The same procedure from non-synchronized cells (- nocodazole) led to samples that did not contain midbodies. (B) Purified midbodies (+ nocodazole) and the control sample (- nocodazole) were immunoblotted with antibodies against MKLP-1 (upper picture) and γ-tubulin (lower picture) as midbody markers to confirm the purification. (C, D) Representative images of integrin α6 (C) or ζPKC (D) (magenta) in 2D polarized MDCK cell cultures treated with the control sample without (- nocodazole) midbodies or with the sample containing ectopic midbodies (+ nocodazole) (MBs), which both were added on top or to the bottom incubated 24 h. Actin was stained with phalloidin (red) and nuclei with Hoechst (blue). Scale bars 10 μm. E-G Fluorescence ratio between the top (apical) and the bottom (basal) membrane is represented for actin (E), integrin α6 (F) and ζPKC (G). n = 100. (H, I) Representative images of cis-Golgi marker GM130 (H) and thigh junction marker ZO-1 (I) in magenta in 2D polarized MDCK cell cultures treated with the control sample without (- nocodazole) midbodies or with the sample containing ectopic midbodies (+ nocodazole), which both were added to the bottom and incubated for 24 h. Nuclei were stained with Hoechst (blue) and actin with phalloidin (red). The percentage of cells with GM130 stained cis-Golgi present between the nucleus and the apical membrane and ZO-1 stained in the upper part of the lateral membrane was calculated. n = 90. J Purified midbodies from YFP-MKLP-1 (green) overexpressing MDCK cells and a non-synchronized control preparation were spinned down over poly-l-lysine coverslips and stained against Cep-55 (magenta) and γ-tubulin (red) to confirm the purification. Right: separated channels showing YFP-MKLP-1 (up), γ-tubulin (middle up), Cep55 (middle down) and merge (down). Scale bars 10 μm. K Representative images of 2D polarized monolayer of MDCK cells where ectopic midbodies purified from YFP-MKLP1 were delivered to the bottom or top (not shown) of the layer (n = 1950). Actin was stained with phalloidin (red) and nuclei with Hoechst (blue). Scale bars 10 μm. Values represent mean plus standard deviation of 3 experiments.

    Journal: Communicative & Integrative Biology

    Article Title: Keep it on the edge: The post-mitotic midbody as a polarity signal unit

    doi: 10.1080/19420889.2017.1338990

    Figure Lengend Snippet: The post-mitotic midbody infers apical specificity to basal membranes. (A) Representative confocal images of midbodies purified from synchronized cells (+ nocodazole) spinned down over poly-l-lysine coverslips and stained with Cep-55 (magenta), MKLP-1 (green) and γ-tubulin (red) antibodies. The same procedure from non-synchronized cells (- nocodazole) led to samples that did not contain midbodies. (B) Purified midbodies (+ nocodazole) and the control sample (- nocodazole) were immunoblotted with antibodies against MKLP-1 (upper picture) and γ-tubulin (lower picture) as midbody markers to confirm the purification. (C, D) Representative images of integrin α6 (C) or ζPKC (D) (magenta) in 2D polarized MDCK cell cultures treated with the control sample without (- nocodazole) midbodies or with the sample containing ectopic midbodies (+ nocodazole) (MBs), which both were added on top or to the bottom incubated 24 h. Actin was stained with phalloidin (red) and nuclei with Hoechst (blue). Scale bars 10 μm. E-G Fluorescence ratio between the top (apical) and the bottom (basal) membrane is represented for actin (E), integrin α6 (F) and ζPKC (G). n = 100. (H, I) Representative images of cis-Golgi marker GM130 (H) and thigh junction marker ZO-1 (I) in magenta in 2D polarized MDCK cell cultures treated with the control sample without (- nocodazole) midbodies or with the sample containing ectopic midbodies (+ nocodazole), which both were added to the bottom and incubated for 24 h. Nuclei were stained with Hoechst (blue) and actin with phalloidin (red). The percentage of cells with GM130 stained cis-Golgi present between the nucleus and the apical membrane and ZO-1 stained in the upper part of the lateral membrane was calculated. n = 90. J Purified midbodies from YFP-MKLP-1 (green) overexpressing MDCK cells and a non-synchronized control preparation were spinned down over poly-l-lysine coverslips and stained against Cep-55 (magenta) and γ-tubulin (red) to confirm the purification. Right: separated channels showing YFP-MKLP-1 (up), γ-tubulin (middle up), Cep55 (middle down) and merge (down). Scale bars 10 μm. K Representative images of 2D polarized monolayer of MDCK cells where ectopic midbodies purified from YFP-MKLP1 were delivered to the bottom or top (not shown) of the layer (n = 1950). Actin was stained with phalloidin (red) and nuclei with Hoechst (blue). Scale bars 10 μm. Values represent mean plus standard deviation of 3 experiments.

    Article Snippet: Primary rat antibody used was anti-integrin α6 (1:100; Millipore).

    Techniques: Purification, Staining, Incubation, Fluorescence, Marker, Standard Deviation

    Integrin α6 subunit expression by Schlemm’s canal cells. A : Confocal immunofluorescence microscopy of outflow tissues including Schlemm’s canal (SC) from human donor eyes showing α6 integrin (INTG) levels. Shown is representative image from eye of individual human donor of 3 donor eyes that were examined. For comparison, a scleral vessel is indicated (*). B : western blot analysis of different human SC and trabecular meshwork (TM) cell strains checking for α6 integrin levels. Cell lysates were first subjected to immunoprecipition using integrin α6-specific IgGs, followed by SDS–PAGE and western blotting using IgGs that recognize both α3 and α6 INTG.

    Journal: Molecular Vision

    Article Title: Structural basement membrane components and corresponding integrins in Schlemm's canal endothelia

    doi:

    Figure Lengend Snippet: Integrin α6 subunit expression by Schlemm’s canal cells. A : Confocal immunofluorescence microscopy of outflow tissues including Schlemm’s canal (SC) from human donor eyes showing α6 integrin (INTG) levels. Shown is representative image from eye of individual human donor of 3 donor eyes that were examined. For comparison, a scleral vessel is indicated (*). B : western blot analysis of different human SC and trabecular meshwork (TM) cell strains checking for α6 integrin levels. Cell lysates were first subjected to immunoprecipition using integrin α6-specific IgGs, followed by SDS–PAGE and western blotting using IgGs that recognize both α3 and α6 INTG.

