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integrin α v β 6  (Bioss)


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    Structured Review

    Bioss integrin α v β 6
    <t>Integrin</t> <t>α</t> <t>v</t> <t>β</t> <t>6</t> active latent TGF‐ β in response to mechanical stress drives the progression of tendinopathy. A) Representative images and B) quantification of immunostaining of tendon sections with antibodies against α v β 6 at 1, 4, and 8 weeks after DI or sham processing. Scale bar: 50 µm. All data are shown as the mean ± standard deviation ( n = 8 mice per group). * p < 0.05 compared with sham group as determined by one‐way analysis of variance. C) A schematic diagram of the ex vivo tensile model. D) Frequency distribution of tendon fiber orientation. E,G) Representative images and F,H) quantification of E,F) pSmad2 + cells and (G, H) TUNEL + cells. Scale bars: 50 µm. I) Western blot of pSmad2 and Smad2 levels in tendon lysates. J) Quantification of pSmad2 relative density relative to physiological loading group (20 g) in tendon lysates after above‐mentioned treatment. K) Quantitative analysis of maximum tensile force and stiffness of tendons. All data from B, F, H, J, and K are shown as the mean ± standard deviation ( n = 8 per group). * p < 0.05 compared with 200 g loaded group as determined by one‐way analysis of variance.
    Integrin α V β 6, supplied by Bioss, used in various techniques. Bioz Stars score: 91/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/integrin α v β 6/product/Bioss
    Average 91 stars, based on 4 article reviews
    integrin α v β 6 - by Bioz Stars, 2026-02
    91/100 stars

    Images

    1) Product Images from "Inhibition of Integrin α v β 6 Activation of TGF‐ β Attenuates Tendinopathy"

    Article Title: Inhibition of Integrin α v β 6 Activation of TGF‐ β Attenuates Tendinopathy

    Journal: Advanced Science

    doi: 10.1002/advs.202104469

    Integrin α v β 6 active latent TGF‐ β in response to mechanical stress drives the progression of tendinopathy. A) Representative images and B) quantification of immunostaining of tendon sections with antibodies against α v β 6 at 1, 4, and 8 weeks after DI or sham processing. Scale bar: 50 µm. All data are shown as the mean ± standard deviation ( n = 8 mice per group). * p < 0.05 compared with sham group as determined by one‐way analysis of variance. C) A schematic diagram of the ex vivo tensile model. D) Frequency distribution of tendon fiber orientation. E,G) Representative images and F,H) quantification of E,F) pSmad2 + cells and (G, H) TUNEL + cells. Scale bars: 50 µm. I) Western blot of pSmad2 and Smad2 levels in tendon lysates. J) Quantification of pSmad2 relative density relative to physiological loading group (20 g) in tendon lysates after above‐mentioned treatment. K) Quantitative analysis of maximum tensile force and stiffness of tendons. All data from B, F, H, J, and K are shown as the mean ± standard deviation ( n = 8 per group). * p < 0.05 compared with 200 g loaded group as determined by one‐way analysis of variance.
    Figure Legend Snippet: Integrin α v β 6 active latent TGF‐ β in response to mechanical stress drives the progression of tendinopathy. A) Representative images and B) quantification of immunostaining of tendon sections with antibodies against α v β 6 at 1, 4, and 8 weeks after DI or sham processing. Scale bar: 50 µm. All data are shown as the mean ± standard deviation ( n = 8 mice per group). * p < 0.05 compared with sham group as determined by one‐way analysis of variance. C) A schematic diagram of the ex vivo tensile model. D) Frequency distribution of tendon fiber orientation. E,G) Representative images and F,H) quantification of E,F) pSmad2 + cells and (G, H) TUNEL + cells. Scale bars: 50 µm. I) Western blot of pSmad2 and Smad2 levels in tendon lysates. J) Quantification of pSmad2 relative density relative to physiological loading group (20 g) in tendon lysates after above‐mentioned treatment. K) Quantitative analysis of maximum tensile force and stiffness of tendons. All data from B, F, H, J, and K are shown as the mean ± standard deviation ( n = 8 per group). * p < 0.05 compared with 200 g loaded group as determined by one‐way analysis of variance.

