human ddr2 antibody Search Results


anti human ddr2  (R&D Systems)
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Figure 1. The IJM region is necessary for collagen-induced <t>DDR2</t> activation. (a) Overall topology and alignment of the transmembrane (TM) domain and the intracellular juxtamembrane region (IJM) of DDR1a and DDR2. The IJM was divided into three regions: JM1, JM2 and JM3. (b) Schematic diagram of various DDR2 constructs used in our study. (c) HEK293T cells transiently transfected with plasmids encoding the full-length DDR2 and F-DJM1-JM2 mutant were stimulated by Type I collagen for 60 min. Tyrosine phosphorylation of the F-DJM1-JM2 mutant was inhibited compared to that of the full-length DDR2. (d) HEK293T cells were transfected with plasmids encoding full-length DDR2, F- DJM1 and F-DJM2 and were stimulated by collagen. The F-DJM2 mutant showed a significant decrease in tyrosine phosphorylation. **p < 0.01, Student’s t-test.
Anti Human Ddr2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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human ddr2 alexa fluor® 647-conjugated antibody  (Bio-Techne corporation)
90
Bio-Techne corporation human ddr2 alexa fluor® 647-conjugated antibody
Figure 1. The IJM region is necessary for collagen-induced <t>DDR2</t> activation. (a) Overall topology and alignment of the transmembrane (TM) domain and the intracellular juxtamembrane region (IJM) of DDR1a and DDR2. The IJM was divided into three regions: JM1, JM2 and JM3. (b) Schematic diagram of various DDR2 constructs used in our study. (c) HEK293T cells transiently transfected with plasmids encoding the full-length DDR2 and F-DJM1-JM2 mutant were stimulated by Type I collagen for 60 min. Tyrosine phosphorylation of the F-DJM1-JM2 mutant was inhibited compared to that of the full-length DDR2. (d) HEK293T cells were transfected with plasmids encoding full-length DDR2, F- DJM1 and F-DJM2 and were stimulated by collagen. The F-DJM2 mutant showed a significant decrease in tyrosine phosphorylation. **p < 0.01, Student’s t-test.
Human Ddr2 Alexa Fluor® 647 Conjugated Antibody, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/human ddr2 alexa fluor® 647-conjugated antibody/product/Bio-Techne corporation
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phospho ddr2 antibody  (R&D Systems)
99
R&D Systems phospho ddr2 antibody
Figure 1. The IJM region is necessary for collagen-induced <t>DDR2</t> activation. (a) Overall topology and alignment of the transmembrane (TM) domain and the intracellular juxtamembrane region (IJM) of DDR1a and DDR2. The IJM was divided into three regions: JM1, JM2 and JM3. (b) Schematic diagram of various DDR2 constructs used in our study. (c) HEK293T cells transiently transfected with plasmids encoding the full-length DDR2 and F-DJM1-JM2 mutant were stimulated by Type I collagen for 60 min. Tyrosine phosphorylation of the F-DJM1-JM2 mutant was inhibited compared to that of the full-length DDR2. (d) HEK293T cells were transfected with plasmids encoding full-length DDR2, F- DJM1 and F-DJM2 and were stimulated by collagen. The F-DJM2 mutant showed a significant decrease in tyrosine phosphorylation. **p < 0.01, Student’s t-test.
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anti ddr2  (R&D Systems)
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R&D Systems anti ddr2
Figure 1. The IJM region is necessary for collagen-induced <t>DDR2</t> activation. (a) Overall topology and alignment of the transmembrane (TM) domain and the intracellular juxtamembrane region (IJM) of DDR1a and DDR2. The IJM was divided into three regions: JM1, JM2 and JM3. (b) Schematic diagram of various DDR2 constructs used in our study. (c) HEK293T cells transiently transfected with plasmids encoding the full-length DDR2 and F-DJM1-JM2 mutant were stimulated by Type I collagen for 60 min. Tyrosine phosphorylation of the F-DJM1-JM2 mutant was inhibited compared to that of the full-length DDR2. (d) HEK293T cells were transfected with plasmids encoding full-length DDR2, F- DJM1 and F-DJM2 and were stimulated by collagen. The F-DJM2 mutant showed a significant decrease in tyrosine phosphorylation. **p < 0.01, Student’s t-test.
