integrin α6β4 Search Results


mouse anti-integrin α6β4  (Becton Dickinson)
90
Becton Dickinson mouse anti-integrin α6β4
Mouse Anti Integrin α6β4, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/integrin+%CE%B16%CE%B24/mouse+anti+integrin+%CE%B16%CE%B24/pmc10293300-319-41-44
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mouse anti-integrin α6β4 - by Bioz Stars, 2026-09
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α6β4 integrin mab1964 antibody  (Merck KGaA)
90
Merck KGaA α6β4 integrin mab1964 antibody
MMP-8 expression alters <t>α6β4</t> subcellular distribution and myoepithelial cell morphology. a (i) Confocal images of β6-1089 cells transfected with empty vector ( EMPTY ) wild-type matrix metalloproteinase-8 ( MMP-8 WT ) or inactive mutant MMP-8 ( EA ) and grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( red ) and plectin ( green ). Insert: cartoon illustrating hemidesmosome ( HD ) components, indicating the <t>integrin</t> α6β4 associates with plectin to link the complex to the keratin cytoskeleton. (ii) Co-localisation of α6β4 and plectin was determined by quantifying the number of yellow pixels per field of view in each condition then expressed as a ratio as compared to EMPTY. β6-1089 transfected with WT demonstrated a significant increase in α6β4 and plectin co-localisation, while the β6-1089 transfected with EA exhibited no change as compared to EMPTY. b (i) Confocal images of β6-1089 cells transfected with empty vector (EMPTY) wild-type MMP-8 (WT) or inactive mutant MMP-8 (EA) and grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( green ) and phallodin ( red ). (ii) Morphological features of the transfected β6-1089 were analysed and length of trailing fibres was noted to be altered. Analysis of the length of these fibres indicated that β6-1089 transfected with MMP-8 WT significantly reduced the fibre length as compared to β6-1089 transfected with empty vector or MMP-8 EA. (iii) Analysis of the number of these fibres per cell also demonstrated a significant reduction in β6-1089 transfected with MMP-8 WT as compared to β6-1089 transfected with empty vector or MMP-8 EA. (iv) The final morphological alteration analysed was the physical space the cells occupied, the relative area occupied by β6-1089 transfected with MMP-8 WT was significantly larger than that occupied by β6-1089 transfected with empty vector or MMP-8 EA. c (i) Confocal images of N-1089 cells transfected with siRNA targeting MMP-8 ( siMMP-8 ) or Luciferase ( siLuc ) as a control grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( green ) and phallodin ( red ). (ii) Trailing fibre length was significantly longer in N-1089 transfected with siMMP8 as compared to siLUC. (iii) There were significantly more trailing fibres per cell in the N-1089 + siMMP8 group as compared to N-1089 transfected with siLUC. * p = 0.05 ** p = 0.01, *** p = 0.001 (Student’s t test). Error bars = SEM, n = 3 independent experiments
α6β4 Integrin Mab1964 Antibody, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/integrin+%CE%B16%CE%B24/%CE%B16%CE%B24+integrin+mab1964+antibody/pmc05363009-150-4-6
Average 90 stars, based on 1 article reviews
α6β4 integrin mab1964 antibody - by Bioz Stars, 2026-09
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integrins α6β1 and α6β4  (The Company of Biologists)
90
The Company of Biologists integrins α6β1 and α6β4
MMP-8 expression alters <t>α6β4</t> subcellular distribution and myoepithelial cell morphology. a (i) Confocal images of β6-1089 cells transfected with empty vector ( EMPTY ) wild-type matrix metalloproteinase-8 ( MMP-8 WT ) or inactive mutant MMP-8 ( EA ) and grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( red ) and plectin ( green ). Insert: cartoon illustrating hemidesmosome ( HD ) components, indicating the <t>integrin</t> α6β4 associates with plectin to link the complex to the keratin cytoskeleton. (ii) Co-localisation of α6β4 and plectin was determined by quantifying the number of yellow pixels per field of view in each condition then expressed as a ratio as compared to EMPTY. β6-1089 transfected with WT demonstrated a significant increase in α6β4 and plectin co-localisation, while the β6-1089 transfected with EA exhibited no change as compared to EMPTY. b (i) Confocal images of β6-1089 cells transfected with empty vector (EMPTY) wild-type MMP-8 (WT) or inactive mutant MMP-8 (EA) and grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( green ) and phallodin ( red ). (ii) Morphological features of the transfected β6-1089 were analysed and length of trailing fibres was noted to be altered. Analysis of the length of these fibres indicated that β6-1089 transfected with MMP-8 WT significantly reduced the fibre length as compared to β6-1089 transfected with empty vector or MMP-8 EA. (iii) Analysis of the number of these fibres per cell also demonstrated a significant reduction in β6-1089 transfected with MMP-8 WT as compared to β6-1089 transfected with empty vector or MMP-8 EA. (iv) The final morphological alteration analysed was the physical space the cells occupied, the relative area occupied by β6-1089 transfected with MMP-8 WT was significantly larger than that occupied by β6-1089 transfected with empty vector or MMP-8 EA. c (i) Confocal images of N-1089 cells transfected with siRNA targeting MMP-8 ( siMMP-8 ) or Luciferase ( siLuc ) as a control grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( green ) and phallodin ( red ). (ii) Trailing fibre length was significantly longer in N-1089 transfected with siMMP8 as compared to siLUC. (iii) There were significantly more trailing fibres per cell in the N-1089 + siMMP8 group as compared to N-1089 transfected with siLUC. * p = 0.05 ** p = 0.01, *** p = 0.001 (Student’s t test). Error bars = SEM, n = 3 independent experiments
Integrins α6β1 And α6β4, supplied by The Company of Biologists, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/integrin+%CE%B16%CE%B24/integrins+%CE%B16%CE%B21+and+%CE%B16%CE%B24/pm10433923-27-24-14
Average 90 stars, based on 1 article reviews
integrins α6β1 and α6β4 - by Bioz Stars, 2026-09
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rat monoclonal anti-integrin α6β4 antibody  (Immunotec inc)
90
Immunotec inc rat monoclonal anti-integrin α6β4 antibody
MMP-8 expression alters <t>α6β4</t> subcellular distribution and myoepithelial cell morphology. a (i) Confocal images of β6-1089 cells transfected with empty vector ( EMPTY ) wild-type matrix metalloproteinase-8 ( MMP-8 WT ) or inactive mutant MMP-8 ( EA ) and grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( red ) and plectin ( green ). Insert: cartoon illustrating hemidesmosome ( HD ) components, indicating the <t>integrin</t> α6β4 associates with plectin to link the complex to the keratin cytoskeleton. (ii) Co-localisation of α6β4 and plectin was determined by quantifying the number of yellow pixels per field of view in each condition then expressed as a ratio as compared to EMPTY. β6-1089 transfected with WT demonstrated a significant increase in α6β4 and plectin co-localisation, while the β6-1089 transfected with EA exhibited no change as compared to EMPTY. b (i) Confocal images of β6-1089 cells transfected with empty vector (EMPTY) wild-type MMP-8 (WT) or inactive mutant MMP-8 (EA) and grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( green ) and phallodin ( red ). (ii) Morphological features of the transfected β6-1089 were analysed and length of trailing fibres was noted to be altered. Analysis of the length of these fibres indicated that β6-1089 transfected with MMP-8 WT significantly reduced the fibre length as compared to β6-1089 transfected with empty vector or MMP-8 EA. (iii) Analysis of the number of these fibres per cell also demonstrated a significant reduction in β6-1089 transfected with MMP-8 WT as compared to β6-1089 transfected with empty vector or MMP-8 EA. (iv) The final morphological alteration analysed was the physical space the cells occupied, the relative area occupied by β6-1089 transfected with MMP-8 WT was significantly larger than that occupied by β6-1089 transfected with empty vector or MMP-8 EA. c (i) Confocal images of N-1089 cells transfected with siRNA targeting MMP-8 ( siMMP-8 ) or Luciferase ( siLuc ) as a control grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( green ) and phallodin ( red ). (ii) Trailing fibre length was significantly longer in N-1089 transfected with siMMP8 as compared to siLUC. (iii) There were significantly more trailing fibres per cell in the N-1089 + siMMP8 group as compared to N-1089 transfected with siLUC. * p = 0.05 ** p = 0.01, *** p = 0.001 (Student’s t test). Error bars = SEM, n = 3 independent experiments
Rat Monoclonal Anti Integrin α6β4 Antibody, supplied by Immunotec inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/integrin+%CE%B16%CE%B24/rat+monoclonal+anti+integrin+%CE%B16%CE%B24+antibody/pm17522999-50-0-10
Average 90 stars, based on 1 article reviews
rat monoclonal anti-integrin α6β4 antibody - by Bioz Stars, 2026-09
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exosomal integrins α6β4  (Exosome Diagnostics)
86
Exosome Diagnostics exosomal integrins α6β4
MMP-8 expression alters <t>α6β4</t> subcellular distribution and myoepithelial cell morphology. a (i) Confocal images of β6-1089 cells transfected with empty vector ( EMPTY ) wild-type matrix metalloproteinase-8 ( MMP-8 WT ) or inactive mutant MMP-8 ( EA ) and grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( red ) and plectin ( green ). Insert: cartoon illustrating hemidesmosome ( HD ) components, indicating the <t>integrin</t> α6β4 associates with plectin to link the complex to the keratin cytoskeleton. (ii) Co-localisation of α6β4 and plectin was determined by quantifying the number of yellow pixels per field of view in each condition then expressed as a ratio as compared to EMPTY. β6-1089 transfected with WT demonstrated a significant increase in α6β4 and plectin co-localisation, while the β6-1089 transfected with EA exhibited no change as compared to EMPTY. b (i) Confocal images of β6-1089 cells transfected with empty vector (EMPTY) wild-type MMP-8 (WT) or inactive mutant MMP-8 (EA) and grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( green ) and phallodin ( red ). (ii) Morphological features of the transfected β6-1089 were analysed and length of trailing fibres was noted to be altered. Analysis of the length of these fibres indicated that β6-1089 transfected with MMP-8 WT significantly reduced the fibre length as compared to β6-1089 transfected with empty vector or MMP-8 EA. (iii) Analysis of the number of these fibres per cell also demonstrated a significant reduction in β6-1089 transfected with MMP-8 WT as compared to β6-1089 transfected with empty vector or MMP-8 EA. (iv) The final morphological alteration analysed was the physical space the cells occupied, the relative area occupied by β6-1089 transfected with MMP-8 WT was significantly larger than that occupied by β6-1089 transfected with empty vector or MMP-8 EA. c (i) Confocal images of N-1089 cells transfected with siRNA targeting MMP-8 ( siMMP-8 ) or Luciferase ( siLuc ) as a control grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( green ) and phallodin ( red ). (ii) Trailing fibre length was significantly longer in N-1089 transfected with siMMP8 as compared to siLUC. (iii) There were significantly more trailing fibres per cell in the N-1089 + siMMP8 group as compared to N-1089 transfected with siLUC. * p = 0.05 ** p = 0.01, *** p = 0.001 (Student’s t test). Error bars = SEM, n = 3 independent experiments
Exosomal Integrins α6β4, supplied by Exosome Diagnostics, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/integrin+%CE%B16%CE%B24/exosomal+integrins+%CE%B16%CE%B24/pm38750233-195-10-0
Average 86 stars, based on 1 article reviews
exosomal integrins α6β4 - by Bioz Stars, 2026-09
86/100 stars
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Image Search Results