    Techniques Used: Immunostaining, Standard Deviation, Ex Vivo, TUNEL Assay, Western Blot



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    ( A ) Chemical structures of 64 Cu-radiolabeled-ABM-α v <t>β</t> <t>6</t> -BP: [ 64 Cu]Cu DOTA-EB-α v β 6 -BP and [ 64 Cu]Cu DOTA-IP-α v β 6 -BP ([ 64 Cu] 1 and [ 64 Cu] 2 ). ( B ) Chemical structures of 64 Cu-radiolabeled non-targeting-ABM controls: [ 64 Cu]Cu DOTA-EB and [ 64 Cu]Cu DOTA-IP ([ 64 Cu] 3 and [ 64 Cu] 4 ). [α v β 6 -BP = PEG 28 -NAVPNLRGDLQVLAQRVART-PEG 28 -CONH 2 ].
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    <t>Integrin</t> <t>α</t> <t>v</t> <t>β</t> <t>6</t> active latent TGF‐ β in response to mechanical stress drives the progression of tendinopathy. A) Representative images and B) quantification of immunostaining of tendon sections with antibodies against α v β 6 at 1, 4, and 8 weeks after DI or sham processing. Scale bar: 50 µm. All data are shown as the mean ± standard deviation ( n = 8 mice per group). * p < 0.05 compared with sham group as determined by one‐way analysis of variance. C) A schematic diagram of the ex vivo tensile model. D) Frequency distribution of tendon fiber orientation. E,G) Representative images and F,H) quantification of E,F) pSmad2 + cells and (G, H) TUNEL + cells. Scale bars: 50 µm. I) Western blot of pSmad2 and Smad2 levels in tendon lysates. J) Quantification of pSmad2 relative density relative to physiological loading group (20 g) in tendon lysates after above‐mentioned treatment. K) Quantitative analysis of maximum tensile force and stiffness of tendons. All data from B, F, H, J, and K are shown as the mean ± standard deviation ( n = 8 per group). * p < 0.05 compared with 200 g loaded group as determined by one‐way analysis of variance.
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    <t>Integrin</t> <t>α</t> <t>v</t> <t>β</t> <t>6</t> active latent TGF‐ β in response to mechanical stress drives the progression of tendinopathy. A) Representative images and B) quantification of immunostaining of tendon sections with antibodies against α v β 6 at 1, 4, and 8 weeks after DI or sham processing. Scale bar: 50 µm. All data are shown as the mean ± standard deviation ( n = 8 mice per group). * p < 0.05 compared with sham group as determined by one‐way analysis of variance. C) A schematic diagram of the ex vivo tensile model. D) Frequency distribution of tendon fiber orientation. E,G) Representative images and F,H) quantification of E,F) pSmad2 + cells and (G, H) TUNEL + cells. Scale bars: 50 µm. I) Western blot of pSmad2 and Smad2 levels in tendon lysates. J) Quantification of pSmad2 relative density relative to physiological loading group (20 g) in tendon lysates after above‐mentioned treatment. K) Quantitative analysis of maximum tensile force and stiffness of tendons. All data from B, F, H, J, and K are shown as the mean ± standard deviation ( n = 8 per group). * p < 0.05 compared with 200 g loaded group as determined by one‐way analysis of variance.
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    Bioss rabbit antihuman integrin α v β 6 antibody
    (A) Chemical structure of DOTA-cycratide. (B) Inhibition of 64Cu-cycratide binding to <t>integrin</t> αvβ6 on BxPC-3 cells by cycratide, DOTA-cycratide, and linear-pep. Data are shown as mean ± SD, n = 4. (C) Binding of 68Ga-cycratide to BxPC-3 with or without blocking of cold cycratide or linear-pep. %AD/106 cells = percentage of total added dose per million cells. Data are shown as mean ± SD, n = 4. (D) Metabolic stability of 68Ga-cycratide in blood and urine of BALB/c mice (data are representative of 3 independent experiments). **P < 0.01.
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    Image Search Results


    Selected clinical IPF candidates

    Journal: Nature Biotechnology

    Article Title: Fighting fibrosis

    doi: 10.1038/s41587-022-01412-0

    Figure Lengend Snippet: Selected clinical IPF candidates

    Article Snippet: In early 2022, AbbVie axed two α v β 6 integrin inhibitors licensed two years earlier from Morphic Therapeutic because of on-target safety signals found in preclinical testing.