Anti Ddr2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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phosphoddr2 y740  (R&D Systems)
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Figure 1. The IJM region is necessary for collagen-induced <t>DDR2</t> activation. (a) Overall topology and alignment of the transmembrane (TM) domain and the intracellular juxtamembrane region (IJM) of DDR1a and DDR2. The IJM was divided into three regions: JM1, JM2 and JM3. (b) Schematic diagram of various DDR2 constructs used in our study. (c) HEK293T cells transiently transfected with plasmids encoding the full-length DDR2 and F-DJM1-JM2 mutant were stimulated by Type I collagen for 60 min. Tyrosine phosphorylation of the F-DJM1-JM2 mutant was inhibited compared to that of the full-length DDR2. (d) HEK293T cells were transfected with plasmids encoding full-length DDR2, F- DJM1 and F-DJM2 and were stimulated by collagen. The F-DJM2 mutant showed a significant decrease in tyrosine phosphorylation. **p < 0.01, Student’s t-test.
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ddr2  (R&D Systems)
94
R&D Systems ddr2
Fibroblasts Display Activated Phenotype in Allograft Heart. A , t-SNE plot of fibroblast populations of control group ( BALB/c ) and allograft-2 w group. Cd34.high.FB, high expression of FB; ECM.FB, enriched genes and functions related to ECM organization; JF.high.FB, high expression of Jun and Fos ; IFN.FB, high expression of genes related to interferon. B , Pie plot showing the percentage of cell composition in two groups (inside: control; outside: allo-2 w). C , Dot plot shows selected GO terms enriched in fibroblast sub-clusters. D , Violin plot showing the combination expression level (right) of selected activated fibroblast genes (left) in sub-population from two groups. E , Bar plot showing the percentage of activated fibroblasts and other fibroblasts in two datasets. The activated fibroblasts were identified according to combination expression level of genes in Figure d. F , Ridgeline chart showing the expression score of fibrosis-related score in fibroblasts from two groups. G , mRNA quantification of activated fibroblast-associated genes in the hearts from two groups, mRNA expression in the control group as the criterion (1.0). Number of mice in each group: n = 9 (Control), n = 6 (Allo-2 w); unpaired t-test. Postn (Periostin), Col1a1 (Collagen, type I, alpha 1), Col3a1 (Collagen, type III, alpha 1), <t>Ddr2</t> (Discoidin domain-containing receptor 2), Fn1 (Fibronectin), Pdgfra (Platelet-derived growth factor receptorα). H , I , Immunostaining ( H ) and quantification ( I ) of POSTN expression in control group and allograft group, the area of POSTN expression in the control group as the criterion (1.0). The images within the dashed box are displayed in the second row. Number of mice in each group: n = 4 (Control), n = 4 (Allo-1 w), n = 7 (Allo-2 w); one-way ANOVA test. J , Immuno-staining of POSTN and LYVE1, Collagen I and LYVE1, DDR2 and LYVE1 in two groups. The images within the dashed box are displayed in the second row. Scale bars, 100 µm (H,J). Allo: allograft; FB: fibroblast.
Ddr2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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wells  (R&D Systems)
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R&D Systems wells
Fibroblasts Display Activated Phenotype in Allograft Heart. A , t-SNE plot of fibroblast populations of control group ( BALB/c ) and allograft-2 w group. Cd34.high.FB, high expression of FB; ECM.FB, enriched genes and functions related to ECM organization; JF.high.FB, high expression of Jun and Fos ; IFN.FB, high expression of genes related to interferon. B , Pie plot showing the percentage of cell composition in two groups (inside: control; outside: allo-2 w). C , Dot plot shows selected GO terms enriched in fibroblast sub-clusters. D , Violin plot showing the combination expression level (right) of selected activated fibroblast genes (left) in sub-population from two groups. E , Bar plot showing the percentage of activated fibroblasts and other fibroblasts in two datasets. The activated fibroblasts were identified according to combination expression level of genes in Figure d. F , Ridgeline chart showing the expression score of fibrosis-related score in fibroblasts from two groups. G , mRNA quantification of activated fibroblast-associated genes in the hearts from two groups, mRNA expression in the control group as the criterion (1.0). Number of mice in each group: n = 9 (Control), n = 6 (Allo-2 w); unpaired t-test. Postn (Periostin), Col1a1 (Collagen, type I, alpha 1), