α2 Search Results


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  • 94
    New England Biolabs α2 3 neuraminidase
    α2 3 Neuraminidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 51 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore α2 antiplasmin
    Plasmin-mediated amyloid fibrillogenesis of S52P TTR. A , increase in ThT emission fluorescence for S52P TTR incubated in the presence of plasmin compared with trypsin. No amyloid-specific ThT signal was seen after incubation of S52P TTR with thrombin, chymotrypsin, or proteinase K. B and C , negatively stained transmission electron micrographs of S52P TTR amyloid fibrils formed in the presence of trypsin ( B ) or plasmin ( C ). Scale bar , 100 nm. D , 15% SDS-PAGE under reducing conditions. M , marker proteins (14.4, 20.1, 30.0, 45.0, 66.0, and 97.0 kDa); lane 1 , S52P TTR at time 0; lane 2 , S52P TTR fibrils formed in the presence of trypsin; and lane 3 , S52P TTR fibrils formed in the presence of plasmin. E , immunoblot analysis of samples separated in 15% SDS-PAGE (see lanes 1 , 2 , and 3 in D ). Position of marker proteins at 15 and 10 kDa are indicated. F , inhibition by <t>α2-antiplasmin</t> of fibril formation by S52P TTR mediated by 20 ng/μl plasmin. The data were normalized to the ThT signal plateau in the samples without α2-antiplasmin. Mean ± S.D. of three replicates is shown. a.u. , arbitrary units.
    α2 Antiplasmin, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 121 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore α2 macroglobulin
    Survival of Culex quinquefasciatus larvae exposed to blastospores (BS) and conidia (C) of M. brunneum in the presence and absence of a protease inhibitor. Cx. quinquefasciatus (n = 72, 24 larvae per replicate) were exposed to M. brunneum blastospores and conidia (10 7 spores ml −1 ) with and without the protease inhibitor <t>α2-macroglobulin.</t> Controls consisted of either distilled water or 0.03% aq. Tween 80 with and without the inhibitor. Error bars represent ± SE.
    α2 Macroglobulin, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 176 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore anti laminin 2 alpha 2 chain antibody rat monoclonal
    Survival of Culex quinquefasciatus larvae exposed to blastospores (BS) and conidia (C) of M. brunneum in the presence and absence of a protease inhibitor. Cx. quinquefasciatus (n = 72, 24 larvae per replicate) were exposed to M. brunneum blastospores and conidia (10 7 spores ml −1 ) with and without the protease inhibitor <t>α2-macroglobulin.</t> Controls consisted of either distilled water or 0.03% aq. Tween 80 with and without the inhibitor. Error bars represent ± SE.
    Anti Laminin 2 Alpha 2 Chain Antibody Rat Monoclonal, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 175 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Takeda s laminin alpha2 chain null mutant mice
    Survival of Culex quinquefasciatus larvae exposed to blastospores (BS) and conidia (C) of M. brunneum in the presence and absence of a protease inhibitor. Cx. quinquefasciatus (n = 72, 24 larvae per replicate) were exposed to M. brunneum blastospores and conidia (10 7 spores ml −1 ) with and without the protease inhibitor <t>α2-macroglobulin.</t> Controls consisted of either distilled water or 0.03% aq. Tween 80 with and without the inhibitor. Error bars represent ± SE.
    S Laminin Alpha2 Chain Null Mutant Mice, supplied by Takeda, used in various techniques. Bioz Stars score: 88/100, based on 51 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    BioLegend anti cd49b
    Survival of Culex quinquefasciatus larvae exposed to blastospores (BS) and conidia (C) of M. brunneum in the presence and absence of a protease inhibitor. Cx. quinquefasciatus (n = 72, 24 larvae per replicate) were exposed to M. brunneum blastospores and conidia (10 7 spores ml −1 ) with and without the protease inhibitor <t>α2-macroglobulin.</t> Controls consisted of either distilled water or 0.03% aq. Tween 80 with and without the inhibitor. Error bars represent ± SE.
    Anti Cd49b, supplied by BioLegend, used in various techniques. Bioz Stars score: 98/100, based on 462 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore anti α2
    Survival of Culex quinquefasciatus larvae exposed to blastospores (BS) and conidia (C) of M. brunneum in the presence and absence of a protease inhibitor. Cx. quinquefasciatus (n = 72, 24 larvae per replicate) were exposed to M. brunneum blastospores and conidia (10 7 spores ml −1 ) with and without the protease inhibitor <t>α2-macroglobulin.</t> Controls consisted of either distilled water or 0.03% aq. Tween 80 with and without the inhibitor. Error bars represent ± SE.
    Anti α2, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 51 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore laminin α2
    Survival of Culex quinquefasciatus larvae exposed to blastospores (BS) and conidia (C) of M. brunneum in the presence and absence of a protease inhibitor. Cx. quinquefasciatus (n = 72, 24 larvae per replicate) were exposed to M. brunneum blastospores and conidia (10 7 spores ml −1 ) with and without the protease inhibitor <t>α2-macroglobulin.</t> Controls consisted of either distilled water or 0.03% aq. Tween 80 with and without the inhibitor. Error bars represent ± SE.
    Laminin α2, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 108 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    New England Biolabs α2 3 6 8 neuraminidase
    Survival of Culex quinquefasciatus larvae exposed to blastospores (BS) and conidia (C) of M. brunneum in the presence and absence of a protease inhibitor. Cx. quinquefasciatus (n = 72, 24 larvae per replicate) were exposed to M. brunneum blastospores and conidia (10 7 spores ml −1 ) with and without the protease inhibitor <t>α2-macroglobulin.</t> Controls consisted of either distilled water or 0.03% aq. Tween 80 with and without the inhibitor. Error bars represent ± SE.
    α2 3 6 8 Neuraminidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore α2 3
    Survival of Culex quinquefasciatus larvae exposed to blastospores (BS) and conidia (C) of M. brunneum in the presence and absence of a protease inhibitor. Cx. quinquefasciatus (n = 72, 24 larvae per replicate) were exposed to M. brunneum blastospores and conidia (10 7 spores ml −1 ) with and without the protease inhibitor <t>α2-macroglobulin.</t> Controls consisted of either distilled water or 0.03% aq. Tween 80 with and without the inhibitor. Error bars represent ± SE.
    α2 3, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 81 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Enzo Biochem anti laminin α2
    Spatio-temporal distribution of <t>laminin-α1</t> and laminin-α5 in regenerating muscles. a Immunofluorescence analysis of <t>laminin-α2</t> (green, top panels), laminin-α1 (green, middle panels), and laminin-α5 (gray, bottom panels) in regenerating TA muscle following cardiotoxin-mediated injury. Panels on the right are high magnification images of the 2 dpi images (indicated by a white rectangle, with small inserts showing the same image with the laminin channel only). The insert shown at 4 dpi in the laminin-α5 panels illustrates increased laminin α5 (white) deposition at the surface of satellite cells. White arrows indicate satellite cells. Yellow arrows indicate MyoD − or Pax7 − (GFP − ) cells positive for laminin-α1 or α5. Scale bar, 50 μm. b Quantification of the number of laminin-α1 + myogenic cells in regenerating muscles. c qPCR analysis of Lama1 and Lama5 gene expression in myofibers cultured for 0–72 h. n = 6 experiments. Graphs show mean + sem
    Anti Laminin α2, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 88/100, based on 109 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore α2 3 n sialyltransferase
    Spatio-temporal distribution of <t>laminin-α1</t> and laminin-α5 in regenerating muscles. a Immunofluorescence analysis of <t>laminin-α2</t> (green, top panels), laminin-α1 (green, middle panels), and laminin-α5 (gray, bottom panels) in regenerating TA muscle following cardiotoxin-mediated injury. Panels on the right are high magnification images of the 2 dpi images (indicated by a white rectangle, with small inserts showing the same image with the laminin channel only). The insert shown at 4 dpi in the laminin-α5 panels illustrates increased laminin α5 (white) deposition at the surface of satellite cells. White arrows indicate satellite cells. Yellow arrows indicate MyoD − or Pax7 − (GFP − ) cells positive for laminin-α1 or α5. Scale bar, 50 μm. b Quantification of the number of laminin-α1 + myogenic cells in regenerating muscles. c qPCR analysis of Lama1 and Lama5 gene expression in myofibers cultured for 0–72 h. n = 6 experiments. Graphs show mean + sem
    α2 3 N Sialyltransferase, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 48 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore α2 m
    Spatio-temporal distribution of <t>laminin-α1</t> and laminin-α5 in regenerating muscles. a Immunofluorescence analysis of <t>laminin-α2</t> (green, top panels), laminin-α1 (green, middle panels), and laminin-α5 (gray, bottom panels) in regenerating TA muscle following cardiotoxin-mediated injury. Panels on the right are high magnification images of the 2 dpi images (indicated by a white rectangle, with small inserts showing the same image with the laminin channel only). The insert shown at 4 dpi in the laminin-α5 panels illustrates increased laminin α5 (white) deposition at the surface of satellite cells. White arrows indicate satellite cells. Yellow arrows indicate MyoD − or Pax7 − (GFP − ) cells positive for laminin-α1 or α5. Scale bar, 50 μm. b Quantification of the number of laminin-α1 + myogenic cells in regenerating muscles. c qPCR analysis of Lama1 and Lama5 gene expression in myofibers cultured for 0–72 h. n = 6 experiments. Graphs show mean + sem
    α2 M, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 123 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore α2 6 n sialyltransferase
    Spatio-temporal distribution of <t>laminin-α1</t> and laminin-α5 in regenerating muscles. a Immunofluorescence analysis of <t>laminin-α2</t> (green, top panels), laminin-α1 (green, middle panels), and laminin-α5 (gray, bottom panels) in regenerating TA muscle following cardiotoxin-mediated injury. Panels on the right are high magnification images of the 2 dpi images (indicated by a white rectangle, with small inserts showing the same image with the laminin channel only). The insert shown at 4 dpi in the laminin-α5 panels illustrates increased laminin α5 (white) deposition at the surface of satellite cells. White arrows indicate satellite cells. Yellow arrows indicate MyoD − or Pax7 − (GFP − ) cells positive for laminin-α1 or α5. Scale bar, 50 μm. b Quantification of the number of laminin-α1 + myogenic cells in regenerating muscles. c qPCR analysis of Lama1 and Lama5 gene expression in myofibers cultured for 0–72 h. n = 6 experiments. Graphs show mean + sem
    α2 6 N Sialyltransferase, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Millipore a2m
    Protease inhibitors alpha-2-macroglobulin <t>(A2m)</t> and proteinase 15 (Pi15) decrease MMP9 activity and expression in 17-week old mandibular condylar fibrocartilage. ( A ) Immunohistochemistry of A2m in all groups. ( B ) Explant study timeline and digital micrograph illustrating the mandible in culture for 48 hours of A2m treatment (0, 100, or 200 nM) or Pi15 treatment (0, 50, or 100 nM). ( C ) Zymogram using 10% gelatin substrate illustrating protease activity as a function of A2m dose ( D ) qPCR gene expression of MMP9 in A2m treatment explant culture. ( E ) Zymogram using 10% gelatin substrate illustrating protease activity as a function of Pi15 dose ( F . All values represent means ± standard deviation. n = 5 for explant culture datum, ^ p
    A2m, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Santa Cruz Biotechnology ampk α2
    The α1-, <t>α2-,</t> γ1-, γ2-, and γ3-subunits of <t>AMPK</t> are O -GlcNAcylated. A , recombinant AMPK-α1β1γ1 or -α2β1γ1 complexes were incubated with recombinant O -GlcNAc transferase
    Ampk α2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Abcam integrin α2
    <t>Integrin</t> α5 is necessary for P4G11-mediated restoration of epithelial junctions in vitro. (A) Immunoblot analysis of total levels of integrin α5, integrin β1, integrin <t>α2,</t> and β-actin in SW480 cells engineered to produce anti–integrin α5 shRNA in the presence (ON) or absence (OFF) of doxycycline. Two different shRNAs (A5sh1 and A5sh3) targeting different parts of the integrin α5 gene were compared. (B) Quantification of the percentage of invasive SC colonies present when cells in A were grown in 3D type 1 collagen and treated with P4G11 in the presence (shA5 +) or absence (shA5 –) of anti–integrin α5 shRNA. Note lack of response to P4G11 in colonies expressing anti–integrin α5 shRNA (mean ± SEM; > 300 colonies from three separate replicates). (C) Representative confocal image of cells in A grown in 3D type 1 collagen as in Figure 1 A and treated with P4G11 in presence (ON) or absence (OFF) of anti–integrin α5 shRNA (A5sh1 shown) stained with phalloidin (red) and DAPI (blue). Scale bar, 100 μm. (D) Representative maximum intensity projections of SW480 cells grown on MMC-coated coverglass stained with phalloidin (red), DAPI (blue), and an antibody against ZO-1 (green). Scale bar, 20 μm. (E) Quantification of number of cells exhibiting ZO-1 localization of cell–cell membranes through ImageJ analysis (see Materials and Methods ; mean ± SEM; more than five 20× fields of view from three separate replicates). (F) Representative XZ -plane reconstruction of cells in A stained with antibodies against ZO-1 (green), phalloidin (red), and DAPI (blue). Scale bar, 20 μm. Asterisks signify statistical significance with p
    Integrin α2, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Santa Cruz Biotechnology integrin α2
    Cisplatin impedes migration by deterring <t>Integrin/Fak</t> signalling in aspirin pre-treated spheroids. ( A ) Percent <t>Integrin-α2</t> (left panel), Integrin-α5 (middle panel) and Integrin-β1 (right panel) expression was represented graphically as detected by flow-cytometry in A549 parental cell and spheroids. ( B ) Western blot analysis of Integrin-α2, Integrin-α5, Integrin-β1 and p-FAK in untreated or aspirin/-cisplatin/-aspirin + cisplatin treated A549 spheroids. α-Actin was used as loading control. ( C ) Percent cell migration was calculated and represented graphically in control and Integrin-α2-siRNA, Integrin-α5–siRNA or Integrin-β1-siRNA transfected A549 spheroids as detected by transwell migration assay. The inset shows the immunoblot analysis of Integrinα2, Integrinα5 or Integrinβ1 levels for the transfection efficiency of Integrin-α2-siRNA, Integrin-α5–siRNA and Integrin-β1-siRNA respectively. ( D ) Protein expression levels of MMP-2 and MMP-9 in untreated or aspirin + cisplatin treated A549 spheroid. α-Actin served as loading control. Values are mean ± SEM of three independent experiments in each case or representative of typical experiment *p
    Integrin α2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Upstate Biotechnology Inc alpha2
    Cisplatin impedes migration by deterring <t>Integrin/Fak</t> signalling in aspirin pre-treated spheroids. ( A ) Percent <t>Integrin-α2</t> (left panel), Integrin-α5 (middle panel) and Integrin-β1 (right panel) expression was represented graphically as detected by flow-cytometry in A549 parental cell and spheroids. ( B ) Western blot analysis of Integrin-α2, Integrin-α5, Integrin-β1 and p-FAK in untreated or aspirin/-cisplatin/-aspirin + cisplatin treated A549 spheroids. α-Actin was used as loading control. ( C ) Percent cell migration was calculated and represented graphically in control and Integrin-α2-siRNA, Integrin-α5–siRNA or Integrin-β1-siRNA transfected A549 spheroids as detected by transwell migration assay. The inset shows the immunoblot analysis of Integrinα2, Integrinα5 or Integrinβ1 levels for the transfection efficiency of Integrin-α2-siRNA, Integrin-α5–siRNA and Integrin-β1-siRNA respectively. ( D ) Protein expression levels of MMP-2 and MMP-9 in untreated or aspirin + cisplatin treated A549 spheroid. α-Actin served as loading control. Values are mean ± SEM of three independent experiments in each case or representative of typical experiment *p
    Alpha2, supplied by Upstate Biotechnology Inc, used in various techniques. Bioz Stars score: 88/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    N/A
    Category Kits ELISA Kits Rat α2 AP α2 Antiplasmin ELISA Kit Size 96T Price 609 Reactivity Rat
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    N/A
    AChRα5 α2 Antibody 267 is a rat monoclonal IgG2a provided at 200 µg ml raised against purified AChR from brain tissue homogenate of chicken origin recommended for detection of nicotinic
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    N/A
    CRISPR Cas9 KO Plasmids consists of CapZ α2 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
    Gene Silencers generally consist of pools of three to five target specific 19 25 nucleotide sequences in length For independent verification of CapZ α2 gene silencing results individual duplex components
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    Image Search Results