    Article Snippet: Laminin α5 was labeled with rabbit anti-Laminin α5 IgG (Santa Cruz Biotechnology, Santa Cruz, CA) diluted 1:50 in PBS and incubated overnight at 4 ⁰C, followed by incubation in Alexa-647 goat anti-rabbit IgG (Invitrogen, Austin, TX) diluted 1:150 for 3 h. Integrin α6 was labeled with rat anti-Integrin α6 (gift of Damsky Lab) diluted 1:50 in dPBS and incubated overnight at 4 °C, followed by incubation in Cy3 goat anti-rat IgG (Abcam, Cambridge, MA) diluted 1:100 in dPBS, for 3 h at RT.

    Techniques: Expressing, Immunofluorescence, Microscopy, Western Blot, SDS Page

    En face confocal immunofluorescence microscopy of Schlemm’s canal inner wall. Shown is labeling of the inner wall of SC (viewed from luminal side) for integrin α6 ( A , green), laminin α5 ( B , red), CD31 ( C , blue). Panel D is a merged image of all three proteins plus nuclei (brown). Shown is representative image from a human donor eye of 6 total eyes that were examined.

    Journal: Molecular Vision

    Article Title: Structural basement membrane components and corresponding integrins in Schlemm's canal endothelia

    doi:

    Figure Lengend Snippet: En face confocal immunofluorescence microscopy of Schlemm’s canal inner wall. Shown is labeling of the inner wall of SC (viewed from luminal side) for integrin α6 ( A , green), laminin α5 ( B , red), CD31 ( C , blue). Panel D is a merged image of all three proteins plus nuclei (brown). Shown is representative image from a human donor eye of 6 total eyes that were examined.

    Article Snippet: Laminin α5 was labeled with rabbit anti-Laminin α5 IgG (Santa Cruz Biotechnology, Santa Cruz, CA) diluted 1:50 in PBS and incubated overnight at 4 ⁰C, followed by incubation in Alexa-647 goat anti-rabbit IgG (Invitrogen, Austin, TX) diluted 1:150 for 3 h. Integrin α6 was labeled with rat anti-Integrin α6 (gift of Damsky Lab) diluted 1:50 in dPBS and incubated overnight at 4 °C, followed by incubation in Cy3 goat anti-rat IgG (Abcam, Cambridge, MA) diluted 1:100 in dPBS, for 3 h at RT.

    Techniques: Immunofluorescence, Microscopy, Labeling

    A , integrin endocytosis assay to examine the recycling α6 integrin. BV2 and iPLA-KD cells were plated on LN-coated coverslips, and an integrin endocytosis assay was performed as described under “Experimental Procedures.” In untreated BV2 and iPLA-KD cells, endocytosed α6 integrin was found predominantly in a perinuclear vesicular structure. Following ADP treatment, α6 integrin localization changed to plasma membrane or vesicles in the periphery of BV2 cells, but this change is absent in iPLA-KD cells. Scale bar , 10 μm. The ratios of fluorescence intensities in the perinuclear area and cellular periphery from 10 cells were determined and are shown in the graph. Error bars represent S.E. **, p

    Journal: The Journal of Biological Chemistry

    Article Title: Regulation of Integrin α6 Recycling by Calcium-independent Phospholipase A2 (iPLA2) to Promote Microglia Chemotaxis on Laminin *

    doi: 10.1074/jbc.M116.732610

    Figure Lengend Snippet: A , integrin endocytosis assay to examine the recycling α6 integrin. BV2 and iPLA-KD cells were plated on LN-coated coverslips, and an integrin endocytosis assay was performed as described under “Experimental Procedures.” In untreated BV2 and iPLA-KD cells, endocytosed α6 integrin was found predominantly in a perinuclear vesicular structure. Following ADP treatment, α6 integrin localization changed to plasma membrane or vesicles in the periphery of BV2 cells, but this change is absent in iPLA-KD cells. Scale bar , 10 μm. The ratios of fluorescence intensities in the perinuclear area and cellular periphery from 10 cells were determined and are shown in the graph. Error bars represent S.E. **, p

    Article Snippet: For labeling, cells were incubated for 1 h at 4 °C with a 1:200 dilution of primary antibody against α5 or α6 integrin (BD Biosciences).

    Techniques: Endocytosis Assay, Fluorescence

    A , knockdown of endogenous (mouse) α6 integrin with shRNA. The Western blot of α6 integrin in α6-KD cells shows a significant reduction of α6 integrin. B , cell adhesion/spreading assay on LN to determine whether human α6-GFP expressed in α6-KD cells is functional. A 96-well plate was coated with 3 μg/ml LN at 4 °C overnight. 1 × 10 4 cells were added to each well and incubated for a specific time period. After washing off non-attached cells, four non-overlapping images from each well were taken with a 10× objective, and the percentage of cells (% cells adhered ) that show partially or fully spread morphologies among total cells attached on the substrate after certain times of incubation was determined. 12 images in three different wells from the one culture are shown. Expression of human α6-GFP can rescue the adhesion/spreading defects of α6-KD cells. A specific iPLA 2 inhibitor, BEL, also inhibits cell adhesion/spreading on LN. Error bars represent S.E. C , localization of α6 integrin-GFP was examined with live cell imaging in cells plated on different matrix proteins. Localization of α6 integrin-GFP was observed on vesicles and membrane protrusions ( arrow ) in cells plated on FN. α6 integrin-GFP localizes to focal contacts and adhesions ( arrow ) in cells plated on LN.

    Journal: The Journal of Biological Chemistry

    Article Title: Regulation of Integrin α6 Recycling by Calcium-independent Phospholipase A2 (iPLA2) to Promote Microglia Chemotaxis on Laminin *

    doi: 10.1074/jbc.M116.732610

    Figure Lengend Snippet: A , knockdown of endogenous (mouse) α6 integrin with shRNA. The Western blot of α6 integrin in α6-KD cells shows a significant reduction of α6 integrin. B , cell adhesion/spreading assay on LN to determine whether human α6-GFP expressed in α6-KD cells is functional. A 96-well plate was coated with 3 μg/ml LN at 4 °C overnight. 1 × 10 4 cells were added to each well and incubated for a specific time period. After washing off non-attached cells, four non-overlapping images from each well were taken with a 10× objective, and the percentage of cells (% cells adhered ) that show partially or fully spread morphologies among total cells attached on the substrate after certain times of incubation was determined. 12 images in three different wells from the one culture are shown. Expression of human α6-GFP can rescue the adhesion/spreading defects of α6-KD cells. A specific iPLA 2 inhibitor, BEL, also inhibits cell adhesion/spreading on LN. Error bars represent S.E. C , localization of α6 integrin-GFP was examined with live cell imaging in cells plated on different matrix proteins. Localization of α6 integrin-GFP was observed on vesicles and membrane protrusions ( arrow ) in cells plated on FN. α6 integrin-GFP localizes to focal contacts and adhesions ( arrow ) in cells plated on LN.

    Article Snippet: For labeling, cells were incubated for 1 h at 4 °C with a 1:200 dilution of primary antibody against α5 or α6 integrin (BD Biosciences).

    Techniques: shRNA, Western Blot, Functional Assay, Incubation, Expressing, Live Cell Imaging

    Tracking of α6-GFP vesicle movements in control or iPLA 2 -KD cells by live cell imaging. A , images of cells expressing α6 integrin-GFP were acquired at 6-s intervals for 15 min, and tracks of vesicles were traced. B , six representative paths taken by vesicles carrying α6 integrin-GFP are shown. C , histograms of the velocity of α6 integrin-GFP vesicles. Trajectories for 15–20 α6-GFP vesicles from four independent movies were traced. The speed was calculated from the distance between two successive positions, and speeds of vesicles were sorted into bins by tallying how many speeds there are in each bin range. The frequency of high speeds is clearly lower in iPLA 2 -KD or BEL-treated BV2 cells.

    Journal: The Journal of Biological Chemistry

    Article Title: Regulation of Integrin α6 Recycling by Calcium-independent Phospholipase A2 (iPLA2) to Promote Microglia Chemotaxis on Laminin *

    doi: 10.1074/jbc.M116.732610

    Figure Lengend Snippet: Tracking of α6-GFP vesicle movements in control or iPLA 2 -KD cells by live cell imaging. A , images of cells expressing α6 integrin-GFP were acquired at 6-s intervals for 15 min, and tracks of vesicles were traced. B , six representative paths taken by vesicles carrying α6 integrin-GFP are shown. C , histograms of the velocity of α6 integrin-GFP vesicles. Trajectories for 15–20 α6-GFP vesicles from four independent movies were traced. The speed was calculated from the distance between two successive positions, and speeds of vesicles were sorted into bins by tallying how many speeds there are in each bin range. The frequency of high speeds is clearly lower in iPLA 2 -KD or BEL-treated BV2 cells.

    Article Snippet: For labeling, cells were incubated for 1 h at 4 °C with a 1:200 dilution of primary antibody against α5 or α6 integrin (BD Biosciences).

    Techniques: Live Cell Imaging, Expressing

    Integrin α3β1 promotes CD cell adhesion, migration, and proliferation on LM-332 and LM-511. (A) Lysates from Itgα3 −/− and Itgα3 f/f CD cells (20 μg total protein/lane) were immunoblotted for integrin β1, α3, and α6 subunits. β-actin served as a loading control. (B) Surface expression of integrin β1, α3, and α6 subunits was determined on Itgα3 −/− and Itgα3 f/f CD cells by flow cytometry using R-phycoerythrin (PE). (C) Lysates from Itgα3 −/− and Itgα3 f/f CD cells (100 μg total protein) were immunoprecipitated with anti-Itgα6 antibody or normal rabbit IgG and immunoblotted for integrin subunits β1 and β4. Adhesion (D and E), migration (F), and proliferation (G) of Itgα3 f/f and Itgα3 −/− CD cells on LM-332 and LM-511 were evaluated as described in Materials and Methods . Mean measurements ±SEM of four to six independent experiments are shown; *, p ≤ 0.05 between Itgα3 f/f and Itgα3 −/− CD cells. (H) Itgα3 f/f and Itgα3 −/− CD cells were treated with blocking anti-Itgα6 antibody and plated on LM-332. Adhesion was evaluated as described in Materials and Methods . Mean measurements ± SEM of three independent experiments are shown; *, p ≤ 0.05 between CD cells and CD cells treated with blocking anti-Itgα6 antibody.

    Journal: Molecular Biology of the Cell

    Article Title: Integrin α3β1 regulates kidney collecting duct development via TRAF6-dependent K63-linked polyubiquitination of Akt

    doi: 10.1091/mbc.E14-07-1203

    Figure Lengend Snippet: Integrin α3β1 promotes CD cell adhesion, migration, and proliferation on LM-332 and LM-511. (A) Lysates from Itgα3 −/− and Itgα3 f/f CD cells (20 μg total protein/lane) were immunoblotted for integrin β1, α3, and α6 subunits. β-actin served as a loading control. (B) Surface expression of integrin β1, α3, and α6 subunits was determined on Itgα3 −/− and Itgα3 f/f CD cells by flow cytometry using R-phycoerythrin (PE). (C) Lysates from Itgα3 −/− and Itgα3 f/f CD cells (100 μg total protein) were immunoprecipitated with anti-Itgα6 antibody or normal rabbit IgG and immunoblotted for integrin subunits β1 and β4. Adhesion (D and E), migration (F), and proliferation (G) of Itgα3 f/f and Itgα3 −/− CD cells on LM-332 and LM-511 were evaluated as described in Materials and Methods . Mean measurements ±SEM of four to six independent experiments are shown; *, p ≤ 0.05 between Itgα3 f/f and Itgα3 −/− CD cells. (H) Itgα3 f/f and Itgα3 −/− CD cells were treated with blocking anti-Itgα6 antibody and plated on LM-332. Adhesion was evaluated as described in Materials and Methods . Mean measurements ± SEM of three independent experiments are shown; *, p ≤ 0.05 between CD cells and CD cells treated with blocking anti-Itgα6 antibody.

    Article Snippet: Antibodies to integrin α6 (555734; BD Biosciences) were used in adhesion assays.

    Techniques: Migration, Expressing, Flow Cytometry, Cytometry, Immunoprecipitation, Blocking Assay

    Hoxb7Cre:Itgα3 flox/flox mice have defective UB development and decreased activation of Akt, GSK-3β, and p38 MAPK. (A–L) H E stained kidneys of WT mice (Itgα3 flox/flox ) and mice lacking integrin α3 in the UB (Hoxb7:Itgα3 flox/flox ) at various stages of development. Magnification is 40× (A–F, I, and J) and 100× (G, H, K, and L). Note the mild branching defect from E15 onward and the hypoplastic papilla, which is characterized by fewer but dilated CDs in the Hoxb7:Itgα3 flox/flox mice from E18 onward (arrows). (M) Lysates of papillae (20 μg total protein/lane) from 3-d-old Itgα3 flox/flox and Hoxb7:Itgα3 flox/flox mice were analyzed by Western blotting for levels of integrin subunits α3, α6, and β1; phospho-Akt Ser473 , phospho-GSK-3β, phospho-p38, and phospho-ERK1/2. Bands of phosphorylated and total proteins as well as β-actin (loading control) were measured by densitometry. The amount of phosphorylated proteins was normalized to total protein and β-actin levels and presented as mean ±SEM from at least three animals; *, p

    Journal: Molecular Biology of the Cell

    Article Title: Integrin α3β1 regulates kidney collecting duct development via TRAF6-dependent K63-linked polyubiquitination of Akt

    doi: 10.1091/mbc.E14-07-1203

    Figure Lengend Snippet: Hoxb7Cre:Itgα3 flox/flox mice have defective UB development and decreased activation of Akt, GSK-3β, and p38 MAPK. (A–L) H E stained kidneys of WT mice (Itgα3 flox/flox ) and mice lacking integrin α3 in the UB (Hoxb7:Itgα3 flox/flox ) at various stages of development. Magnification is 40× (A–F, I, and J) and 100× (G, H, K, and L). Note the mild branching defect from E15 onward and the hypoplastic papilla, which is characterized by fewer but dilated CDs in the Hoxb7:Itgα3 flox/flox mice from E18 onward (arrows). (M) Lysates of papillae (20 μg total protein/lane) from 3-d-old Itgα3 flox/flox and Hoxb7:Itgα3 flox/flox mice were analyzed by Western blotting for levels of integrin subunits α3, α6, and β1; phospho-Akt Ser473 , phospho-GSK-3β, phospho-p38, and phospho-ERK1/2. Bands of phosphorylated and total proteins as well as β-actin (loading control) were measured by densitometry. The amount of phosphorylated proteins was normalized to total protein and β-actin levels and presented as mean ±SEM from at least three animals; *, p

    Article Snippet: Antibodies to integrin α6 (555734; BD Biosciences) were used in adhesion assays.

    Techniques: Mouse Assay, Activation Assay, Staining, Western Blot

    Integrin α6 expression rescues KLF9-induced growth inhibition of glioma xenografts. GBM1b neurospheres were infected with lentivirus to express FLAG-KLF9, integrin α6, or both. A , immunofluorescence of neurosphere cells shows the expression

    Journal: The Journal of Biological Chemistry

    Article Title: Kruppel-like Factor-9 (KLF9) Inhibits Glioblastoma Stemness through Global Transcription Repression and Integrin α6 Inhibition *

    doi: 10.1074/jbc.M114.588988

    Figure Lengend Snippet: Integrin α6 expression rescues KLF9-induced growth inhibition of glioma xenografts. GBM1b neurospheres were infected with lentivirus to express FLAG-KLF9, integrin α6, or both. A , immunofluorescence of neurosphere cells shows the expression

    Article Snippet: The cells were immunostained with anti-FLAG (Sigma-Aldrich) and anti-integrin α6 (Cell Signaling Technology) antibodies and Hoechst 33342 nucleic acid stain (Invitrogen).

    Techniques: Expressing, Inhibition, Infection, Immunofluorescence

    KLF9 down-regulates integrin α6 by promoter binding. A , schematic of the human ITGA6 promoter with a KLF9 binding peak identified by ChIP-Seq (−25,000 to +3,000 bp relative to TSS). Primers were designed for segments A–D. B , Dox-treated

    Journal: The Journal of Biological Chemistry

    Article Title: Kruppel-like Factor-9 (KLF9) Inhibits Glioblastoma Stemness through Global Transcription Repression and Integrin α6 Inhibition *

    doi: 10.1074/jbc.M114.588988

    Figure Lengend Snippet: KLF9 down-regulates integrin α6 by promoter binding. A , schematic of the human ITGA6 promoter with a KLF9 binding peak identified by ChIP-Seq (−25,000 to +3,000 bp relative to TSS). Primers were designed for segments A–D. B , Dox-treated

    Article Snippet: The cells were immunostained with anti-FLAG (Sigma-Aldrich) and anti-integrin α6 (Cell Signaling Technology) antibodies and Hoechst 33342 nucleic acid stain (Invitrogen).