MMP-8 expression alters α6β4 subcellular distribution and myoepithelial cell morphology. a (i) Confocal images of β6-1089 cells transfected with empty vector ( EMPTY ) wild-type matrix metalloproteinase-8 ( MMP-8 WT ) or inactive mutant MMP-8 ( EA ) and grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( red ) and plectin ( green ). Insert: cartoon illustrating hemidesmosome ( HD ) components, indicating the integrin α6β4 associates with plectin to link the complex to the keratin cytoskeleton. (ii) Co-localisation of α6β4 and plectin was determined by quantifying the number of yellow pixels per field of view in each condition then expressed as a ratio as compared to EMPTY. β6-1089 transfected with WT demonstrated a significant increase in α6β4 and plectin co-localisation, while the β6-1089 transfected with EA exhibited no change as compared to EMPTY. b (i) Confocal images of β6-1089 cells transfected with empty vector (EMPTY) wild-type MMP-8 (WT) or inactive mutant MMP-8 (EA) and grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( green ) and phallodin ( red ). (ii) Morphological features of the transfected β6-1089 were analysed and length of trailing fibres was noted to be altered. Analysis of the length of these fibres indicated that β6-1089 transfected with MMP-8 WT significantly reduced the fibre length as compared to β6-1089 transfected with empty vector or MMP-8 EA. (iii) Analysis of the number of these fibres per cell also demonstrated a significant reduction in β6-1089 transfected with MMP-8 WT as compared to β6-1089 transfected with empty vector or MMP-8 EA. (iv) The final morphological alteration analysed was the physical space the cells occupied, the relative area occupied by β6-1089 transfected with MMP-8 WT was significantly larger than that occupied by β6-1089 transfected with empty vector or MMP-8 EA. c (i) Confocal images of N-1089 cells transfected with siRNA targeting MMP-8 ( siMMP-8 ) or Luciferase ( siLuc ) as a control grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( green ) and phallodin ( red ). (ii) Trailing fibre length was significantly longer in N-1089 transfected with siMMP8 as compared to siLUC. (iii) There were significantly more trailing fibres per cell in the N-1089 + siMMP8 group as compared to N-1089 transfected with siLUC. * p = 0.05 ** p = 0.01, *** p = 0.001 (Student’s t test). Error bars = SEM, n = 3 independent experiments

Journal: Breast Cancer Research : BCR

Article Title: Loss of MMP-8 in ductal carcinoma in situ (DCIS)-associated myoepithelial cells contributes to tumour promotion through altered adhesive and proteolytic function

doi: 10.1186/s13058-017-0822-9

Figure Lengend Snippet: MMP-8 expression alters α6β4 subcellular distribution and myoepithelial cell morphology. a (i) Confocal images of β6-1089 cells transfected with empty vector ( EMPTY ) wild-type matrix metalloproteinase-8 ( MMP-8 WT ) or inactive mutant MMP-8 ( EA ) and grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( red ) and plectin ( green ). Insert: cartoon illustrating hemidesmosome ( HD ) components, indicating the integrin α6β4 associates with plectin to link the complex to the keratin cytoskeleton. (ii) Co-localisation of α6β4 and plectin was determined by quantifying the number of yellow pixels per field of view in each condition then expressed as a ratio as compared to EMPTY. β6-1089 transfected with WT demonstrated a significant increase in α6β4 and plectin co-localisation, while the β6-1089 transfected with EA exhibited no change as compared to EMPTY. b (i) Confocal images of β6-1089 cells transfected with empty vector (EMPTY) wild-type MMP-8 (WT) or inactive mutant MMP-8 (EA) and grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( green ) and phallodin ( red ). (ii) Morphological features of the transfected β6-1089 were analysed and length of trailing fibres was noted to be altered. Analysis of the length of these fibres indicated that β6-1089 transfected with MMP-8 WT significantly reduced the fibre length as compared to β6-1089 transfected with empty vector or MMP-8 EA. (iii) Analysis of the number of these fibres per cell also demonstrated a significant reduction in β6-1089 transfected with MMP-8 WT as compared to β6-1089 transfected with empty vector or MMP-8 EA. (iv) The final morphological alteration analysed was the physical space the cells occupied, the relative area occupied by β6-1089 transfected with MMP-8 WT was significantly larger than that occupied by β6-1089 transfected with empty vector or MMP-8 EA. c (i) Confocal images of N-1089 cells transfected with siRNA targeting MMP-8 ( siMMP-8 ) or Luciferase ( siLuc ) as a control grown on Fibronectin for 24 hours then fixed and co-stained for α6β4 ( green ) and phallodin ( red ). (ii) Trailing fibre length was significantly longer in N-1089 transfected with siMMP8 as compared to siLUC. (iii) There were significantly more trailing fibres per cell in the N-1089 + siMMP8 group as compared to N-1089 transfected with siLUC. * p = 0.05 ** p = 0.01, *** p = 0.001 (Student’s t test). Error bars = SEM, n = 3 independent experiments

Article Snippet: Primary antibodies used were α6β4 integrin (Merck Millipore, Billerica, MA, USA, MAB1964) and plectin (Epitomics, Burlingame, CA, USA, 1399).

Techniques: Expressing, Transfection, Plasmid Preparation, Mutagenesis, Staining, Luciferase, Control