    Plasmin-mediated amyloid fibrillogenesis of S52P TTR. A , increase in ThT emission fluorescence for S52P TTR incubated in the presence of plasmin compared with trypsin. No amyloid-specific ThT signal was seen after incubation of S52P TTR with thrombin, chymotrypsin, or proteinase K. B and C , negatively stained transmission electron micrographs of S52P TTR amyloid fibrils formed in the presence of trypsin ( B ) or plasmin ( C ). Scale bar , 100 nm. D , 15% SDS-PAGE under reducing conditions. M , marker proteins (14.4, 20.1, 30.0, 45.0, 66.0, and 97.0 kDa); lane 1 , S52P TTR at time 0; lane 2 , S52P TTR fibrils formed in the presence of trypsin; and lane 3 , S52P TTR fibrils formed in the presence of plasmin. E , immunoblot analysis of samples separated in 15% SDS-PAGE (see lanes 1 , 2 , and 3 in D ). Position of marker proteins at 15 and 10 kDa are indicated. F , inhibition by α2-antiplasmin of fibril formation by S52P TTR mediated by 20 ng/μl plasmin. The data were normalized to the ThT signal plateau in the samples without α2-antiplasmin. Mean ± S.D. of three replicates is shown. a.u. , arbitrary units.

    Journal: The Journal of Biological Chemistry

    Article Title: Plasminogen activation triggers transthyretin amyloidogenesis in vitro

    doi: 10.1074/jbc.RA118.003990

    Figure Lengend Snippet: Plasmin-mediated amyloid fibrillogenesis of S52P TTR. A , increase in ThT emission fluorescence for S52P TTR incubated in the presence of plasmin compared with trypsin. No amyloid-specific ThT signal was seen after incubation of S52P TTR with thrombin, chymotrypsin, or proteinase K. B and C , negatively stained transmission electron micrographs of S52P TTR amyloid fibrils formed in the presence of trypsin ( B ) or plasmin ( C ). Scale bar , 100 nm. D , 15% SDS-PAGE under reducing conditions. M , marker proteins (14.4, 20.1, 30.0, 45.0, 66.0, and 97.0 kDa); lane 1 , S52P TTR at time 0; lane 2 , S52P TTR fibrils formed in the presence of trypsin; and lane 3 , S52P TTR fibrils formed in the presence of plasmin. E , immunoblot analysis of samples separated in 15% SDS-PAGE (see lanes 1 , 2 , and 3 in D ). Position of marker proteins at 15 and 10 kDa are indicated. F , inhibition by α2-antiplasmin of fibril formation by S52P TTR mediated by 20 ng/μl plasmin. The data were normalized to the ThT signal plateau in the samples without α2-antiplasmin. Mean ± S.D. of three replicates is shown. a.u. , arbitrary units.

    Article Snippet: All other reagents including α2-antiplasmin (SRP6313) were purchased from Sigma-Aldrich unless otherwise stated.

    Techniques: Fluorescence, Incubation, Staining, Transmission Assay, SDS Page, Marker, Inhibition

    Survival of Culex quinquefasciatus larvae exposed to blastospores (BS) and conidia (C) of M. brunneum in the presence and absence of a protease inhibitor. Cx. quinquefasciatus (n = 72, 24 larvae per replicate) were exposed to M. brunneum blastospores and conidia (10 7 spores ml −1 ) with and without the protease inhibitor α2-macroglobulin. Controls consisted of either distilled water or 0.03% aq. Tween 80 with and without the inhibitor. Error bars represent ± SE.

    Journal: Virulence

    Article Title: Highly specific host-pathogen interactions influence Metarhizium brunneum blastospore virulence against Culex quinquefasciatus larvae

    doi: 10.1080/21505594.2018.1509665

    Figure Lengend Snippet: Survival of Culex quinquefasciatus larvae exposed to blastospores (BS) and conidia (C) of M. brunneum in the presence and absence of a protease inhibitor. Cx. quinquefasciatus (n = 72, 24 larvae per replicate) were exposed to M. brunneum blastospores and conidia (10 7 spores ml −1 ) with and without the protease inhibitor α2-macroglobulin. Controls consisted of either distilled water or 0.03% aq. Tween 80 with and without the inhibitor. Error bars represent ± SE.

    Article Snippet: Each larva was exposed to a 1 mL suspension of blastospores or conidia of M. brunneum ARSEF 4556 at a concentration of 107 spores mL−1 using the following treatments; (1) blastospores, (2) blastospores incubated with α2-macroglobulin (1 μg ml−1 , Sigma-Aldrich, St Louise, USA), (3) conidia, (4) conidia incubated with α2-macroglobulin.

    Techniques: Protease Inhibitor

    α2M altered osteoclast activity and reduced the apoptosis rate in hBMMSCs after irradiation. (A and B) Osteoclast activity was evaluated using TRAP staining. TRAP-positive cells (osteoclasts) are stained in red. Black arrows indicate osteoclasts (scale bar, 50 µ m). (C and D) Cell apoptosis was examined using TUNEL staining. Cells were stained using a TUNEL assay kit (green) and counterstained with DAPI (blue). Data represent the means ± standard deviation of three independent experiments. Scale bar, 50 µ m. * P

    Journal: International Journal of Oncology

    Article Title: Effect of α2-macroglobulin in the early stage of jaw osteoradionecrosis

    doi: 10.3892/ijo.2020.5051

    Figure Lengend Snippet: α2M altered osteoclast activity and reduced the apoptosis rate in hBMMSCs after irradiation. (A and B) Osteoclast activity was evaluated using TRAP staining. TRAP-positive cells (osteoclasts) are stained in red. Black arrows indicate osteoclasts (scale bar, 50 µ m). (C and D) Cell apoptosis was examined using TUNEL staining. Cells were stained using a TUNEL assay kit (green) and counterstained with DAPI (blue). Data represent the means ± standard deviation of three independent experiments. Scale bar, 50 µ m. * P

    Article Snippet: Following anesthesia with pentobarbital (1%; 50 mg/kg, intraperitoneal injection), a subperiosteal injection of 0.5 ml of 2 mg/ml α2M (cat. no. 441251-10MG; EMD Millipore) was prophylactically administered to mice from the α2M and α2M + RT groups 30 min prior to IR, whereas the control and RT groups were injected with the same volume of physiological saline.

    Techniques: Activity Assay, Irradiation, Staining, TUNEL Assay, Standard Deviation

    α2M reduced the apoptosis rate, improved the antioxidant capacity and upregulated Akt phosphorylation in the IR-treated hBMMSCs. (A) Different groups of hBMMSCs were evaluated 24 h after IR. Scale bar, 200 µ m. (B) CCK-8 assay was used to detect the effects of IR on hBMMSC proliferation 24, 48 and 72 h after IR. (C and D) α2M decreased the apoptosis rate in hBMMSCs 24 h after IR. Apoptotic rate was calculated by adding the Q2 and Q4 percentages (Q2, Annexin V and PI-positive cells; Q4, Annexin V-positive and PI-negative cells). (E and F) α2M decreased ROS level in the α2M + RT group detected by fluorescent microscopy (E, scale bar, 100 µ m) followed by statistical analysis. (G and H) α2M decreased ROS level in the α2M + RT group detected by flow cytometry followed by a statistical analysis. (I and J) Western blotting used to detect the effect of α2M on p-Akt, Akt, HO-1 and SOD2 expression in hBMMSCs 24 h after IR. * P

    Journal: International Journal of Oncology

    Article Title: Effect of α2-macroglobulin in the early stage of jaw osteoradionecrosis

    doi: 10.3892/ijo.2020.5051

    Figure Lengend Snippet: α2M reduced the apoptosis rate, improved the antioxidant capacity and upregulated Akt phosphorylation in the IR-treated hBMMSCs. (A) Different groups of hBMMSCs were evaluated 24 h after IR. Scale bar, 200 µ m. (B) CCK-8 assay was used to detect the effects of IR on hBMMSC proliferation 24, 48 and 72 h after IR. (C and D) α2M decreased the apoptosis rate in hBMMSCs 24 h after IR. Apoptotic rate was calculated by adding the Q2 and Q4 percentages (Q2, Annexin V and PI-positive cells; Q4, Annexin V-positive and PI-negative cells). (E and F) α2M decreased ROS level in the α2M + RT group detected by fluorescent microscopy (E, scale bar, 100 µ m) followed by statistical analysis. (G and H) α2M decreased ROS level in the α2M + RT group detected by flow cytometry followed by a statistical analysis. (I and J) Western blotting used to detect the effect of α2M on p-Akt, Akt, HO-1 and SOD2 expression in hBMMSCs 24 h after IR. * P

    Article Snippet: Following anesthesia with pentobarbital (1%; 50 mg/kg, intraperitoneal injection), a subperiosteal injection of 0.5 ml of 2 mg/ml α2M (cat. no. 441251-10MG; EMD Millipore) was prophylactically administered to mice from the α2M and α2M + RT groups 30 min prior to IR, whereas the control and RT groups were injected with the same volume of physiological saline.

    Techniques: CCK-8 Assay, Microscopy, Flow Cytometry, Western Blot, Expressing

    Pathophysiological changes associated with osteoradionecrosis in the jaws of mice in the four groups. (A) Haematoxylin and eosin staining. RT group showed significant increase in cell loss and vessel injury at each time point compared with α2M + RT group (scale bar, 100 µ m). (B) Empty lacunae were observed in HPFs in all groups. (C) Masson's trichrome staining. α2M+RT group exhibited fewer fat vacuoles compared with RT group, but more than in the control group (scale bar, 100 µ m). (D) Fat vacuoles were evaluated in HPFs in all groups. Pathological changes were more serious in the RT group than in the α2M+RT group at each time point. (E and F) RT group showed serious injuries with more regions of ulceration and erosion in the mucosa (E, scale bar, 2.5 mm) and tongue (F, scale bar, 100 µ m). Dotted lines indicate the basement membrane and black arrows indicate the ulcerated area. (B) *** P

    Journal: International Journal of Oncology

    Article Title: Effect of α2-macroglobulin in the early stage of jaw osteoradionecrosis

    doi: 10.3892/ijo.2020.5051

    Figure Lengend Snippet: Pathophysiological changes associated with osteoradionecrosis in the jaws of mice in the four groups. (A) Haematoxylin and eosin staining. RT group showed significant increase in cell loss and vessel injury at each time point compared with α2M + RT group (scale bar, 100 µ m). (B) Empty lacunae were observed in HPFs in all groups. (C) Masson's trichrome staining. α2M+RT group exhibited fewer fat vacuoles compared with RT group, but more than in the control group (scale bar, 100 µ m). (D) Fat vacuoles were evaluated in HPFs in all groups. Pathological changes were more serious in the RT group than in the α2M+RT group at each time point. (E and F) RT group showed serious injuries with more regions of ulceration and erosion in the mucosa (E, scale bar, 2.5 mm) and tongue (F, scale bar, 100 µ m). Dotted lines indicate the basement membrane and black arrows indicate the ulcerated area. (B) *** P

    Article Snippet: Following anesthesia with pentobarbital (1%; 50 mg/kg, intraperitoneal injection), a subperiosteal injection of 0.5 ml of 2 mg/ml α2M (cat. no. 441251-10MG; EMD Millipore) was prophylactically administered to mice from the α2M and α2M + RT groups 30 min prior to IR, whereas the control and RT groups were injected with the same volume of physiological saline.

    Techniques: Mouse Assay, Staining

    α2M increased SOD2 expression and decreased 8-OHdG level in bone and soft tissues after irradiation. (A and B) Level of 8-OHdG in bone from the α2M + RT group was lower than in the RT group. Scale bar, 100 µ m. (C and D) Levels of 8-OHdG in the tongue tissue after IR was lower in the α2M + RT group than in the RT group. Scale bar, 100 µ m. (E and F) SOD2 was expressed at higher level in the mucosa of the α2M + RT group than in the RT group. Scale bar, 100 µ m. (G and H) SOD2 was expressed at a higher level in the tongue tissue after IR in the α2M+RT group than the RT group. Scale bar, 100 µ m. * P

    Journal: International Journal of Oncology

    Article Title: Effect of α2-macroglobulin in the early stage of jaw osteoradionecrosis

    doi: 10.3892/ijo.2020.5051

    Figure Lengend Snippet: α2M increased SOD2 expression and decreased 8-OHdG level in bone and soft tissues after irradiation. (A and B) Level of 8-OHdG in bone from the α2M + RT group was lower than in the RT group. Scale bar, 100 µ m. (C and D) Levels of 8-OHdG in the tongue tissue after IR was lower in the α2M + RT group than in the RT group. Scale bar, 100 µ m. (E and F) SOD2 was expressed at higher level in the mucosa of the α2M + RT group than in the RT group. Scale bar, 100 µ m. (G and H) SOD2 was expressed at a higher level in the tongue tissue after IR in the α2M+RT group than the RT group. Scale bar, 100 µ m. * P

    Article Snippet: Following anesthesia with pentobarbital (1%; 50 mg/kg, intraperitoneal injection), a subperiosteal injection of 0.5 ml of 2 mg/ml α2M (cat. no. 441251-10MG; EMD Millipore) was prophylactically administered to mice from the α2M and α2M + RT groups 30 min prior to IR, whereas the control and RT groups were injected with the same volume of physiological saline.

    Techniques: Expressing, Irradiation

    Radiation-induced injury and clinical symptoms and quantitation of body weight and food intake in rats. (A) RT group showed serious symptoms, including drooling, alopecia, ulceration, exudation and superficial incrustation in the irradiated area at the early stage of osteoradionecrosis. (B) α2M + RT group exhibited mild damage and low levels of alopecia. Red arrows in Fig. 1A and the rectangles in Fig. 1B indicate areas affected by alopecia. (C and D) Signs of irradiation are red and swollen tongue with erosive lesions and atrophied mucosa in the RT group, whereas conditions of the mucosa and tongue were substantially better in the rats in the α2M + RT group compared with rats in the RT group. Red arrows in Fig. 1D indicate the ulcerated areas. (E and F) Weight and food intake of rats measured weekly. * P

    Journal: International Journal of Oncology

    Article Title: Effect of α2-macroglobulin in the early stage of jaw osteoradionecrosis

    doi: 10.3892/ijo.2020.5051

    Figure Lengend Snippet: Radiation-induced injury and clinical symptoms and quantitation of body weight and food intake in rats. (A) RT group showed serious symptoms, including drooling, alopecia, ulceration, exudation and superficial incrustation in the irradiated area at the early stage of osteoradionecrosis. (B) α2M + RT group exhibited mild damage and low levels of alopecia. Red arrows in Fig. 1A and the rectangles in Fig. 1B indicate areas affected by alopecia. (C and D) Signs of irradiation are red and swollen tongue with erosive lesions and atrophied mucosa in the RT group, whereas conditions of the mucosa and tongue were substantially better in the rats in the α2M + RT group compared with rats in the RT group. Red arrows in Fig. 1D indicate the ulcerated areas. (E and F) Weight and food intake of rats measured weekly. * P

    Article Snippet: Following anesthesia with pentobarbital (1%; 50 mg/kg, intraperitoneal injection), a subperiosteal injection of 0.5 ml of 2 mg/ml α2M (cat. no. 441251-10MG; EMD Millipore) was prophylactically administered to mice from the α2M and α2M + RT groups 30 min prior to IR, whereas the control and RT groups were injected with the same volume of physiological saline.

    Techniques: Quantitation Assay, Irradiation

    Spatio-temporal distribution of laminin-α1 and laminin-α5 in regenerating muscles. a Immunofluorescence analysis of laminin-α2 (green, top panels), laminin-α1 (green, middle panels), and laminin-α5 (gray, bottom panels) in regenerating TA muscle following cardiotoxin-mediated injury. Panels on the right are high magnification images of the 2 dpi images (indicated by a white rectangle, with small inserts showing the same image with the laminin channel only). The insert shown at 4 dpi in the laminin-α5 panels illustrates increased laminin α5 (white) deposition at the surface of satellite cells. White arrows indicate satellite cells. Yellow arrows indicate MyoD − or Pax7 − (GFP − ) cells positive for laminin-α1 or α5. Scale bar, 50 μm. b Quantification of the number of laminin-α1 + myogenic cells in regenerating muscles. c qPCR analysis of Lama1 and Lama5 gene expression in myofibers cultured for 0–72 h. n = 6 experiments. Graphs show mean + sem

    Journal: Nature Communications

    Article Title: Basal lamina remodeling at the skeletal muscle stem cell niche mediates stem cell self-renewal

    doi: 10.1038/s41467-018-03425-3

    Figure Lengend Snippet: Spatio-temporal distribution of laminin-α1 and laminin-α5 in regenerating muscles. a Immunofluorescence analysis of laminin-α2 (green, top panels), laminin-α1 (green, middle panels), and laminin-α5 (gray, bottom panels) in regenerating TA muscle following cardiotoxin-mediated injury. Panels on the right are high magnification images of the 2 dpi images (indicated by a white rectangle, with small inserts showing the same image with the laminin channel only). The insert shown at 4 dpi in the laminin-α5 panels illustrates increased laminin α5 (white) deposition at the surface of satellite cells. White arrows indicate satellite cells. Yellow arrows indicate MyoD − or Pax7 − (GFP − ) cells positive for laminin-α1 or α5. Scale bar, 50 μm. b Quantification of the number of laminin-α1 + myogenic cells in regenerating muscles. c qPCR analysis of Lama1 and Lama5 gene expression in myofibers cultured for 0–72 h. n = 6 experiments. Graphs show mean + sem

    Article Snippet: Primary antibodies used were anti-caveolin-1 (1:400; sc-894, Santa Cruz), anti-pax7 (1:20, DHSB), anti-myoD (1:1000; sc-304, Santa Cruz), anti-myf5 (1:2000; sc-302, Santa Cruz), anti-myogenin (1:50; F5D, DHSB), anti-laminin-α2 (1:200; 4H8–2, Enzo), anti-laminin-α1 (MAB-1903 at 1:200, Chemicon; mab200 at 1:2, and sc-65645 at 1:100, Santa Cruz), anti-laminin-α5 (1:10000; clone 405, a gift from L. Sorokin ), anti-laminin-α1 (1:200; MAB1905, Chemicon), anti-integrin-α6 (1:40; MCA699, AbD SeroTec), FITC anti-F4/80 (1:100; ab105155, AbCAM), FITC anti-CD206 (1:250; clone C068C2, BioLegend UK), anti-CD31 (1:100; AF3628, R & D Systems), anti-Collagen I (1:300; AB765P, Chemicon), anti-Ki67 (1:300; NCL-Ki67p, Novocastra), anti-MMP9 (1:200; sc-6841, Santa Cruz), anti-MMP2 (1: 300; sc-10736, Santa Cruz), and anti-Par3 (1:750; 07–330, Millipore).

    Techniques: Immunofluorescence, Real-time Polymerase Chain Reaction, Expressing, Cell Culture

    Laminin-α1 is essential for SC proliferation. a Control and Lama1 cko Tibialis anterior (TA) muscle analyzed at 14 days post injury by Haematoxylin and Eosin staining, and immunofluorescence for laminin-α2 (green), MyoD (red), and collagen I (red). Black and white arrowheads indicate the presence of smaller regenerated myofibers in Lama1 cko mice. White arrows indicate sites of fibrosis. The graph shows the minimal Feret diameter analysis of control and Lama1 cko TA muscles at 14 dpi. Scale bar, 50 μm. n = 3 per genotype. b Number of MyoD + cells in injured TA muscles at 2, 4, and 7 dpi in control and Lama1 cko mice. n = 3 per genotype. c Number of Ki67 + cells in injured TA muscles at 2 and 4 dpi in control and Lama1 cko mice. d Quantification of the number of satellite cells activated (blue), proliferating (yellow), self-renewing (green), and differentiating (purple) in a 72-hour ex-vivo culture of control, heterozygous, and Lama1 cko myofibers. n = 3 per genotype with 31–79 myofibers per time point. Graphs show mean + sem. * P

    Journal: Nature Communications

    Article Title: Basal lamina remodeling at the skeletal muscle stem cell niche mediates stem cell self-renewal

    doi: 10.1038/s41467-018-03425-3

    Figure Lengend Snippet: Laminin-α1 is essential for SC proliferation. a Control and Lama1 cko Tibialis anterior (TA) muscle analyzed at 14 days post injury by Haematoxylin and Eosin staining, and immunofluorescence for laminin-α2 (green), MyoD (red), and collagen I (red). Black and white arrowheads indicate the presence of smaller regenerated myofibers in Lama1 cko mice. White arrows indicate sites of fibrosis. The graph shows the minimal Feret diameter analysis of control and Lama1 cko TA muscles at 14 dpi. Scale bar, 50 μm. n = 3 per genotype. b Number of MyoD + cells in injured TA muscles at 2, 4, and 7 dpi in control and Lama1 cko mice. n = 3 per genotype. c Number of Ki67 + cells in injured TA muscles at 2 and 4 dpi in control and Lama1 cko mice. d Quantification of the number of satellite cells activated (blue), proliferating (yellow), self-renewing (green), and differentiating (purple) in a 72-hour ex-vivo culture of control, heterozygous, and Lama1 cko myofibers. n = 3 per genotype with 31–79 myofibers per time point. Graphs show mean + sem. * P

    Article Snippet: Primary antibodies used were anti-caveolin-1 (1:400; sc-894, Santa Cruz), anti-pax7 (1:20, DHSB), anti-myoD (1:1000; sc-304, Santa Cruz), anti-myf5 (1:2000; sc-302, Santa Cruz), anti-myogenin (1:50; F5D, DHSB), anti-laminin-α2 (1:200; 4H8–2, Enzo), anti-laminin-α1 (MAB-1903 at 1:200, Chemicon; mab200 at 1:2, and sc-65645 at 1:100, Santa Cruz), anti-laminin-α5 (1:10000; clone 405, a gift from L. Sorokin ), anti-laminin-α1 (1:200; MAB1905, Chemicon), anti-integrin-α6 (1:40; MCA699, AbD SeroTec), FITC anti-F4/80 (1:100; ab105155, AbCAM), FITC anti-CD206 (1:250; clone C068C2, BioLegend UK), anti-CD31 (1:100; AF3628, R & D Systems), anti-Collagen I (1:300; AB765P, Chemicon), anti-Ki67 (1:300; NCL-Ki67p, Novocastra), anti-MMP9 (1:200; sc-6841, Santa Cruz), anti-MMP2 (1: 300; sc-10736, Santa Cruz), and anti-Par3 (1:750; 07–330, Millipore).

    Techniques: Staining, Immunofluorescence, Mouse Assay, Ex Vivo

    Protease inhibitors alpha-2-macroglobulin (A2m) and proteinase 15 (Pi15) decrease MMP9 activity and expression in 17-week old mandibular condylar fibrocartilage. ( A ) Immunohistochemistry of A2m in all groups. ( B ) Explant study timeline and digital micrograph illustrating the mandible in culture for 48 hours of A2m treatment (0, 100, or 200 nM) or Pi15 treatment (0, 50, or 100 nM). ( C ) Zymogram using 10% gelatin substrate illustrating protease activity as a function of A2m dose ( D ) qPCR gene expression of MMP9 in A2m treatment explant culture. ( E ) Zymogram using 10% gelatin substrate illustrating protease activity as a function of Pi15 dose ( F . All values represent means ± standard deviation. n = 5 for explant culture datum, ^ p

    Journal: Scientific Reports

    Article Title: Estrogen Promotes Mandibular Condylar Fibrocartilage Chondrogenesis and Inhibits Degeneration via Estrogen Receptor Alpha in Female Mice

    doi: 10.1038/s41598-018-26937-w

    Figure Lengend Snippet: Protease inhibitors alpha-2-macroglobulin (A2m) and proteinase 15 (Pi15) decrease MMP9 activity and expression in 17-week old mandibular condylar fibrocartilage. ( A ) Immunohistochemistry of A2m in all groups. ( B ) Explant study timeline and digital micrograph illustrating the mandible in culture for 48 hours of A2m treatment (0, 100, or 200 nM) or Pi15 treatment (0, 50, or 100 nM). ( C ) Zymogram using 10% gelatin substrate illustrating protease activity as a function of A2m dose ( D ) qPCR gene expression of MMP9 in A2m treatment explant culture. ( E ) Zymogram using 10% gelatin substrate illustrating protease activity as a function of Pi15 dose ( F . All values represent means ± standard deviation. n = 5 for explant culture datum, ^ p

    Article Snippet: Following overnight incubation, media was removed, samples were washed 2 × with sterile PBS, and fresh media with either 0 M, 10−8 M, or 10−6 M 17β-estradiol (17β-estradiol, Sigma E2758, for the estradiol study), 100 nM and 200 nM A2m (from human plasma, Sigma SRP6314), or 50 nM and 100 nM Pi15 (synthetic – based on human peptide sequence, abcam ab23016) was added and incubated for 48 hours.

    Techniques: Activity Assay, Expressing, Immunohistochemistry, Real-time Polymerase Chain Reaction, Standard Deviation

    Estradiol via ERα upregulates anabolic extracellular matrix genes and downregulates catabolic genes in 17-week old mandibular condylar fibrocartilage. ( A ) Heat map illustrating upregulation of protease inhibitors and matrix proteins and downregulated of proteases with estradiol treatment in WT but not ERαKO samples. Z-score values were calculated by subtracting the sample mean from the raw expression value and divided by the standard deviation of the sample ( B ) qPCR gene expression of Pi15 an A2m in all WT and ERαKO groups. All values represent means ± standard deviation. n = 6 for PCR datum, ^ p

    Journal: Scientific Reports

    Article Title: Estrogen Promotes Mandibular Condylar Fibrocartilage Chondrogenesis and Inhibits Degeneration via Estrogen Receptor Alpha in Female Mice

    doi: 10.1038/s41598-018-26937-w

    Figure Lengend Snippet: Estradiol via ERα upregulates anabolic extracellular matrix genes and downregulates catabolic genes in 17-week old mandibular condylar fibrocartilage. ( A ) Heat map illustrating upregulation of protease inhibitors and matrix proteins and downregulated of proteases with estradiol treatment in WT but not ERαKO samples. Z-score values were calculated by subtracting the sample mean from the raw expression value and divided by the standard deviation of the sample ( B ) qPCR gene expression of Pi15 an A2m in all WT and ERαKO groups. All values represent means ± standard deviation. n = 6 for PCR datum, ^ p

    Article Snippet: Following overnight incubation, media was removed, samples were washed 2 × with sterile PBS, and fresh media with either 0 M, 10−8 M, or 10−6 M 17β-estradiol (17β-estradiol, Sigma E2758, for the estradiol study), 100 nM and 200 nM A2m (from human plasma, Sigma SRP6314), or 50 nM and 100 nM Pi15 (synthetic – based on human peptide sequence, abcam ab23016) was added and incubated for 48 hours.

    Techniques: Expressing, Standard Deviation, Real-time Polymerase Chain Reaction, Polymerase Chain Reaction

    The α1-, α2-, γ1-, γ2-, and γ3-subunits of AMPK are O -GlcNAcylated. A , recombinant AMPK-α1β1γ1 or -α2β1γ1 complexes were incubated with recombinant O -GlcNAc transferase

    Journal: The Journal of Biological Chemistry

    Article Title: Cross-talk between Two Essential Nutrient-sensitive Enzymes

    doi: 10.1074/jbc.M113.523068

    Figure Lengend Snippet: The α1-, α2-, γ1-, γ2-, and γ3-subunits of AMPK are O -GlcNAcylated. A , recombinant AMPK-α1β1γ1 or -α2β1γ1 complexes were incubated with recombinant O -GlcNAc transferase

    Article Snippet: Endogenous AMPK-α2, OGT, and phospho-T444 OGT (pT444-OGT) were immunoprecipitated from cell lysate using antibodies specific for AMPK-α2 (Santa Cruz Biotechnology), OGT (AL28), or pT444-OGT (custom), respectively.

    Techniques: Recombinant, Incubation

    Integrin α5 is necessary for P4G11-mediated restoration of epithelial junctions in vitro. (A) Immunoblot analysis of total levels of integrin α5, integrin β1, integrin α2, and β-actin in SW480 cells engineered to produce anti–integrin α5 shRNA in the presence (ON) or absence (OFF) of doxycycline. Two different shRNAs (A5sh1 and A5sh3) targeting different parts of the integrin α5 gene were compared. (B) Quantification of the percentage of invasive SC colonies present when cells in A were grown in 3D type 1 collagen and treated with P4G11 in the presence (shA5 +) or absence (shA5 –) of anti–integrin α5 shRNA. Note lack of response to P4G11 in colonies expressing anti–integrin α5 shRNA (mean ± SEM; > 300 colonies from three separate replicates). (C) Representative confocal image of cells in A grown in 3D type 1 collagen as in Figure 1 A and treated with P4G11 in presence (ON) or absence (OFF) of anti–integrin α5 shRNA (A5sh1 shown) stained with phalloidin (red) and DAPI (blue). Scale bar, 100 μm. (D) Representative maximum intensity projections of SW480 cells grown on MMC-coated coverglass stained with phalloidin (red), DAPI (blue), and an antibody against ZO-1 (green). Scale bar, 20 μm. (E) Quantification of number of cells exhibiting ZO-1 localization of cell–cell membranes through ImageJ analysis (see Materials and Methods ; mean ± SEM; more than five 20× fields of view from three separate replicates). (F) Representative XZ -plane reconstruction of cells in A stained with antibodies against ZO-1 (green), phalloidin (red), and DAPI (blue). Scale bar, 20 μm. Asterisks signify statistical significance with p

    Journal: Molecular Biology of the Cell

    Article Title: Clustering of integrin α5 at the lateral membrane restores epithelial polarity in invasive colorectal cancer cells

    doi: 10.1091/mbc.E16-12-0852

    Figure Lengend Snippet: Integrin α5 is necessary for P4G11-mediated restoration of epithelial junctions in vitro. (A) Immunoblot analysis of total levels of integrin α5, integrin β1, integrin α2, and β-actin in SW480 cells engineered to produce anti–integrin α5 shRNA in the presence (ON) or absence (OFF) of doxycycline. Two different shRNAs (A5sh1 and A5sh3) targeting different parts of the integrin α5 gene were compared. (B) Quantification of the percentage of invasive SC colonies present when cells in A were grown in 3D type 1 collagen and treated with P4G11 in the presence (shA5 +) or absence (shA5 –) of anti–integrin α5 shRNA. Note lack of response to P4G11 in colonies expressing anti–integrin α5 shRNA (mean ± SEM; > 300 colonies from three separate replicates). (C) Representative confocal image of cells in A grown in 3D type 1 collagen as in Figure 1 A and treated with P4G11 in presence (ON) or absence (OFF) of anti–integrin α5 shRNA (A5sh1 shown) stained with phalloidin (red) and DAPI (blue). Scale bar, 100 μm. (D) Representative maximum intensity projections of SW480 cells grown on MMC-coated coverglass stained with phalloidin (red), DAPI (blue), and an antibody against ZO-1 (green). Scale bar, 20 μm. (E) Quantification of number of cells exhibiting ZO-1 localization of cell–cell membranes through ImageJ analysis (see Materials and Methods ; mean ± SEM; more than five 20× fields of view from three separate replicates). (F) Representative XZ -plane reconstruction of cells in A stained with antibodies against ZO-1 (green), phalloidin (red), and DAPI (blue). Scale bar, 20 μm. Asterisks signify statistical significance with p

    Article Snippet: Antibodies for ezrin, fibronectin, paxillin, ZO-1, integrin α2, and TrfR were purchased from Abcam.

    Techniques: In Vitro, shRNA, Expressing, Staining

    Integrin α5 is present at the lateral surface in the terminally differentiated compartment of the normal human colon. (A) Representative confocal images of a normal human colon section stained with antibody against integrin α5 (green), phalloidin (red), and DAPI (blue); scale bar, 100 μm. High-magnification view of differentiated (1) and progenitor (2) regions of crypt. Scale bar, 50 μm. (B) High magnification of epithelial cells at the luminal surface stained with antibodies against integrin α5 (red), fibronectin (green), integrin β1 (blue), and DAPI (teal). (C–F) Sections of normal human colon stained with antibodies against integrin α5 (C), integrin β1 (D), fibronectin (E), and integrin α2 (F). Scale bars, 50 μm.

    Journal: Molecular Biology of the Cell

    Article Title: Clustering of integrin α5 at the lateral membrane restores epithelial polarity in invasive colorectal cancer cells

    doi: 10.1091/mbc.E16-12-0852

    Figure Lengend Snippet: Integrin α5 is present at the lateral surface in the terminally differentiated compartment of the normal human colon. (A) Representative confocal images of a normal human colon section stained with antibody against integrin α5 (green), phalloidin (red), and DAPI (blue); scale bar, 100 μm. High-magnification view of differentiated (1) and progenitor (2) regions of crypt. Scale bar, 50 μm. (B) High magnification of epithelial cells at the luminal surface stained with antibodies against integrin α5 (red), fibronectin (green), integrin β1 (blue), and DAPI (teal). (C–F) Sections of normal human colon stained with antibodies against integrin α5 (C), integrin β1 (D), fibronectin (E), and integrin α2 (F). Scale bars, 50 μm.

    Article Snippet: Antibodies for ezrin, fibronectin, paxillin, ZO-1, integrin α2, and TrfR were purchased from Abcam.