    Techniques: Binding Assay, Chromatin Immunoprecipitation

    Intravenous immunoglobulin (IVIg) prevents BP-IgG-induced type XVII collagen (COL17) depletion. DJM-1 cells (40% confluency) were treated with 1.0 mg/ml BP-IgG. Western blotting using total cell lysate was performed for anti-COL17. (A) DJM-1 cells were treated with IVIg (5–0.5–0.05–0.005 mg/ml) for 1 h followed by BP-IgG for 4 h (pretreatment). (B) DJM-1 cells were treated with BP-IgG for 4 h followed by IVIg for 1 h (posttreatment). (C) BP-IgG and IVIg were incubated in advance, and then added to the culture medium together (simultaneous). (D) DJM-1 cells were treated with appropriate controls. The amount of integrin α6, which is a transmembrane protein and a hemidesmosome component, was not changed. The representative Western blot is presented. Each experiment was performed at least three times, with p

    Journal: Frontiers in Immunology

    Article Title: Anti-idiotypic Antibodies against BP-IgG Prevent Type XVII Collagen Depletion

    doi: 10.3389/fimmu.2017.01669

    Figure Lengend Snippet: Intravenous immunoglobulin (IVIg) prevents BP-IgG-induced type XVII collagen (COL17) depletion. DJM-1 cells (40% confluency) were treated with 1.0 mg/ml BP-IgG. Western blotting using total cell lysate was performed for anti-COL17. (A) DJM-1 cells were treated with IVIg (5–0.5–0.05–0.005 mg/ml) for 1 h followed by BP-IgG for 4 h (pretreatment). (B) DJM-1 cells were treated with BP-IgG for 4 h followed by IVIg for 1 h (posttreatment). (C) BP-IgG and IVIg were incubated in advance, and then added to the culture medium together (simultaneous). (D) DJM-1 cells were treated with appropriate controls. The amount of integrin α6, which is a transmembrane protein and a hemidesmosome component, was not changed. The representative Western blot is presented. Each experiment was performed at least three times, with p

    Article Snippet: Blotting was performed using rabbit anti-COL17 (1:2,000 dilution) , rabbit anti-β-tubulin (Abcam, Tokyo, Japan, 1:20,000 dilution), and anti-integrin α6 (Santa Cruz, Dallas, TX, USA, 1:500 dilution) as the primary antibodies, followed by incubation with HRP-conjugated goat anti-rabbit or anti-mouse IgG (Life Technologies, 1:5,000 dilution).

    Techniques: Western Blot, Incubation

    GIPC1 is required for NRP-1 coupling to downstream signaling events. a GIPC1 is elevated in ECS cells. Extracts were prepared from SCC-13 non-stem cancer cells (monolayer) and ECS cells (5-day spheroids) for detection of GIPC1. b, c NRP-1/α6-integrin/GIPC1

    Journal: Oncogene

    Article Title: NRP-1 interacts with GIPC1 and α6/β4-integrins to increase YAP1/ΔNp63α-dependent epidermal cancer stem cell survival

    doi: 10.1038/s41388-018-0290-4

    Figure Lengend Snippet: GIPC1 is required for NRP-1 coupling to downstream signaling events. a GIPC1 is elevated in ECS cells. Extracts were prepared from SCC-13 non-stem cancer cells (monolayer) and ECS cells (5-day spheroids) for detection of GIPC1. b, c NRP-1/α6-integrin/GIPC1

    Article Snippet: Antibodies to GIPC1 (sc-9648), β4-integrin (sc-9090), α6-integrin (sc-374057), and p63 (sc-8431) were obtained from Santa Cruz (Dallas, TX).

    Techniques:

    FKBP10 promotes adhesion of GC cells (A) FKBP10 protein expression in gastric cancer cell line and GES-1. ( B ) and ( C ) FKBP10 mRNA and protein expression levels were tested by qRT-PCR and Western blot analysis in HGC-27 and MKN-7 cells after transfected with siFKBP10 for 48 hours. ( D ) Adhesion assay was used to detect changes in adhesion ability of HGC-27 and MKN-7 cells after transfected with siFKBP10 for 48 hours. ( E ) Quantifications of cells are shown as proportions of the number of control cells. Original magnification, 200×. Scale bar: 100 µM. ( F ) and ( G ) Integrin α1, integrin α2, integrin α5, integrin αV, integrin α6, AKT, P-AKT 308, P-AKT 473 proteins were detected by Western blot analysis in HGC-27 and MKN-7 cells after transfected with siFKBP10 for 48 hours. β-actin was used as a loading control in Western blot.(*P

    Journal: OncoTargets and therapy

    Article Title: FKBP10 Acts as a New Biomarker for Prognosis and Lymph Node Metastasis of Gastric Cancer by Bioinformatics Analysis and in Vitro Experiments

    doi: 10.2147/OTT.S253154

    Figure Lengend Snippet: FKBP10 promotes adhesion of GC cells (A) FKBP10 protein expression in gastric cancer cell line and GES-1. ( B ) and ( C ) FKBP10 mRNA and protein expression levels were tested by qRT-PCR and Western blot analysis in HGC-27 and MKN-7 cells after transfected with siFKBP10 for 48 hours. ( D ) Adhesion assay was used to detect changes in adhesion ability of HGC-27 and MKN-7 cells after transfected with siFKBP10 for 48 hours. ( E ) Quantifications of cells are shown as proportions of the number of control cells. Original magnification, 200×. Scale bar: 100 µM. ( F ) and ( G ) Integrin α1, integrin α2, integrin α5, integrin αV, integrin α6, AKT, P-AKT 308, P-AKT 473 proteins were detected by Western blot analysis in HGC-27 and MKN-7 cells after transfected with siFKBP10 for 48 hours. β-actin was used as a loading control in Western blot.(*P

    Article Snippet: Anti-integrin α6 (ab97760,1:500) was purchased from Abcam (Cambridge, MA, USA).

    Techniques: Expressing, Quantitative RT-PCR, Western Blot, Transfection, Cell Adhesion Assay

    Effect of laminin isoforms on limbal progenitor cell adhesion and migration. ( A ) The effect of laminin (LN) isoforms on cell adhesion was tested by seeding limbal epithelial progenitor cells (LEPC) at a density of 50,000 cells/cm 2 and spectrophotometric measurement of adherent cells 30 and 60 minutes after seeding. Data are expressed as means ± SEM (n = 4). ( B ) Phase contrast images of LEPC cultured on LN isoforms; magnification ×100. ( C ) Flow cytometry analyses of cultured LEPC showing expression of integrin α3 (ITGA3), integrin α6 (ITGA6), integrin β1 (ITGB1), and integrin β4 (ITGB4) on their surface. Percentages (%) of positive cells are expressed as means ± SEM percentage (%) (n = 3). ( D ) Functional blocking of integrin-mediated LEPC adhesion to LN-521, -511, -511-E8 and -332 was tested using neutralizing antibodies against integrin α3β1 and α6β1 60 minutes seeding. Data are expressed as means ± SEM (n = 4). ( E ) The effect of LN isoforms on LEPC migration was analyzed in two well-culture inserts with a defined cell-free gap and measurement of gap closure 3 and 6 hours after removal of the culture inserts. Data are expressed as means ± SEM (n = 3); *p

