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
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mouse anti-integrin α6β4 - by Bioz Stars, 2026-03
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phenotypic spectrum of epidermolysis bullosa associated with α6β4 integrin mutations  (Hausser Scientific)
90
Hausser Scientific phenotypic spectrum of epidermolysis bullosa associated with α6β4 integrin mutations
Phenotypic Spectrum Of Epidermolysis Bullosa Associated With α6β4 Integrin Mutations, supplied by Hausser Scientific, 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/result/phenotypic spectrum of epidermolysis bullosa associated with α6β4 integrin mutations/product/Hausser Scientific
Average 90 stars, based on 1 article reviews
phenotypic spectrum of epidermolysis bullosa associated with α6β4 integrin mutations - by Bioz Stars, 2026-03
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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/result/α6β4 integrin mab1964 antibody/product/Merck KGaA
Average 90 stars, based on 1 article reviews
α6β4 integrin mab1964 antibody - by Bioz Stars, 2026-03
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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/result/rat monoclonal anti-integrin α6β4 antibody/product/Immunotec inc
Average 90 stars, based on 1 article reviews
rat monoclonal anti-integrin α6β4 antibody - by Bioz Stars, 2026-03
90/100 stars
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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/result/integrins α6β1 and α6β4/product/The Company of Biologists
Average 90 stars, based on 1 article reviews
integrins α6β1 and α6β4 - by Bioz Stars, 2026-03
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purified integrin α6β4  (Sino Biological)
90
Sino Biological purified integrin 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
Purified Integrin α6β4, supplied by Sino Biological, 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/result/purified integrin α6β4/product/Sino Biological
Average 90 stars, based on 1 article reviews
purified integrin α6β4 - by Bioz Stars, 2026-03
90/100 stars
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integrin α6β4  (Aktin Chemicals Inc)
90
Aktin Chemicals Inc integrin 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
Integrin α6β4, supplied by Aktin Chemicals 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/result/integrin α6β4/product/Aktin Chemicals Inc
Average 90 stars, based on 1 article reviews
integrin α6β4 - by Bioz Stars, 2026-03
90/100 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