    Techniques: Recombinant

    ( A ) Chemical structures of 64 Cu-radiolabeled-ABM-α v β 6 -BP: [ 64 Cu]Cu DOTA-EB-α v β 6 -BP and [ 64 Cu]Cu DOTA-IP-α v β 6 -BP ([ 64 Cu] 1 and [ 64 Cu] 2 ). ( B ) Chemical structures of 64 Cu-radiolabeled non-targeting-ABM controls: [ 64 Cu]Cu DOTA-EB and [ 64 Cu]Cu DOTA-IP ([ 64 Cu] 3 and [ 64 Cu] 4 ). [α v β 6 -BP = PEG 28 -NAVPNLRGDLQVLAQRVART-PEG 28 -CONH 2 ].

    Journal: Pharmaceutics

    Article Title: A Comparison of Evans Blue and 4-( p -Iodophenyl)butyryl Albumin Binding Moieties on an Integrin α v β 6 Binding Peptide

    doi: 10.3390/pharmaceutics14040745

    Figure Lengend Snippet: ( A ) Chemical structures of 64 Cu-radiolabeled-ABM-α v β 6 -BP: [ 64 Cu]Cu DOTA-EB-α v β 6 -BP and [ 64 Cu]Cu DOTA-IP-α v β 6 -BP ([ 64 Cu] 1 and [ 64 Cu] 2 ). ( B ) Chemical structures of 64 Cu-radiolabeled non-targeting-ABM controls: [ 64 Cu]Cu DOTA-EB and [ 64 Cu]Cu DOTA-IP ([ 64 Cu] 3 and [ 64 Cu] 4 ). [α v β 6 -BP = PEG 28 -NAVPNLRGDLQVLAQRVART-PEG 28 -CONH 2 ].

    Article Snippet: Purified integrin α v β 6 (R&D Systems, Minneapolis, MN, USA) in conjugate buffer (50 μL/well, 20mM Tris, 1 mM MnCl 2 , 150 mM NaCl, 0.1% Tween, 0.1% milk powder in water) was then added to each well, incubated at 37 °C for 1 h, followed by washing using wash buffer 3×).

    Techniques:

    Cell binding (■) and internalization (□) for [ 64 Cu]Cu DOTA-EB-α v β 6 -BP ([ 64 Cu] 1 ) and [ 64 Cu]Cu DOTA-IP-α v β 6 -BP ([ 64 Cu] 2 ) for ( A ) DX3puroβ6 (α v β 6 +) and DX3puro(α v β 6 −) cells and ( B ) BxPC-3 (α v β 6 +) cells.

    Journal: Pharmaceutics

    Article Title: A Comparison of Evans Blue and 4-( p -Iodophenyl)butyryl Albumin Binding Moieties on an Integrin α v β 6 Binding Peptide

    doi: 10.3390/pharmaceutics14040745

    Figure Lengend Snippet: Cell binding (■) and internalization (□) for [ 64 Cu]Cu DOTA-EB-α v β 6 -BP ([ 64 Cu] 1 ) and [ 64 Cu]Cu DOTA-IP-α v β 6 -BP ([ 64 Cu] 2 ) for ( A ) DX3puroβ6 (α v β 6 +) and DX3puro(α v β 6 −) cells and ( B ) BxPC-3 (α v β 6 +) cells.

    Article Snippet: Purified integrin α v β 6 (R&D Systems, Minneapolis, MN, USA) in conjugate buffer (50 μL/well, 20mM Tris, 1 mM MnCl 2 , 150 mM NaCl, 0.1% Tween, 0.1% milk powder in water) was then added to each well, incubated at 37 °C for 1 h, followed by washing using wash buffer 3×).