    Journal: Scientific Reports

    Article Title: Laminin-511 and -521-based matrices for efficient ex vivo-expansion of human limbal epithelial progenitor cells

    doi: 10.1038/s41598-017-04916-x

    Figure Lengend Snippet: Effect of laminin isoforms on limbal progenitor cell adhesion and migration. ( A ) The effect of laminin (LN) isoforms on cell adhesion was tested by seeding limbal epithelial progenitor cells (LEPC) at a density of 50,000 cells/cm 2 and spectrophotometric measurement of adherent cells 30 and 60 minutes after seeding. Data are expressed as means ± SEM (n = 4). ( B ) Phase contrast images of LEPC cultured on LN isoforms; magnification ×100. ( C ) Flow cytometry analyses of cultured LEPC showing expression of integrin α3 (ITGA3), integrin α6 (ITGA6), integrin β1 (ITGB1), and integrin β4 (ITGB4) on their surface. Percentages (%) of positive cells are expressed as means ± SEM percentage (%) (n = 3). ( D ) Functional blocking of integrin-mediated LEPC adhesion to LN-521, -511, -511-E8 and -332 was tested using neutralizing antibodies against integrin α3β1 and α6β1 60 minutes seeding. Data are expressed as means ± SEM (n = 4). ( E ) The effect of LN isoforms on LEPC migration was analyzed in two well-culture inserts with a defined cell-free gap and measurement of gap closure 3 and 6 hours after removal of the culture inserts. Data are expressed as means ± SEM (n = 3); *p

    Article Snippet: The effect of an interaction between cellular integrins and extracellular LNs on cell adhesion was evaluated by seeding LEPC (50,000 cells/cm2 ) in 96-well plates coated with recombinant LN-332, -511, -521, and LN-511-E8 in the presence or absence of integrin-neutralizing antibodies, i.e., anti-α3 integrin (20 µg/ml) (Merck Millipore, Darmstadt, Germany), anti-α6 integrin (20 µg/ml) (Merck Millipore) and anti-β1 integrin (2.5 µg/ml) (R & D Systems Inc., Minneapolis, MN, USA).

    Techniques: Migration, Cell Culture, Flow Cytometry, Cytometry, Expressing, Functional Assay, Blocking Assay

    Tissue engineering of corneal epithelial constructs. ( A ) Phase contrast images of limbal epithelial progenitor cells (LEPC) growing on fibrin gels without or with incorporated recombinant laminin (LN)-511-E8 for 5 days (magnification ×100). ( B ) Light micrographs of epithelial cell sheets after two weeks of LEPC culture on fibrin gels without or with incorporated LN-511-E8 (i, periodic acid-Schiff staining; ii, hematoxylin-eosin staining; scale bar = 25 µm). ( C ) Transmission electron micrographs of epithelial cell sheets after two weeks of LEPC culture on fibrin gels (FG) without or with incorporated LN-511-E8; formation of hemidesmosomes (arrows) and basement membrane (arrowheads) can be seen on LN-511-E8 containing gels (scale bar = 5 µm in i, and 1 µm in ii). ( D ) Immunofluorescence analysis of epithelial constructs showing expression patterns of cytokeratin (CK)3, CK15, p63α, integrin α6, integrin ß1, and LN-α5 in epithelial constructs established on LN-511-E8 containing gels and bare fibrin gels (nuclear counterstaining with DAPI (blue); scale bar = 25 µm).

    Journal: Scientific Reports

    Article Title: Laminin-511 and -521-based matrices for efficient ex vivo-expansion of human limbal epithelial progenitor cells

    doi: 10.1038/s41598-017-04916-x

    Figure Lengend Snippet: Tissue engineering of corneal epithelial constructs. ( A ) Phase contrast images of limbal epithelial progenitor cells (LEPC) growing on fibrin gels without or with incorporated recombinant laminin (LN)-511-E8 for 5 days (magnification ×100). ( B ) Light micrographs of epithelial cell sheets after two weeks of LEPC culture on fibrin gels without or with incorporated LN-511-E8 (i, periodic acid-Schiff staining; ii, hematoxylin-eosin staining; scale bar = 25 µm). ( C ) Transmission electron micrographs of epithelial cell sheets after two weeks of LEPC culture on fibrin gels (FG) without or with incorporated LN-511-E8; formation of hemidesmosomes (arrows) and basement membrane (arrowheads) can be seen on LN-511-E8 containing gels (scale bar = 5 µm in i, and 1 µm in ii). ( D ) Immunofluorescence analysis of epithelial constructs showing expression patterns of cytokeratin (CK)3, CK15, p63α, integrin α6, integrin ß1, and LN-α5 in epithelial constructs established on LN-511-E8 containing gels and bare fibrin gels (nuclear counterstaining with DAPI (blue); scale bar = 25 µm).

    Article Snippet: The effect of an interaction between cellular integrins and extracellular LNs on cell adhesion was evaluated by seeding LEPC (50,000 cells/cm2 ) in 96-well plates coated with recombinant LN-332, -511, -521, and LN-511-E8 in the presence or absence of integrin-neutralizing antibodies, i.e., anti-α3 integrin (20 µg/ml) (Merck Millipore, Darmstadt, Germany), anti-α6 integrin (20 µg/ml) (Merck Millipore) and anti-β1 integrin (2.5 µg/ml) (R & D Systems Inc., Minneapolis, MN, USA).

