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    Abcam immunohistochemical staining immunohistochemical staining
    Representative image of <t>immunohistochemical</t> staining in patients with pulmonary pleomorphic carcinoma (PPC). ( a ) Immunopositivity for VEGFR2 in resected samples was observed mainly in the cytoplasm, with some samples also showing positive staining on the cellular membrane. ( b ) Immunopositivity for STMN1 showed a score of grade 4 and positive staining in the cytoplasm. ( c ) Immunopositivity for TUBB3 showed an H-score of 7 and positive staining in the cytoplasm. ( d ) Immunopositivity for TS showed a score of grade 5 and positive staining in nuclei and the cytoplasm. ( e ) Immunopositivity for Topo-II showed a score of grade 5 and positive staining in nuclei. ( f ) Immunopositivity for glucose-regulated protein and 78 kDa (GRP78/BiP) showed a score of grade 5 and positive staining in the cytoplasm. STMN1, stathmin 1; Topo-II, topoisomerase II; TS, thymidylate synthase; TUBB3, tubulin β3 class III; VEGFR2, vascular endothelial growth factor receptor 2. Original magnification, ×200.
    Immunohistochemical Staining Immunohistochemical Staining, supplied by Abcam, used in various techniques. Bioz Stars score: 90/100, based on 398 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/immunohistochemical staining immunohistochemical staining/product/Abcam
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    immunohistochemical staining immunohistochemical staining - by Bioz Stars, 2020-09
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    Images

    1) Product Images from "Clinical Significance of Various Drug-Sensitivity Markers in Patients with Surgically Resected Pulmonary Pleomorphic Carcinoma"

    Article Title: Clinical Significance of Various Drug-Sensitivity Markers in Patients with Surgically Resected Pulmonary Pleomorphic Carcinoma

    Journal: Cancers

    doi: 10.3390/cancers11111636

    Representative image of immunohistochemical staining in patients with pulmonary pleomorphic carcinoma (PPC). ( a ) Immunopositivity for VEGFR2 in resected samples was observed mainly in the cytoplasm, with some samples also showing positive staining on the cellular membrane. ( b ) Immunopositivity for STMN1 showed a score of grade 4 and positive staining in the cytoplasm. ( c ) Immunopositivity for TUBB3 showed an H-score of 7 and positive staining in the cytoplasm. ( d ) Immunopositivity for TS showed a score of grade 5 and positive staining in nuclei and the cytoplasm. ( e ) Immunopositivity for Topo-II showed a score of grade 5 and positive staining in nuclei. ( f ) Immunopositivity for glucose-regulated protein and 78 kDa (GRP78/BiP) showed a score of grade 5 and positive staining in the cytoplasm. STMN1, stathmin 1; Topo-II, topoisomerase II; TS, thymidylate synthase; TUBB3, tubulin β3 class III; VEGFR2, vascular endothelial growth factor receptor 2. Original magnification, ×200.
    Figure Legend Snippet: Representative image of immunohistochemical staining in patients with pulmonary pleomorphic carcinoma (PPC). ( a ) Immunopositivity for VEGFR2 in resected samples was observed mainly in the cytoplasm, with some samples also showing positive staining on the cellular membrane. ( b ) Immunopositivity for STMN1 showed a score of grade 4 and positive staining in the cytoplasm. ( c ) Immunopositivity for TUBB3 showed an H-score of 7 and positive staining in the cytoplasm. ( d ) Immunopositivity for TS showed a score of grade 5 and positive staining in nuclei and the cytoplasm. ( e ) Immunopositivity for Topo-II showed a score of grade 5 and positive staining in nuclei. ( f ) Immunopositivity for glucose-regulated protein and 78 kDa (GRP78/BiP) showed a score of grade 5 and positive staining in the cytoplasm. STMN1, stathmin 1; Topo-II, topoisomerase II; TS, thymidylate synthase; TUBB3, tubulin β3 class III; VEGFR2, vascular endothelial growth factor receptor 2. Original magnification, ×200.