    Techniques: Staining

    P4G11 selectively induces membrane localization of integrin α5β1. (A) CC, SC, and SC treated with P4G11 were grown in 3D type 1 collagen as in Figure 1 A. Immunoblot analysis of total levels of integrin α5, integrin α2, and actin. (B) Representative XZ -plane reconstruction of CC, SC, and SC treated with P4G11, grown on MMC-coated Transwell filters for 5 d, and treated with P4G11 on days 5–6, stained with antibodies against integrin α5β1 (red), integrin α2 (green), and DAPI (blue). Scale bar, 20 μm. (C) Representative confocal image of SC cells treated with P4G11 for indicated lengths of time, stained with antibody against integrin α5β1 (red) and DAPI (blue). Scale bar, 20 μm. (D, E) Representative XZ -plane of SC cells grown on Transwell filters for 5 d, stained with antibodies against integrin α2 (H, green), TrfR (I, green), and DAPI (blue). Scale bar, 20 μm. (F) SC grown on Transwell filters as in B underwent cell-surface biotinylation at 4°C, followed by lysis and streptavidin (SA) pull down of biotinylated protein. Relative levels of integrin α5, integrin β1, integrin α2, and actin in total and after SA pull down were analyzed in each fraction by immunoblotting. (G) Levels of integrin α5 in F were quantified using ImageJ (mean ± SEM; n = 3). (H) Representative confocal image of SC treated with P4G11 in 3D type 1 collagen as in Figure 1 A, stained with antibody against integrin α5β1 green) and DAPI (blue). Scale bar, 20 μm. (I) Representative confocal image of SC treated with P4G11 in 3D type 1 collagen, stained with an antibody against integrin α2 (green) and DAPI (blue). Scale bar, 20 μm. Asterisks signify statistical significance with p

    Journal: Molecular Biology of the Cell

    Article Title: Clustering of integrin α5 at the lateral membrane restores epithelial polarity in invasive colorectal cancer cells

    doi: 10.1091/mbc.E16-12-0852

    Figure Lengend Snippet: P4G11 selectively induces membrane localization of integrin α5β1. (A) CC, SC, and SC treated with P4G11 were grown in 3D type 1 collagen as in Figure 1 A. Immunoblot analysis of total levels of integrin α5, integrin α2, and actin. (B) Representative XZ -plane reconstruction of CC, SC, and SC treated with P4G11, grown on MMC-coated Transwell filters for 5 d, and treated with P4G11 on days 5–6, stained with antibodies against integrin α5β1 (red), integrin α2 (green), and DAPI (blue). Scale bar, 20 μm. (C) Representative confocal image of SC cells treated with P4G11 for indicated lengths of time, stained with antibody against integrin α5β1 (red) and DAPI (blue). Scale bar, 20 μm. (D, E) Representative XZ -plane of SC cells grown on Transwell filters for 5 d, stained with antibodies against integrin α2 (H, green), TrfR (I, green), and DAPI (blue). Scale bar, 20 μm. (F) SC grown on Transwell filters as in B underwent cell-surface biotinylation at 4°C, followed by lysis and streptavidin (SA) pull down of biotinylated protein. Relative levels of integrin α5, integrin β1, integrin α2, and actin in total and after SA pull down were analyzed in each fraction by immunoblotting. (G) Levels of integrin α5 in F were quantified using ImageJ (mean ± SEM; n = 3). (H) Representative confocal image of SC treated with P4G11 in 3D type 1 collagen as in Figure 1 A, stained with antibody against integrin α5β1 green) and DAPI (blue). Scale bar, 20 μm. (I) Representative confocal image of SC treated with P4G11 in 3D type 1 collagen, stained with an antibody against integrin α2 (green) and DAPI (blue). Scale bar, 20 μm. Asterisks signify statistical significance with p

    Article Snippet: Antibodies for ezrin, fibronectin, paxillin, ZO-1, integrin α2, and TrfR were purchased from Abcam.

    Techniques: Staining, Lysis

    Cisplatin impedes migration by deterring Integrin/Fak signalling in aspirin pre-treated spheroids. ( A ) Percent Integrin-α2 (left panel), Integrin-α5 (middle panel) and Integrin-β1 (right panel) expression was represented graphically as detected by flow-cytometry in A549 parental cell and spheroids. ( B ) Western blot analysis of Integrin-α2, Integrin-α5, Integrin-β1 and p-FAK in untreated or aspirin/-cisplatin/-aspirin + cisplatin treated A549 spheroids. α-Actin was used as loading control. ( C ) Percent cell migration was calculated and represented graphically in control and Integrin-α2-siRNA, Integrin-α5–siRNA or Integrin-β1-siRNA transfected A549 spheroids as detected by transwell migration assay. The inset shows the immunoblot analysis of Integrinα2, Integrinα5 or Integrinβ1 levels for the transfection efficiency of Integrin-α2-siRNA, Integrin-α5–siRNA and Integrin-β1-siRNA respectively. ( D ) Protein expression levels of MMP-2 and MMP-9 in untreated or aspirin + cisplatin treated A549 spheroid. α-Actin served as loading control. Values are mean ± SEM of three independent experiments in each case or representative of typical experiment *p

    Journal: Scientific Reports

    Article Title: Aspirin enhances cisplatin sensitivity of resistant non-small cell lung carcinoma stem-like cells by targeting mTOR-Akt axis to repress migration

    doi: 10.1038/s41598-019-53134-0

    Figure Lengend Snippet: Cisplatin impedes migration by deterring Integrin/Fak signalling in aspirin pre-treated spheroids. ( A ) Percent Integrin-α2 (left panel), Integrin-α5 (middle panel) and Integrin-β1 (right panel) expression was represented graphically as detected by flow-cytometry in A549 parental cell and spheroids. ( B ) Western blot analysis of Integrin-α2, Integrin-α5, Integrin-β1 and p-FAK in untreated or aspirin/-cisplatin/-aspirin + cisplatin treated A549 spheroids. α-Actin was used as loading control. ( C ) Percent cell migration was calculated and represented graphically in control and Integrin-α2-siRNA, Integrin-α5–siRNA or Integrin-β1-siRNA transfected A549 spheroids as detected by transwell migration assay. The inset shows the immunoblot analysis of Integrinα2, Integrinα5 or Integrinβ1 levels for the transfection efficiency of Integrin-α2-siRNA, Integrin-α5–siRNA and Integrin-β1-siRNA respectively. ( D ) Protein expression levels of MMP-2 and MMP-9 in untreated or aspirin + cisplatin treated A549 spheroid. α-Actin served as loading control. Values are mean ± SEM of three independent experiments in each case or representative of typical experiment *p

    Article Snippet: This was further probed with specific antibodies , for example, anti- Akt/- p-Akt (Ser473)/- p-Akt (Thr308 )/- mTOR/- GSK-3β/- p- GSK-3β/-NFκB/- p300/- β-catenin/- snail/- slug/- Ub/- Integrin- α2/- Integrin- α5/- Integrin-β1/- p-FAK/- Integrin-α2/- Mmp-2/- Mmp-9 antibodies (Santa Cruz, CA, USA), thereafter the immunoblots were visualized by chemiluminescence (GE Biosciences, NJ, USA) . α- actin or HDAC-2 was used as loading control .

    Techniques: Migration, Expressing, Flow Cytometry, Cytometry, Western Blot, Transfection, Transwell Migration Assay