    Techniques: Construct, Recombinant, Staining, Transmission Assay, Immunofluorescence, Expressing

    Genetic signature of TPA treated and expanded epidermis. a , Representative FACS plots showing the strategy used to isolate basal cells. Single living cells were gated by debris exclusion (P1), DAPI exclusion (P2), doublet elimination (P3) and basal IFE Integrin-α6 high CD34 neg cell were sorted (P4). n=10 independent experiments. b, c , mRNA expression of genes that were upregulated in basal cells at EXP D4 (n = 3) and in cells treated with TPA (n = 2). These genes are related to a generic stress signature (b) , regulating ECM remodeling and cytoskeleton, important for cell survival and cell cycle (c). Bars are mean with s.e.m. d , Representative images of Paxillin immunostaining color-coded for the signal intensity with ImageJ. Protein expression is visualized as a color gradient going from black to yellow with black as indicator of no expression and yellow as indicator of maximal expression. Scale bar, 10 μm e , Quantification of the average integrated density signal for Paxillin as in d. Each data point is the average of 3 sections per mouse (n = 3 mice per condition). f , Geometric mean fluorescence intensity for the indicated integrin in CTRL (grey, n = 4 mice) and EXP D4 (red, n = 6 mice) from FACS analysis of basal IFE Integrin-α6 high CD34 neg cells. g-k , ATAC-seq profiles showing increasing accessibility of chromatin regions that are specifically remodeled during mechanical expansion (CTRL in grey and EXP D2 in orange). l , Quantification of the number of cells FOSL1+ in the basal layer related to . m , Immunostaining on skin sections for c-JUN (white) in control and EXP D4. n , Quantification of the number of cells c-JUN+ in the basal layer related to m. o . p . q , Immunohistochemistry on paraffin sections for c-FOS in control and EXPD4. Scale bar, 20 μm. r , Quantification of the number of cells c-FOSL+ in the basal layer related to q. s , Immunofluorescence on tissue sections for pSTAT3 in green and K14 (red) to identified the epidermis. Scale bar, 20 μm. t , Quantification of the number of cells positive for pSTAT3 in the basal layer related to s. l, n, o, p, r, t , 3 sections quantified per n = number of mice and total number of cells indicated in parentheses d, m, q, s , Dashed lines delineate the basal lamina. e, f, l, n, o, p, r, t , Two-tailed Mann–Whitney test, Mean + s.e.m. Fig. 3d

    Journal: Nature

    Article Title: Mechanisms of stretch-mediated skin expansion at single-cell resolution

    doi: 10.1038/s41586-020-2555-7

    Figure Lengend Snippet: Genetic signature of TPA treated and expanded epidermis. a , Representative FACS plots showing the strategy used to isolate basal cells. Single living cells were gated by debris exclusion (P1), DAPI exclusion (P2), doublet elimination (P3) and basal IFE Integrin-α6 high CD34 neg cell were sorted (P4). n=10 independent experiments. b, c , mRNA expression of genes that were upregulated in basal cells at EXP D4 (n = 3) and in cells treated with TPA (n = 2). These genes are related to a generic stress signature (b) , regulating ECM remodeling and cytoskeleton, important for cell survival and cell cycle (c). Bars are mean with s.e.m. d , Representative images of Paxillin immunostaining color-coded for the signal intensity with ImageJ. Protein expression is visualized as a color gradient going from black to yellow with black as indicator of no expression and yellow as indicator of maximal expression. Scale bar, 10 μm e , Quantification of the average integrated density signal for Paxillin as in d. Each data point is the average of 3 sections per mouse (n = 3 mice per condition). f , Geometric mean fluorescence intensity for the indicated integrin in CTRL (grey, n = 4 mice) and EXP D4 (red, n = 6 mice) from FACS analysis of basal IFE Integrin-α6 high CD34 neg cells. g-k , ATAC-seq profiles showing increasing accessibility of chromatin regions that are specifically remodeled during mechanical expansion (CTRL in grey and EXP D2 in orange). l , Quantification of the number of cells FOSL1+ in the basal layer related to . m , Immunostaining on skin sections for c-JUN (white) in control and EXP D4. n , Quantification of the number of cells c-JUN+ in the basal layer related to m. o . p . q , Immunohistochemistry on paraffin sections for c-FOS in control and EXPD4. Scale bar, 20 μm. r , Quantification of the number of cells c-FOSL+ in the basal layer related to q. s , Immunofluorescence on tissue sections for pSTAT3 in green and K14 (red) to identified the epidermis. Scale bar, 20 μm. t , Quantification of the number of cells positive for pSTAT3 in the basal layer related to s. l, n, o, p, r, t , 3 sections quantified per n = number of mice and total number of cells indicated in parentheses d, m, q, s , Dashed lines delineate the basal lamina. e, f, l, n, o, p, r, t , Two-tailed Mann–Whitney test, Mean + s.e.m. Fig. 3d

    Article Snippet: Basal IFE and infundibulum cells were stained using PEconjugated anti-α6-integrin (clone GoH3, 1:200, ebioscience) or FITC- conjugated anti-α6-integrin (clone GoH3, 1:200, ebioscience) and bulge cells were stained with biotinylated CD34 (clone RAM34; 1:50, BD Biosciences).

    Techniques: FACS, Expressing, Immunostaining, Mouse Assay, Fluorescence, Immunohistochemistry, Immunofluorescence, Two Tailed Test, MANN-WHITNEY

    α6-integrin is required for inhibition of Rac1b membrane localization and induction of EMT. (a–f) Immunofluorescence images of cells cotransfected with YFP-Rac1b and a scrambled shRNA or shα6 cultured on TCPS and on lrECM. Arrows

    Journal: Differentiation; research in biological diversity

    Article Title: Extracellular matrix proteins regulate epithelial-mesenchymal transition in mammary epithelial cells

    doi: 10.1016/j.diff.2013.03.003

    Figure Lengend Snippet: α6-integrin is required for inhibition of Rac1b membrane localization and induction of EMT. (a–f) Immunofluorescence images of cells cotransfected with YFP-Rac1b and a scrambled shRNA or shα6 cultured on TCPS and on lrECM. Arrows

    Article Snippet: shRNAs targeting the Mus musculus sequences of α5-integrin ( ) and α6-integrin ( ) were obtained from Open Biosystems ( ).