    Techniques Used: Immunohistochemistry, Staining

    2) Product Images from "Clinical Significance of Various Drug-Sensitivity Markers in Patients with Surgically Resected Pulmonary Pleomorphic Carcinoma"

    Article Title: Clinical Significance of Various Drug-Sensitivity Markers in Patients with Surgically Resected Pulmonary Pleomorphic Carcinoma

    Journal: Cancers

    doi: 10.3390/cancers11111636

    Representative image of immunohistochemical staining in patients with pulmonary pleomorphic carcinoma (PPC). ( a ) Immunopositivity for VEGFR2 in resected samples was observed mainly in the cytoplasm, with some samples also showing positive staining on the cellular membrane. ( b ) Immunopositivity for STMN1 showed a score of grade 4 and positive staining in the cytoplasm. ( c ) Immunopositivity for TUBB3 showed an H-score of 7 and positive staining in the cytoplasm. ( d ) Immunopositivity for TS showed a score of grade 5 and positive staining in nuclei and the cytoplasm. ( e ) Immunopositivity for Topo-II showed a score of grade 5 and positive staining in nuclei. ( f ) Immunopositivity for glucose-regulated protein and 78 kDa (GRP78/BiP) showed a score of grade 5 and positive staining in the cytoplasm. STMN1, stathmin 1; Topo-II, topoisomerase II; TS, thymidylate synthase; TUBB3, tubulin β3 class III; VEGFR2, vascular endothelial growth factor receptor 2. Original magnification, ×200.
    Figure Legend Snippet: Representative image of immunohistochemical staining in patients with pulmonary pleomorphic carcinoma (PPC). ( a ) Immunopositivity for VEGFR2 in resected samples was observed mainly in the cytoplasm, with some samples also showing positive staining on the cellular membrane. ( b ) Immunopositivity for STMN1 showed a score of grade 4 and positive staining in the cytoplasm. ( c ) Immunopositivity for TUBB3 showed an H-score of 7 and positive staining in the cytoplasm. ( d ) Immunopositivity for TS showed a score of grade 5 and positive staining in nuclei and the cytoplasm. ( e ) Immunopositivity for Topo-II showed a score of grade 5 and positive staining in nuclei. ( f ) Immunopositivity for glucose-regulated protein and 78 kDa (GRP78/BiP) showed a score of grade 5 and positive staining in the cytoplasm. STMN1, stathmin 1; Topo-II, topoisomerase II; TS, thymidylate synthase; TUBB3, tubulin β3 class III; VEGFR2, vascular endothelial growth factor receptor 2. Original magnification, ×200.

    Techniques Used: Immunohistochemistry, Staining

    Kaplan-Meier survival curves for patients exhibiting differential marker levels. Kaplan-Meier plots showing OS according to ( a ) VEGFR2 level (VEGFR2-high/-low) [VEGFR2-high, median = 352 days; VEGFR2-low, median = 1209 days (log-rank: p
    Figure Legend Snippet: Kaplan-Meier survival curves for patients exhibiting differential marker levels. Kaplan-Meier plots showing OS according to ( a ) VEGFR2 level (VEGFR2-high/-low) [VEGFR2-high, median = 352 days; VEGFR2-low, median = 1209 days (log-rank: p

    Techniques Used: Marker

    3) Product Images from "Chromokinesin KIF4A teams up with stathmin 1 to regulate abscission in a SUMO-dependent manner"

    Article Title: Chromokinesin KIF4A teams up with stathmin 1 to regulate abscission in a SUMO-dependent manner