    Techniques: Binding Assay

    Integrin α v β 6 active latent TGF‐ β in response to mechanical stress drives the progression of tendinopathy. A) Representative images and B) quantification of immunostaining of tendon sections with antibodies against α v β 6 at 1, 4, and 8 weeks after DI or sham processing. Scale bar: 50 µm. All data are shown as the mean ± standard deviation ( n = 8 mice per group). * p < 0.05 compared with sham group as determined by one‐way analysis of variance. C) A schematic diagram of the ex vivo tensile model. D) Frequency distribution of tendon fiber orientation. E,G) Representative images and F,H) quantification of E,F) pSmad2 + cells and (G, H) TUNEL + cells. Scale bars: 50 µm. I) Western blot of pSmad2 and Smad2 levels in tendon lysates. J) Quantification of pSmad2 relative density relative to physiological loading group (20 g) in tendon lysates after above‐mentioned treatment. K) Quantitative analysis of maximum tensile force and stiffness of tendons. All data from B, F, H, J, and K are shown as the mean ± standard deviation ( n = 8 per group). * p < 0.05 compared with 200 g loaded group as determined by one‐way analysis of variance.

    Journal: Advanced Science

    Article Title: Inhibition of Integrin α v β 6 Activation of TGF‐ β Attenuates Tendinopathy

    doi: 10.1002/advs.202104469

    Figure Lengend Snippet: Integrin α v β 6 active latent TGF‐ β in response to mechanical stress drives the progression of tendinopathy. A) Representative images and B) quantification of immunostaining of tendon sections with antibodies against α v β 6 at 1, 4, and 8 weeks after DI or sham processing. Scale bar: 50 µm. All data are shown as the mean ± standard deviation ( n = 8 mice per group). * p < 0.05 compared with sham group as determined by one‐way analysis of variance. C) A schematic diagram of the ex vivo tensile model. D) Frequency distribution of tendon fiber orientation. E,G) Representative images and F,H) quantification of E,F) pSmad2 + cells and (G, H) TUNEL + cells. Scale bars: 50 µm. I) Western blot of pSmad2 and Smad2 levels in tendon lysates. J) Quantification of pSmad2 relative density relative to physiological loading group (20 g) in tendon lysates after above‐mentioned treatment. K) Quantitative analysis of maximum tensile force and stiffness of tendons. All data from B, F, H, J, and K are shown as the mean ± standard deviation ( n = 8 per group). * p < 0.05 compared with 200 g loaded group as determined by one‐way analysis of variance.

    Article Snippet: Sections were incubated with primary antibodies to human CD68 (Abcam, Cambridge, UK, ab955, 1:200), human Col2 (Abcam, ab34712, 1:100), human MMP13 (Abcam, ab3208, 1:40), human/mouse pSmad2 (Santa Cruz Biotechnology, Dallas, TX, sc‐11769, 1:50), mouse Col2 (Abcam, ab185430, 1:100), mouse CD68 (Abcam, ab125212, 1:100), mouse MMP13 (Abcam, ab219620, 1:100), mouse green fluorescent protein (Abcam, ab290, 1:200), and integrin α v β 6 (Bioss Antibodies, Woburn, MA, bs‐5791R‐Biotin, 1:100) overnight at 4 °C.

    Techniques: Immunostaining, Standard Deviation, Ex Vivo, TUNEL Assay, Western Blot

    (A) Chemical structure of DOTA-cycratide. (B) Inhibition of 64Cu-cycratide binding to integrin αvβ6 on BxPC-3 cells by cycratide, DOTA-cycratide, and linear-pep. Data are shown as mean ± SD, n = 4. (C) Binding of 68Ga-cycratide to BxPC-3 with or without blocking of cold cycratide or linear-pep. %AD/106 cells = percentage of total added dose per million cells. Data are shown as mean ± SD, n = 4. (D) Metabolic stability of 68Ga-cycratide in blood and urine of BALB/c mice (data are representative of 3 independent experiments). **P < 0.01.

    Journal: Journal of Nuclear Medicine

    Article Title: Clinical Translation of a 68 Ga-Labeled Integrin α v β 6 –Targeting Cyclic Radiotracer for PET Imaging of Pancreatic Cancer

    doi: 10.2967/jnumed.119.237347

    Figure Lengend Snippet: (A) Chemical structure of DOTA-cycratide. (B) Inhibition of 64Cu-cycratide binding to integrin αvβ6 on BxPC-3 cells by cycratide, DOTA-cycratide, and linear-pep. Data are shown as mean ± SD, n = 4. (C) Binding of 68Ga-cycratide to BxPC-3 with or without blocking of cold cycratide or linear-pep. %AD/106 cells = percentage of total added dose per million cells. Data are shown as mean ± SD, n = 4. (D) Metabolic stability of 68Ga-cycratide in blood and urine of BALB/c mice (data are representative of 3 independent experiments). **P < 0.01.

