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  • 93
    Cell Signaling Technology Inc bub3
    Bub3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bub3/product/Cell Signaling Technology Inc
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    91
    Tocris ep1 ep3 receptor agonist sulprostone
    Ep1 Ep3 Receptor Agonist Sulprostone, supplied by Tocris, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Tocris cav channel blocker benidipine hcl
    Hv1a/GNA consumption does not affect honeybee learning and memory. ( a ) The rate of learning is reduced in the positive control (the calcium channel blocker, <t>benidipine</t> HCl; Ben), whereas acute exposure to Hv1a/GNA (Hv1a), or GNA, does not significantly influence olfactory learning relative to the control (Con). N control = 20, N GNA = 20, N Ben = 23, N Hv1a/GNA = 23. ( b ) Short term memory (STM) was impaired for the Ben group, but not for the other treatments (lsc comparisons against the control: GNA, p = 0.740, Ben, p = 0.025, Hv1a/GNA, p = 0.661). ( c ) The rate of learning was not significantly different for bees fed Hv1a/GNA for 7 days. N control = 26, N Hv1a/GNA = 20. ( d ) STM (10 min) and long term memory (24 h) were not significantly different for bees fed Hv1a/GNA prior to conditioning; con, control; Hv1a, Hv1a/GNA. Data represent mean response probabilities ± 95% CIs. (Online version in colour.)
    Cav Channel Blocker Benidipine Hcl, supplied by Tocris, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Novus Biologicals goat anti kif5b
    (A) Silver stained gel showing proteins co-purified by GST-pulldown from HEK293 cells expressing GST-Fat3 fusion proteins corresponding to proteins encoded by alternative splice isoforms, and mutants targeting the conserved Kif5-ID. Arrows mark a unique protein that binds the Kif5-ID of GST-Fat3 and GST-Fat3 (Y/F) mutants that was identified as <t>Kif5B</t> by mass spectrometry analysis. Asterisks show the position of purified GST-fusion proteins. (B) Western blot analysis of GST-pulldowns from HEK293 cells using a Kif5B antibody confirms the mass spec identification and further demonstrates the specificity of Kif5B binding to different Fat3 splice isoforms and mutants. (C) Western blot using an antibody against the Kinesin3 motor protein Kif1A demonstrates Kif1A expression in HEK293 cells but no binding to Fat3. As previously reported, Kif1A occasionally runs as a dimer when detected in whole tissue lysate such as brain . (D) Immunoprecipitation of YFP-Kif5B fusion protein using goat anti-GFP antibodies from HEK293 cells co-transfected with HA-tagged, membrane spanning Fat3 constructs. Immunoprecipitation using non-specific antisera (IgG) served as a negative control. (E) Immunoprecipitation of full length Fat3 from P2 mouse olfactory bulb using a mouse polyclonal antibody co-precipitated all endogenous Kif5 isoforms (Kif5A, Kif5B, Kif5C). Western blot analysis using a second, rabbit anti-Fat3 antibody demonstrated expression in this tissue and immunoprecipitation efficiency. (F) GST-pulldown of GST-Fat3 fusion proteins from HEK293 cells co-transfected with mCherry-KLC2. Western blot analysis using dsRed antibodies to detect mCherry demonstrate co-purification of mCherry-KLC2 with Fat3 regardless of splice isoform or mutation of a putative bipartite WD Kinesin binding motif.
    Goat Anti Kif5b, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Santa Cruz Biotechnology egfr
    <t>CXCR4</t> modulates <t>EGFR</t> protein expression and MMP-9 production. (A) EGFR expression was analyzed by western blot analysis of control, mock and CXCR4-expressing cells. β-tubulin was used as a loading control. (B) A representative result of gelatinolytic zymography demonstrated MMP-9 activity in the conditioned medium from control and CXCR4-expressing cells. Loading control, non-target protein bands in Coomassie Blue staining gel prior to transferring to a nitrocellulose membrane. CXCR4, CXC receptor 4; EGFR, epidermal growth factor 4; MMP-9, matrix metallopeptidase-9.
    Egfr, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Hv1a/GNA consumption does not affect honeybee learning and memory. ( a ) The rate of learning is reduced in the positive control (the calcium channel blocker, benidipine HCl; Ben), whereas acute exposure to Hv1a/GNA (Hv1a), or GNA, does not significantly influence olfactory learning relative to the control (Con). N control = 20, N GNA = 20, N Ben = 23, N Hv1a/GNA = 23. ( b ) Short term memory (STM) was impaired for the Ben group, but not for the other treatments (lsc comparisons against the control: GNA, p = 0.740, Ben, p = 0.025, Hv1a/GNA, p = 0.661). ( c ) The rate of learning was not significantly different for bees fed Hv1a/GNA for 7 days. N control = 26, N Hv1a/GNA = 20. ( d ) STM (10 min) and long term memory (24 h) were not significantly different for bees fed Hv1a/GNA prior to conditioning; con, control; Hv1a, Hv1a/GNA. Data represent mean response probabilities ± 95% CIs. (Online version in colour.)

    Journal: Proceedings of the Royal Society B: Biological Sciences

    Article Title: Novel biopesticide based on a spider venom peptide shows no adverse effects on honeybees

    doi: 10.1098/rspb.2014.0619

    Figure Lengend Snippet: Hv1a/GNA consumption does not affect honeybee learning and memory. ( a ) The rate of learning is reduced in the positive control (the calcium channel blocker, benidipine HCl; Ben), whereas acute exposure to Hv1a/GNA (Hv1a), or GNA, does not significantly influence olfactory learning relative to the control (Con). N control = 20, N GNA = 20, N Ben = 23, N Hv1a/GNA = 23. ( b ) Short term memory (STM) was impaired for the Ben group, but not for the other treatments (lsc comparisons against the control: GNA, p = 0.740, Ben, p = 0.025, Hv1a/GNA, p = 0.661). ( c ) The rate of learning was not significantly different for bees fed Hv1a/GNA for 7 days. N control = 26, N Hv1a/GNA = 20. ( d ) STM (10 min) and long term memory (24 h) were not significantly different for bees fed Hv1a/GNA prior to conditioning; con, control; Hv1a, Hv1a/GNA. Data represent mean response probabilities ± 95% CIs. (Online version in colour.)

    Article Snippet: The pesticide thiamethoxam (TMX) (Sigma Aldrich, 99% purity) and the CaV channel blocker benidipine HCl (Tocris Bioscience) were dissolved directly in 1 M sucrose solution for oral administration to adult forager bees.

    Techniques: Positive Control

    (A) Silver stained gel showing proteins co-purified by GST-pulldown from HEK293 cells expressing GST-Fat3 fusion proteins corresponding to proteins encoded by alternative splice isoforms, and mutants targeting the conserved Kif5-ID. Arrows mark a unique protein that binds the Kif5-ID of GST-Fat3 and GST-Fat3 (Y/F) mutants that was identified as Kif5B by mass spectrometry analysis. Asterisks show the position of purified GST-fusion proteins. (B) Western blot analysis of GST-pulldowns from HEK293 cells using a Kif5B antibody confirms the mass spec identification and further demonstrates the specificity of Kif5B binding to different Fat3 splice isoforms and mutants. (C) Western blot using an antibody against the Kinesin3 motor protein Kif1A demonstrates Kif1A expression in HEK293 cells but no binding to Fat3. As previously reported, Kif1A occasionally runs as a dimer when detected in whole tissue lysate such as brain . (D) Immunoprecipitation of YFP-Kif5B fusion protein using goat anti-GFP antibodies from HEK293 cells co-transfected with HA-tagged, membrane spanning Fat3 constructs. Immunoprecipitation using non-specific antisera (IgG) served as a negative control. (E) Immunoprecipitation of full length Fat3 from P2 mouse olfactory bulb using a mouse polyclonal antibody co-precipitated all endogenous Kif5 isoforms (Kif5A, Kif5B, Kif5C). Western blot analysis using a second, rabbit anti-Fat3 antibody demonstrated expression in this tissue and immunoprecipitation efficiency. (F) GST-pulldown of GST-Fat3 fusion proteins from HEK293 cells co-transfected with mCherry-KLC2. Western blot analysis using dsRed antibodies to detect mCherry demonstrate co-purification of mCherry-KLC2 with Fat3 regardless of splice isoform or mutation of a putative bipartite WD Kinesin binding motif.

    Journal: PLoS ONE

    Article Title: Disparate Regulatory Mechanisms Control Fat3 and P75 NTR Protein Transport through a Conserved Kif5-Interaction Domain

    doi: 10.1371/journal.pone.0165519

    Figure Lengend Snippet: (A) Silver stained gel showing proteins co-purified by GST-pulldown from HEK293 cells expressing GST-Fat3 fusion proteins corresponding to proteins encoded by alternative splice isoforms, and mutants targeting the conserved Kif5-ID. Arrows mark a unique protein that binds the Kif5-ID of GST-Fat3 and GST-Fat3 (Y/F) mutants that was identified as Kif5B by mass spectrometry analysis. Asterisks show the position of purified GST-fusion proteins. (B) Western blot analysis of GST-pulldowns from HEK293 cells using a Kif5B antibody confirms the mass spec identification and further demonstrates the specificity of Kif5B binding to different Fat3 splice isoforms and mutants. (C) Western blot using an antibody against the Kinesin3 motor protein Kif1A demonstrates Kif1A expression in HEK293 cells but no binding to Fat3. As previously reported, Kif1A occasionally runs as a dimer when detected in whole tissue lysate such as brain . (D) Immunoprecipitation of YFP-Kif5B fusion protein using goat anti-GFP antibodies from HEK293 cells co-transfected with HA-tagged, membrane spanning Fat3 constructs. Immunoprecipitation using non-specific antisera (IgG) served as a negative control. (E) Immunoprecipitation of full length Fat3 from P2 mouse olfactory bulb using a mouse polyclonal antibody co-precipitated all endogenous Kif5 isoforms (Kif5A, Kif5B, Kif5C). Western blot analysis using a second, rabbit anti-Fat3 antibody demonstrated expression in this tissue and immunoprecipitation efficiency. (F) GST-pulldown of GST-Fat3 fusion proteins from HEK293 cells co-transfected with mCherry-KLC2. Western blot analysis using dsRed antibodies to detect mCherry demonstrate co-purification of mCherry-KLC2 with Fat3 regardless of splice isoform or mutation of a putative bipartite WD Kinesin binding motif.

    Article Snippet: The following primary antibodies were used in this study: Rabbit anti-dsRed (Clontech #632496), Rat anti-E Cadherin (Life Technologies #13–1900), Rabbit anti-Fat3 and polyclonal Mouse anti-Fat3 (Lisa Goodrich, Harvard Medical School [ ]), Goat anti-GFP (Abcam #5450, IF and WB), Goat anti-GFP (Abcam #6673, IP only), Rabbit anti-GST (Cell Signaling Technology #2625S) Mouse anti-HA (Covance #MMS-101P), Mouse anti-Kif1A (BD Biosciences #612094), Rabbit anti-Kif5B (Thermo # PA1-642), Goat anti-Kif5B (Imgenex #IMG-3049), Rabbit anti-Kif5C (Acris # SP5236P), Mouse anti-Phospho-Tyrosine (Cell Signaling Technology #9411).

    Techniques: Staining, Purification, Expressing, Mass Spectrometry, Western Blot, Binding Assay, Immunoprecipitation, Transfection, Construct, Negative Control, Copurification, Mutagenesis

    (A) Two examples of individual polarized MDCK cells transfected with the apical surface marker P75-GFP (green) and membrane spanning HA-Fat3 (magenta) containing an intact Kif5-ID. (B) Individual MDCK cells transfected with HA-Fat3 (+32) (magenta) show restricted distribution of HA immunolabeling at the basolateral surface. (C) Individual MDCK cells transfected with HA-Fat3 (Y/E) (magenta) similarly show restricted distribution of HA immunolabeling to the basolateral surface. (D) Pairs of individual, polarized MDCK cells transfected with membrane spanning HA-Fat3 (magenta) and full-length YFP-Kif5B (green) or (E) the dominant negative Kif5B construct DN-Kif5B in which the motor domain is replaced with GFP (green). Kif5B was visualized using antibodies directed against GFP. (A-E) For each panel, MDCK cell profiles are the orthogonal view reconstructed from Z-stacks spanning the entire height of the cell obtained by structured illumination microscopy, and for one cell in each pair the apical surface is marked by an arrow. (D’&E’) E-cadherin immunolabeling (grayscale) marks the basolateral cell surfaces demonstrating that these cells have maintained apical-basolateral polarization.

    Journal: PLoS ONE

    Article Title: Disparate Regulatory Mechanisms Control Fat3 and P75 NTR Protein Transport through a Conserved Kif5-Interaction Domain

    doi: 10.1371/journal.pone.0165519

    Figure Lengend Snippet: (A) Two examples of individual polarized MDCK cells transfected with the apical surface marker P75-GFP (green) and membrane spanning HA-Fat3 (magenta) containing an intact Kif5-ID. (B) Individual MDCK cells transfected with HA-Fat3 (+32) (magenta) show restricted distribution of HA immunolabeling at the basolateral surface. (C) Individual MDCK cells transfected with HA-Fat3 (Y/E) (magenta) similarly show restricted distribution of HA immunolabeling to the basolateral surface. (D) Pairs of individual, polarized MDCK cells transfected with membrane spanning HA-Fat3 (magenta) and full-length YFP-Kif5B (green) or (E) the dominant negative Kif5B construct DN-Kif5B in which the motor domain is replaced with GFP (green). Kif5B was visualized using antibodies directed against GFP. (A-E) For each panel, MDCK cell profiles are the orthogonal view reconstructed from Z-stacks spanning the entire height of the cell obtained by structured illumination microscopy, and for one cell in each pair the apical surface is marked by an arrow. (D’&E’) E-cadherin immunolabeling (grayscale) marks the basolateral cell surfaces demonstrating that these cells have maintained apical-basolateral polarization.

    Article Snippet: The following primary antibodies were used in this study: Rabbit anti-dsRed (Clontech #632496), Rat anti-E Cadherin (Life Technologies #13–1900), Rabbit anti-Fat3 and polyclonal Mouse anti-Fat3 (Lisa Goodrich, Harvard Medical School [ ]), Goat anti-GFP (Abcam #5450, IF and WB), Goat anti-GFP (Abcam #6673, IP only), Rabbit anti-GST (Cell Signaling Technology #2625S) Mouse anti-HA (Covance #MMS-101P), Mouse anti-Kif1A (BD Biosciences #612094), Rabbit anti-Kif5B (Thermo # PA1-642), Goat anti-Kif5B (Imgenex #IMG-3049), Rabbit anti-Kif5C (Acris # SP5236P), Mouse anti-Phospho-Tyrosine (Cell Signaling Technology #9411).

    Techniques: Transfection, Marker, Immunolabeling, Dominant Negative Mutation, Construct, Microscopy

    (A) Immunoprecipitation of YFP-Kif5B fusion protein using GFP antibodies from HEK293 cells co-transfected with RFP-tagged P75 NTR constructs. Protein interactions required the conserved Kif5-ID and is lost when this domain is deleted (P75-RFP ΔDGGLYS ) and reduced when Y-308 is mutated (P75-RFP (Y/E) ) or replaced with non-phosphorylated phenylalanine. P75-RFP constructs are detected by antibodies against dsRed in Western blots, and immunoprecipitation using non-specific antisera (IgG) served as a negative control. P75-RFP doublets can be resolved with longer electrophoresis times as seen in total cell lysates. (B) HEK293 cell treatment with pervanadate promoted P75-GFP phosphorylation at Y-308 and enabled the co-precipitation of endogenous Kif5B and transfected P75-GFP. P75-GFP was precipitated using Goat (gt) anti-GFP antisera and then Western blotted using Rabbit (rb) anti-GFP to confirm that comparable amounts of P75-GFP were being evaluated for phosphorylation state and Kif5B binding in each condition. Enhanced protein binding and phosphorylation relied specifically on Y-308 and did not occur with P75-GFP (Y/E) mutants.

    Journal: PLoS ONE

    Article Title: Disparate Regulatory Mechanisms Control Fat3 and P75 NTR Protein Transport through a Conserved Kif5-Interaction Domain

    doi: 10.1371/journal.pone.0165519

    Figure Lengend Snippet: (A) Immunoprecipitation of YFP-Kif5B fusion protein using GFP antibodies from HEK293 cells co-transfected with RFP-tagged P75 NTR constructs. Protein interactions required the conserved Kif5-ID and is lost when this domain is deleted (P75-RFP ΔDGGLYS ) and reduced when Y-308 is mutated (P75-RFP (Y/E) ) or replaced with non-phosphorylated phenylalanine. P75-RFP constructs are detected by antibodies against dsRed in Western blots, and immunoprecipitation using non-specific antisera (IgG) served as a negative control. P75-RFP doublets can be resolved with longer electrophoresis times as seen in total cell lysates. (B) HEK293 cell treatment with pervanadate promoted P75-GFP phosphorylation at Y-308 and enabled the co-precipitation of endogenous Kif5B and transfected P75-GFP. P75-GFP was precipitated using Goat (gt) anti-GFP antisera and then Western blotted using Rabbit (rb) anti-GFP to confirm that comparable amounts of P75-GFP were being evaluated for phosphorylation state and Kif5B binding in each condition. Enhanced protein binding and phosphorylation relied specifically on Y-308 and did not occur with P75-GFP (Y/E) mutants.

    Article Snippet: The following primary antibodies were used in this study: Rabbit anti-dsRed (Clontech #632496), Rat anti-E Cadherin (Life Technologies #13–1900), Rabbit anti-Fat3 and polyclonal Mouse anti-Fat3 (Lisa Goodrich, Harvard Medical School [ ]), Goat anti-GFP (Abcam #5450, IF and WB), Goat anti-GFP (Abcam #6673, IP only), Rabbit anti-GST (Cell Signaling Technology #2625S) Mouse anti-HA (Covance #MMS-101P), Mouse anti-Kif1A (BD Biosciences #612094), Rabbit anti-Kif5B (Thermo # PA1-642), Goat anti-Kif5B (Imgenex #IMG-3049), Rabbit anti-Kif5C (Acris # SP5236P), Mouse anti-Phospho-Tyrosine (Cell Signaling Technology #9411).

    Techniques: Immunoprecipitation, Transfection, Construct, Western Blot, Negative Control, Electrophoresis, Binding Assay, Protein Binding

    CXCR4 modulates EGFR protein expression and MMP-9 production. (A) EGFR expression was analyzed by western blot analysis of control, mock and CXCR4-expressing cells. β-tubulin was used as a loading control. (B) A representative result of gelatinolytic zymography demonstrated MMP-9 activity in the conditioned medium from control and CXCR4-expressing cells. Loading control, non-target protein bands in Coomassie Blue staining gel prior to transferring to a nitrocellulose membrane. CXCR4, CXC receptor 4; EGFR, epidermal growth factor 4; MMP-9, matrix metallopeptidase-9.

    Journal: Oncology Letters

    Article Title: Overexpression of CXCR4 promotes invasion and migration of non-small cell lung cancer via EGFR and MMP-9

    doi: 10.3892/ol.2017.7168

    Figure Lengend Snippet: CXCR4 modulates EGFR protein expression and MMP-9 production. (A) EGFR expression was analyzed by western blot analysis of control, mock and CXCR4-expressing cells. β-tubulin was used as a loading control. (B) A representative result of gelatinolytic zymography demonstrated MMP-9 activity in the conditioned medium from control and CXCR4-expressing cells. Loading control, non-target protein bands in Coomassie Blue staining gel prior to transferring to a nitrocellulose membrane. CXCR4, CXC receptor 4; EGFR, epidermal growth factor 4; MMP-9, matrix metallopeptidase-9.

    Article Snippet: Monoclonal antibodies against the following were used: CXCR4 (catalog no. ab1760; Abcam, Cambridge, UK); EGFR (catalog no. sc-3049; Santa Cruz Biotechnology, Inc., Dallas, TX, USA); β-tubulin (catalog no. 560340; BD Pharmingen; BD Biosciences, San Jose, CA, USA); and MMP-9 antibody (5G3; catalog no. ab119906; Abcam).

    Techniques: Expressing, Western Blot, Zymography, Activity Assay, Staining, Transferring

    CXCR4 knockdown inhibits cell migration and invasion induced by EGFR expression in A549 cells. (A) Western blot analysis demonstrated the expression levels of CXCR4 and EGFR in A549 cells transfected with scramble or CXCR4 siRNA. (B) Conditioned medium was prepared from A549 cells transfected with scramble or CXCR4 siRNA, and MMP-9 activity was detected by gelatinolytic zymography. Loading control, non-target protein bands in Coomassie Blue staining gel prior to transferal onto a nitrocellulose membrane. A549 cells transfected with scramble or CXCR4 siRNA were subjected to a Transwell migration assay with (C) Col-I or (D) fibronectin. Results are the mean ± standard deviation (*P<0.05). A549 cells transfected with scramble or CXCR4 siRNA were subjected to a Transwell invasion assay on Transwells coated with (E) Matrigel or (F) Col-I. Results are the mean ± standard deviation (*P<0.05). CXCR4, CXC receptor 4; EGFR, epidermal growth factor 4; MMP-9, matrix metallopeptidase-9; siRNA, small interfering RNA; Col-I, collagen type I; SD, standard deviation.

    Journal: Oncology Letters

    Article Title: Overexpression of CXCR4 promotes invasion and migration of non-small cell lung cancer via EGFR and MMP-9

    doi: 10.3892/ol.2017.7168

    Figure Lengend Snippet: CXCR4 knockdown inhibits cell migration and invasion induced by EGFR expression in A549 cells. (A) Western blot analysis demonstrated the expression levels of CXCR4 and EGFR in A549 cells transfected with scramble or CXCR4 siRNA. (B) Conditioned medium was prepared from A549 cells transfected with scramble or CXCR4 siRNA, and MMP-9 activity was detected by gelatinolytic zymography. Loading control, non-target protein bands in Coomassie Blue staining gel prior to transferal onto a nitrocellulose membrane. A549 cells transfected with scramble or CXCR4 siRNA were subjected to a Transwell migration assay with (C) Col-I or (D) fibronectin. Results are the mean ± standard deviation (*P<0.05). A549 cells transfected with scramble or CXCR4 siRNA were subjected to a Transwell invasion assay on Transwells coated with (E) Matrigel or (F) Col-I. Results are the mean ± standard deviation (*P<0.05). CXCR4, CXC receptor 4; EGFR, epidermal growth factor 4; MMP-9, matrix metallopeptidase-9; siRNA, small interfering RNA; Col-I, collagen type I; SD, standard deviation.

    Article Snippet: Monoclonal antibodies against the following were used: CXCR4 (catalog no. ab1760; Abcam, Cambridge, UK); EGFR (catalog no. sc-3049; Santa Cruz Biotechnology, Inc., Dallas, TX, USA); β-tubulin (catalog no. 560340; BD Pharmingen; BD Biosciences, San Jose, CA, USA); and MMP-9 antibody (5G3; catalog no. ab119906; Abcam).

    Techniques: Migration, Expressing, Western Blot, Transfection, Activity Assay, Zymography, Staining, Transwell Migration Assay, Standard Deviation, Transwell Invasion Assay, Small Interfering RNA

    EGFR, CXCR4 and MMP-9 expression in NSCLC. (A) Hematoxylin and eosin staining is exhibited. (B) The expression of CXCR4, (C) EGFR and (D) MMP-9 in normal lung tissue and NSCLC tissue was examined using immunohistochemistry (magnification, ×40). CXCR4, CXC receptor 4; EGFR, epidermal growth factor 4; MMP-9, matrix metallopeptidase-9; NSCLC, non-small cell lung cancer.

    Journal: Oncology Letters

    Article Title: Overexpression of CXCR4 promotes invasion and migration of non-small cell lung cancer via EGFR and MMP-9

    doi: 10.3892/ol.2017.7168

    Figure Lengend Snippet: EGFR, CXCR4 and MMP-9 expression in NSCLC. (A) Hematoxylin and eosin staining is exhibited. (B) The expression of CXCR4, (C) EGFR and (D) MMP-9 in normal lung tissue and NSCLC tissue was examined using immunohistochemistry (magnification, ×40). CXCR4, CXC receptor 4; EGFR, epidermal growth factor 4; MMP-9, matrix metallopeptidase-9; NSCLC, non-small cell lung cancer.

    Article Snippet: Monoclonal antibodies against the following were used: CXCR4 (catalog no. ab1760; Abcam, Cambridge, UK); EGFR (catalog no. sc-3049; Santa Cruz Biotechnology, Inc., Dallas, TX, USA); β-tubulin (catalog no. 560340; BD Pharmingen; BD Biosciences, San Jose, CA, USA); and MMP-9 antibody (5G3; catalog no. ab119906; Abcam).

    Techniques: Expressing, Staining, Immunohistochemistry

    Association between  EGFR,   CXCR4  and MMP-9 expression and clinicopathological factors in NSCLC.

    Journal: Oncology Letters

    Article Title: Overexpression of CXCR4 promotes invasion and migration of non-small cell lung cancer via EGFR and MMP-9

    doi: 10.3892/ol.2017.7168

    Figure Lengend Snippet: Association between EGFR, CXCR4 and MMP-9 expression and clinicopathological factors in NSCLC.

    Article Snippet: Monoclonal antibodies against the following were used: CXCR4 (catalog no. ab1760; Abcam, Cambridge, UK); EGFR (catalog no. sc-3049; Santa Cruz Biotechnology, Inc., Dallas, TX, USA); β-tubulin (catalog no. 560340; BD Pharmingen; BD Biosciences, San Jose, CA, USA); and MMP-9 antibody (5G3; catalog no. ab119906; Abcam).

    Techniques: Expressing

    Spearman's rank correlation analysis of clinical association between  CXCR4  and  EGFR.

    Journal: Oncology Letters

    Article Title: Overexpression of CXCR4 promotes invasion and migration of non-small cell lung cancer via EGFR and MMP-9

    doi: 10.3892/ol.2017.7168

    Figure Lengend Snippet: Spearman's rank correlation analysis of clinical association between CXCR4 and EGFR.

    Article Snippet: Monoclonal antibodies against the following were used: CXCR4 (catalog no. ab1760; Abcam, Cambridge, UK); EGFR (catalog no. sc-3049; Santa Cruz Biotechnology, Inc., Dallas, TX, USA); β-tubulin (catalog no. 560340; BD Pharmingen; BD Biosciences, San Jose, CA, USA); and MMP-9 antibody (5G3; catalog no. ab119906; Abcam).

    Techniques: Expressing

    Kaplan-Meier estimates of overall survival according to the expression of (A) CXCR4, (B) EGFR and (C) MMP-9. CXCR4, CXC receptor 4; EGFR, epidermal growth factor 4; MMP-9, matrix metallopeptidase-9.

    Journal: Oncology Letters

    Article Title: Overexpression of CXCR4 promotes invasion and migration of non-small cell lung cancer via EGFR and MMP-9

    doi: 10.3892/ol.2017.7168

    Figure Lengend Snippet: Kaplan-Meier estimates of overall survival according to the expression of (A) CXCR4, (B) EGFR and (C) MMP-9. CXCR4, CXC receptor 4; EGFR, epidermal growth factor 4; MMP-9, matrix metallopeptidase-9.

    Article Snippet: Monoclonal antibodies against the following were used: CXCR4 (catalog no. ab1760; Abcam, Cambridge, UK); EGFR (catalog no. sc-3049; Santa Cruz Biotechnology, Inc., Dallas, TX, USA); β-tubulin (catalog no. 560340; BD Pharmingen; BD Biosciences, San Jose, CA, USA); and MMP-9 antibody (5G3; catalog no. ab119906; Abcam).

    Techniques: Expressing