    Journal: Journal of Cell Science

    doi: 10.1242/jcs.248591

    The human chromokinesin KIF4A is modified by a single SUMO moiety. (A) Chromokinesin KIF4A is required for the positioning of mitotic chromosomes and stabilization of the bipolar spindle. In cytokinesis, KIF4A localizes at the intercellular bridge. The post-translational modifier SUMO is required for mitosis, and is conjugated to KIF4A. In this project, we investigate the functional role of KIF4A SUMOylation. (B) U2OS cells without or with stable expression of His 10 –SUMO2 were lysed. A His 10 pulldown was performed to enrich for SUMOylated proteins. Input and pulldown samples were analyzed by immunoblotting using antibodies against KIF4A and SUMO2/3. (C) U2OS cells were transfected with a control or HA–KIF4A WT construct and lysed after 3 days. An HA IP was performed to enrich HA-KIF4A WT. Input and IP samples were analyzed by immunoblotting using antibodies against SUMO2/3 or the HA tag. (D) U2OS cells were transfected with a construct encoding HA–KIF4A WT, lysed after 3 days and an HA IP was performed. The purified HA-KIF4A WT was in vitro SUMOylated by the addition of SUMO E1 and SUMO E2, and either incubated at 4°C for 3 h with the indicated concentrations of SUMO2 (left) or for the indicated time with 220 ng/µl SUMO2 (right). Samples were analyzed by immunoblotting using an antibody against the HA-tag. The experimental procedures for B–D are summarized in the cartoons on the right. Each experiment was performed at least three times.
    Figure Legend Snippet: The human chromokinesin KIF4A is modified by a single SUMO moiety. (A) Chromokinesin KIF4A is required for the positioning of mitotic chromosomes and stabilization of the bipolar spindle. In cytokinesis, KIF4A localizes at the intercellular bridge. The post-translational modifier SUMO is required for mitosis, and is conjugated to KIF4A. In this project, we investigate the functional role of KIF4A SUMOylation. (B) U2OS cells without or with stable expression of His 10 –SUMO2 were lysed. A His 10 pulldown was performed to enrich for SUMOylated proteins. Input and pulldown samples were analyzed by immunoblotting using antibodies against KIF4A and SUMO2/3. (C) U2OS cells were transfected with a control or HA–KIF4A WT construct and lysed after 3 days. An HA IP was performed to enrich HA-KIF4A WT. Input and IP samples were analyzed by immunoblotting using antibodies against SUMO2/3 or the HA tag. (D) U2OS cells were transfected with a construct encoding HA–KIF4A WT, lysed after 3 days and an HA IP was performed. The purified HA-KIF4A WT was in vitro SUMOylated by the addition of SUMO E1 and SUMO E2, and either incubated at 4°C for 3 h with the indicated concentrations of SUMO2 (left) or for the indicated time with 220 ng/µl SUMO2 (right). Samples were analyzed by immunoblotting using an antibody against the HA-tag. The experimental procedures for B–D are summarized in the cartoons on the right. Each experiment was performed at least three times.

    Techniques Used: Modification, Functional Assay, Expressing, Transfection, Construct, Purification, In Vitro, Incubation

    The localization of endogenous KIF4A during mitosis is not dependent on SUMOylation. (A) Three KIF4A mutant (K460R) clones and their KIF4A wild-type (WT) control clones obtained by CRISPR-Cas9-directed genome editing were infected with lentivirus encoding His 10 –SUMO2 and selected with puromycin to obtain stable cell lines. Subsequently, these cells were lysed. A His 10 pulldown was performed to enrich for SUMOylated proteins. Input and pulldown samples were analyzed by immunoblotting using antibodies against KIF4A and SUMO2/3, while Ponceau S staining was used to confirm equal loading. (B,C) U2OS clone 1 with (B) endogenous KIF4A (WT) or (C) with endogenous SUMOylation-deficient KIF4A (K460R) were grown on glass slides, fixed and stained with antibodies against KIF4A (green), tubulin (red) and Hoechst 33258 to visualize DNA (blue). Representative images were taken of cells in subsequent stages of mitosis to visualize KIF4A localization. Arrows highlight midzones and midbodies. Each experiment was performed at least three times. Scale bars: 10 µm.
    Figure Legend Snippet: The localization of endogenous KIF4A during mitosis is not dependent on SUMOylation. (A) Three KIF4A mutant (K460R) clones and their KIF4A wild-type (WT) control clones obtained by CRISPR-Cas9-directed genome editing were infected with lentivirus encoding His 10 –SUMO2 and selected with puromycin to obtain stable cell lines. Subsequently, these cells were lysed. A His 10 pulldown was performed to enrich for SUMOylated proteins. Input and pulldown samples were analyzed by immunoblotting using antibodies against KIF4A and SUMO2/3, while Ponceau S staining was used to confirm equal loading. (B,C) U2OS clone 1 with (B) endogenous KIF4A (WT) or (C) with endogenous SUMOylation-deficient KIF4A (K460R) were grown on glass slides, fixed and stained with antibodies against KIF4A (green), tubulin (red) and Hoechst 33258 to visualize DNA (blue). Representative images were taken of cells in subsequent stages of mitosis to visualize KIF4A localization. Arrows highlight midzones and midbodies. Each experiment was performed at least three times. Scale bars: 10 µm.