    Article Snippet: After endogenous peroxidase activity had been abolished using 0.3% hydrogen peroxide and antigen had been retrieved by microwave, tumor tissues were incubated with rabbit antihuman integrin α v β 6 antibody (bs-5791r; Bioss) overnight at 4°C.

    Techniques: Inhibition, Binding Assay, Blocking Assay

    (A) PET imaging of orthotopic pancreatic cancer lesions in nude mice at 0.5 h after injection of 68Ga-cycratide without or with blocking dose of cold cycratide. Tumors are indicated by arrows. (B) Hematoxylin and eosin (H&E) staining of tumor tissues harvested from orthotopic tumor model. (C) Left, immunofluorescence staining of integrin αvβ6 from tumor tissues harvested from orthotopic tumor model. Right, negative control with secondary antibody only.

    Journal: Journal of Nuclear Medicine

    Article Title: Clinical Translation of a 68 Ga-Labeled Integrin α v β 6 –Targeting Cyclic Radiotracer for PET Imaging of Pancreatic Cancer

    doi: 10.2967/jnumed.119.237347

    Figure Lengend Snippet: (A) PET imaging of orthotopic pancreatic cancer lesions in nude mice at 0.5 h after injection of 68Ga-cycratide without or with blocking dose of cold cycratide. Tumors are indicated by arrows. (B) Hematoxylin and eosin (H&E) staining of tumor tissues harvested from orthotopic tumor model. (C) Left, immunofluorescence staining of integrin αvβ6 from tumor tissues harvested from orthotopic tumor model. Right, negative control with secondary antibody only.

    Article Snippet: After endogenous peroxidase activity had been abolished using 0.3% hydrogen peroxide and antigen had been retrieved by microwave, tumor tissues were incubated with rabbit antihuman integrin α v β 6 antibody (bs-5791r; Bioss) overnight at 4°C.

    Techniques: Imaging, Injection, Blocking Assay, Staining, Immunofluorescence, Negative Control

    (A) PET/CT images of female patient with suspected pancreatic cancer. Images were obtained at 1 h after intravenous administration of 68Ga-cycratide or 18F-FDG. Tumors are indicated by arrows. (B) Immunohistochemical (IHC) staining for integrin αvβ6 in tumor sample from same patient as in A. (C) Contrast-enhanced CT (CECT) image and PET/CT images of male patient with pancreatic cancer 7 mo after surgery at 1 h after administration of 68Ga-cycratide or 18F-FDG, as well as CECT image of same patient 3 mo later (10 mo after surgery). Occupancy lesions in CT are indicated by arrows.

    Journal: Journal of Nuclear Medicine

    Article Title: Clinical Translation of a 68 Ga-Labeled Integrin α v β 6 –Targeting Cyclic Radiotracer for PET Imaging of Pancreatic Cancer

    doi: 10.2967/jnumed.119.237347

    Figure Lengend Snippet: (A) PET/CT images of female patient with suspected pancreatic cancer. Images were obtained at 1 h after intravenous administration of 68Ga-cycratide or 18F-FDG. Tumors are indicated by arrows. (B) Immunohistochemical (IHC) staining for integrin αvβ6 in tumor sample from same patient as in A. (C) Contrast-enhanced CT (CECT) image and PET/CT images of male patient with pancreatic cancer 7 mo after surgery at 1 h after administration of 68Ga-cycratide or 18F-FDG, as well as CECT image of same patient 3 mo later (10 mo after surgery). Occupancy lesions in CT are indicated by arrows.

    Article Snippet: After endogenous peroxidase activity had been abolished using 0.3% hydrogen peroxide and antigen had been retrieved by microwave, tumor tissues were incubated with rabbit antihuman integrin α v β 6 antibody (bs-5791r; Bioss) overnight at 4°C.

    Techniques: Positron Emission Tomography-Computed Tomography, Immunohistochemical staining, Immunohistochemistry