    Techniques: Inhibition, Immunofluorescence, shRNA, Cell Culture

    Expression of α6-integrin is required for the inhibition of MMP3-induced EMT by lrECM. (a) Quantification of shRNA-mediated knockdown of α6-integrin as determined by RT-PCR. (b) Relative levels of α6-integrin in control and shα6-expressing

    Journal: Differentiation; research in biological diversity

    Article Title: Extracellular matrix proteins regulate epithelial-mesenchymal transition in mammary epithelial cells

    doi: 10.1016/j.diff.2013.03.003

    Figure Lengend Snippet: Expression of α6-integrin is required for the inhibition of MMP3-induced EMT by lrECM. (a) Quantification of shRNA-mediated knockdown of α6-integrin as determined by RT-PCR. (b) Relative levels of α6-integrin in control and shα6-expressing

    Article Snippet: shRNAs targeting the Mus musculus sequences of α5-integrin ( ) and α6-integrin ( ) were obtained from Open Biosystems ( ).

    Techniques: Expressing, Inhibition, shRNA, Reverse Transcription Polymerase Chain Reaction

    Ectopic expression of α6-integrin blocks induction of Snail1, but has no effect on other markers of EMT. (a) Relative levels of α6-integrin in control and transfected cells, as determined by immunoblot analysis. (b) Quantification of mRNA

    Journal: Differentiation; research in biological diversity

    Article Title: Extracellular matrix proteins regulate epithelial-mesenchymal transition in mammary epithelial cells

    doi: 10.1016/j.diff.2013.03.003

    Figure Lengend Snippet: Ectopic expression of α6-integrin blocks induction of Snail1, but has no effect on other markers of EMT. (a) Relative levels of α6-integrin in control and transfected cells, as determined by immunoblot analysis. (b) Quantification of mRNA

    Article Snippet: shRNAs targeting the Mus musculus sequences of α5-integrin ( ) and α6-integrin ( ) were obtained from Open Biosystems ( ).

    Techniques: Expressing, Transfection

    NF B cells express laminin α5 binding integrins and show some colocalization with laminin α5 in the MZ. ( A ) Representative flow cytometry for cell surface integrin expression on NF B cells with antibody isotype controls shown in gray. ( B ) In vitro adhesion of MZ, FO, and NF B cells to VCAM-1, laminin 511/521, the RGD-containing laminin α5 domain IVa, agrin, fibronectin (all 30 μM), or BSA. Adhesion of NF B cells to VCAM-1, laminin 511/521, or fibronectin was measured in the presence or absence of function blocking antibodies to integrins β1 (Ha2/5), α6 (GoH3), or α4 (PS/2). Data shown are mean values ± SEM from three separate experiments with n = 6 for each treatment in each experiment. ( C ) Immunofluorescence staining shows the presence of IgM + CD21 low and ( D ) IgM + AA4.1 + B cells in the MZ of mature mice (arrowheads). Magnification, 100× ( D , Left ), 200× ( C , Upper ), 400× ( C, Lower , and D, Right ). ( E ) In vivo localization of ex vivo TAMRA-labeled NF B cells or FO B cells (isolated from day 10 mouse spleens) at 16 h after i.v injection into mature mice in the presence or absence of GoH3. Immunofluorescent staining for laminin α5 reveals localization of NF B cells in the MZ (double arrows), follicle, and RP, whereas FO B cells home predominantly to the follicle. Coinjection with GoH3 reduced TAMRA + NF B-cell localization to the MZ only. Magnification: 100×. Bar graph shows quantification of the ratio of MZ/FO localized TAMRA + cells; data are means ± SEM from two experiments with four mice in each category. * P

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Extracellular matrix of secondary lymphoid organs impacts on B-cell fate and survival

    doi: 10.1073/pnas.1218131110

    Figure Lengend Snippet: NF B cells express laminin α5 binding integrins and show some colocalization with laminin α5 in the MZ. ( A ) Representative flow cytometry for cell surface integrin expression on NF B cells with antibody isotype controls shown in gray. ( B ) In vitro adhesion of MZ, FO, and NF B cells to VCAM-1, laminin 511/521, the RGD-containing laminin α5 domain IVa, agrin, fibronectin (all 30 μM), or BSA. Adhesion of NF B cells to VCAM-1, laminin 511/521, or fibronectin was measured in the presence or absence of function blocking antibodies to integrins β1 (Ha2/5), α6 (GoH3), or α4 (PS/2). Data shown are mean values ± SEM from three separate experiments with n = 6 for each treatment in each experiment. ( C ) Immunofluorescence staining shows the presence of IgM + CD21 low and ( D ) IgM + AA4.1 + B cells in the MZ of mature mice (arrowheads). Magnification, 100× ( D , Left ), 200× ( C , Upper ), 400× ( C, Lower , and D, Right ). ( E ) In vivo localization of ex vivo TAMRA-labeled NF B cells or FO B cells (isolated from day 10 mouse spleens) at 16 h after i.v injection into mature mice in the presence or absence of GoH3. Immunofluorescent staining for laminin α5 reveals localization of NF B cells in the MZ (double arrows), follicle, and RP, whereas FO B cells home predominantly to the follicle. Coinjection with GoH3 reduced TAMRA + NF B-cell localization to the MZ only. Magnification: 100×. Bar graph shows quantification of the ratio of MZ/FO localized TAMRA + cells; data are means ± SEM from two experiments with four mice in each category. * P

    Article Snippet: Coverslips were coated overnight at 4 °C with BSA, BAFF, agrin, VCAM, or laminin 511 alone (3 µM), or laminin 511 to which BAFF was subsequently bound by incubation at room temperature for 2 h. NF B cells (1 × 106 ) from WT or TACI−/− mice were added and incubated at 37 °C for 2 h. After washing, coverslips were fixed in 4% PFA, blocked with 2% BSA, and stained with anti-integrin α6, GoH3 (1 µg/mL), and anti-BAFF receptor (anti-CD268, clone ebio7H22-E16; eBioscience, 1 µg/mL).

    Techniques: Binding Assay, Flow Cytometry, Cytometry, Expressing, In Vitro, Blocking Assay, Immunofluorescence, Staining, Mouse Assay, In Vivo, Ex Vivo, Labeling, Isolation, Injection