    Techniques Used: Mutagenesis, Clone Assay, CRISPR, Infection, Stable Transfection, Staining

    KIF4A is SUMOylated on lysine 460 in a SIM-dependent manner. (A) U2OS cells without or with stable expression of His 10 –SUMO2 were transfected with a control, HA–KIF4A WT or indicated mutant construct and lysed after 3 days. A His 10 pulldown was performed to enrich for SUMOylated proteins. The samples were analyzed by immunoblotting using antibodies against the HA tag and SUMO2/3, while equal loading was confirmed by Ponceau S staining. (B) U2OS cells were transfected with plasmids encoding HA–KIF4A WT or the indicated mutants, lysed after 3 days, and the HA-tagged proteins were enriched by IP. An in vitro SUMOylation assay was performed by the addition of SUMO E1 and SUMO E2, followed by incubation for 3 h at 4°C in the presence of 220 ng/µl SUMO2. Samples were analyzed by immunoblotting using an antibody against the HA tag. (C) U2OS cells without or with stable expression of His 10 –SUMO2 were transfected with control plasmid, or plasmids encoding HA–KIF4A WT, HA–KIF4A E458A or HA–KIF4A E461A that either did not or did contain additional mutations to abolish the SUMO interaction motif (SIM ILDLL mutated to AADAA). After 3 days, cells were lysed. Upon enrichment for SUMOylated proteins by His 10 pulldown, samples were analyzed by immunoblotting with antibodies against the HA tag or SUMO2/3, and by Ponceau S staining to confirm equal loading. Each experiment was performed at least three times. (D) A cartoon depicting the proposed mechanism of KIF4A SUMOylation in human cells. The SUMO E2 (UBC9)–SUMO complex interacts with the KIF4A dimer via the SIM in its head domain. Subsequently, UBC9 is able to covalently attach SUMO to lysine 460 in the stalk domain, either directly through the inverted consensus motif (ExK) or with the help of a SUMO E3 ligase through the second motif (KE).
    Figure Legend Snippet: KIF4A is SUMOylated on lysine 460 in a SIM-dependent manner. (A) U2OS cells without or with stable expression of His 10 –SUMO2 were transfected with a control, HA–KIF4A WT or indicated mutant construct and lysed after 3 days. A His 10 pulldown was performed to enrich for SUMOylated proteins. The samples were analyzed by immunoblotting using antibodies against the HA tag and SUMO2/3, while equal loading was confirmed by Ponceau S staining. (B) U2OS cells were transfected with plasmids encoding HA–KIF4A WT or the indicated mutants, lysed after 3 days, and the HA-tagged proteins were enriched by IP. An in vitro SUMOylation assay was performed by the addition of SUMO E1 and SUMO E2, followed by incubation for 3 h at 4°C in the presence of 220 ng/µl SUMO2. Samples were analyzed by immunoblotting using an antibody against the HA tag. (C) U2OS cells without or with stable expression of His 10 –SUMO2 were transfected with control plasmid, or plasmids encoding HA–KIF4A WT, HA–KIF4A E458A or HA–KIF4A E461A that either did not or did contain additional mutations to abolish the SUMO interaction motif (SIM ILDLL mutated to AADAA). After 3 days, cells were lysed. Upon enrichment for SUMOylated proteins by His 10 pulldown, samples were analyzed by immunoblotting with antibodies against the HA tag or SUMO2/3, and by Ponceau S staining to confirm equal loading. Each experiment was performed at least three times. (D) A cartoon depicting the proposed mechanism of KIF4A SUMOylation in human cells. The SUMO E2 (UBC9)–SUMO complex interacts with the KIF4A dimer via the SIM in its head domain. Subsequently, UBC9 is able to covalently attach SUMO to lysine 460 in the stalk domain, either directly through the inverted consensus motif (ExK) or with the help of a SUMO E3 ligase through the second motif (KE).

    Techniques Used: Expressing, Transfection, Mutagenesis, Construct, Staining, In Vitro, Incubation, Plasmid Preparation

    4) Product Images from "microRNA-dependent regulation of biomechanical genes establishes tissue stiffness homeostasis"

    Article Title: microRNA-dependent regulation of biomechanical genes establishes tissue stiffness homeostasis

    Journal: Nature cell biology

    doi: 10.1038/s41556-019-0272-y

    Post-transcriptional regulation of individual CAM genes limits ECs spreading, YAP signaling and/or contractility. ( a ) Experimental strategy to mutate individual MREs in CAM genes’ 3’UTRs to block miRNA binding ( Methods and Supplementary Fig. 2b ). ( b ) Representative immunofluorescence images (top, scale bar = 50μm) and Western blot (bottom) of CAM proteins as indicated (CTGF ~37 kDa, STMN1 ~19kDa, VCL ~116kDa, RHOB ~25kDa, Actin ~47kDa). HUVECs were infected with lentivirus carrying Cas9 and gRNA targeting specific CAM MREs and no-target gRNA ( a ) and processed at 7 days post infection. ( b ) Quantification of cell spreading (n=99, 75, 91, 94, 88, 87, 79, 54, 83 from bottom to top, representative data from two independent experiments), YAP nuclear translocation (n=91, 81, 87, 93, 79, 88, 67, 54, 84 cells from bottom to top, representative data from two independent experiments) and total force per cell (n= 38, 33, 37, 36, 34, 34, 34, 30, 36 cells from bottom to top, from two independent experiments) in HUVECs on 3 kPa PDMS gels for 48 h after mutation of the indicated MREs (all box plots indicate the minimum, maximum, median and quartiles, single dots represent single cell, colors represent p values, one-way ANOVA with fishers LSD). Source data can be found in Supplemental Table 8 .
    Figure Legend Snippet: Post-transcriptional regulation of individual CAM genes limits ECs spreading, YAP signaling and/or contractility. ( a ) Experimental strategy to mutate individual MREs in CAM genes’ 3’UTRs to block miRNA binding ( Methods and Supplementary Fig. 2b ). ( b ) Representative immunofluorescence images (top, scale bar = 50μm) and Western blot (bottom) of CAM proteins as indicated (CTGF ~37 kDa, STMN1 ~19kDa, VCL ~116kDa, RHOB ~25kDa, Actin ~47kDa). HUVECs were infected with lentivirus carrying Cas9 and gRNA targeting specific CAM MREs and no-target gRNA ( a ) and processed at 7 days post infection. ( b ) Quantification of cell spreading (n=99, 75, 91, 94, 88, 87, 79, 54, 83 from bottom to top, representative data from two independent experiments), YAP nuclear translocation (n=91, 81, 87, 93, 79, 88, 67, 54, 84 cells from bottom to top, representative data from two independent experiments) and total force per cell (n= 38, 33, 37, 36, 34, 34, 34, 30, 36 cells from bottom to top, from two independent experiments) in HUVECs on 3 kPa PDMS gels for 48 h after mutation of the indicated MREs (all box plots indicate the minimum, maximum, median and quartiles, single dots represent single cell, colors represent p values, one-way ANOVA with fishers LSD). Source data can be found in Supplemental Table 8 .

    Techniques Used: Chick Chorioallantoic Membrane Assay, Blocking Assay, Binding Assay, Immunofluorescence, Western Blot, Infection, Translocation Assay, Mutagenesis

    5) Product Images from "microRNA-dependent regulation of biomechanical genes establishes tissue stiffness homeostasis"

    Article Title: microRNA-dependent regulation of biomechanical genes establishes tissue stiffness homeostasis

    Journal: Nature cell biology

    doi: 10.1038/s41556-019-0272-y

    Post-transcriptional regulation of individual CAM genes limits ECs spreading, YAP signaling and/or contractility. ( a ) Experimental strategy to mutate individual MREs in CAM genes’ 3’UTRs to block miRNA binding ( Methods and Supplementary Fig. 2b ). ( b ) Representative immunofluorescence images (top, scale bar = 50μm) and Western blot (bottom) of CAM proteins as indicated (CTGF ~37 kDa, STMN1 ~19kDa, VCL ~116kDa, RHOB ~25kDa, Actin ~47kDa). HUVECs were infected with lentivirus carrying Cas9 and gRNA targeting specific CAM MREs and no-target gRNA ( a ) and processed at 7 days post infection. ( b ) Quantification of cell spreading (n=99, 75, 91, 94, 88, 87, 79, 54, 83 from bottom to top, representative data from two independent experiments), YAP nuclear translocation (n=91, 81, 87, 93, 79, 88, 67, 54, 84 cells from bottom to top, representative data from two independent experiments) and total force per cell (n= 38, 33, 37, 36, 34, 34, 34, 30, 36 cells from bottom to top, from two independent experiments) in HUVECs on 3 kPa PDMS gels for 48 h after mutation of the indicated MREs (all box plots indicate the minimum, maximum, median and quartiles, single dots represent single cell, colors represent p values, one-way ANOVA with fishers LSD). Source data can be found in Supplemental Table 8 .
    Figure Legend Snippet: Post-transcriptional regulation of individual CAM genes limits ECs spreading, YAP signaling and/or contractility. ( a ) Experimental strategy to mutate individual MREs in CAM genes’ 3’UTRs to block miRNA binding ( Methods and Supplementary Fig. 2b ). ( b ) Representative immunofluorescence images (top, scale bar = 50μm) and Western blot (bottom) of CAM proteins as indicated (CTGF ~37 kDa, STMN1 ~19kDa, VCL ~116kDa, RHOB ~25kDa, Actin ~47kDa). HUVECs were infected with lentivirus carrying Cas9 and gRNA targeting specific CAM MREs and no-target gRNA ( a ) and processed at 7 days post infection. ( b ) Quantification of cell spreading (n=99, 75, 91, 94, 88, 87, 79, 54, 83 from bottom to top, representative data from two independent experiments), YAP nuclear translocation (n=91, 81, 87, 93, 79, 88, 67, 54, 84 cells from bottom to top, representative data from two independent experiments) and total force per cell (n= 38, 33, 37, 36, 34, 34, 34, 30, 36 cells from bottom to top, from two independent experiments) in HUVECs on 3 kPa PDMS gels for 48 h after mutation of the indicated MREs (all box plots indicate the minimum, maximum, median and quartiles, single dots represent single cell, colors represent p values, one-way ANOVA with fishers LSD). Source data can be found in Supplemental Table 8 .

    Techniques Used: Chick Chorioallantoic Membrane Assay, Blocking Assay, Binding Assay, Immunofluorescence, Western Blot, Infection, Translocation Assay, Mutagenesis

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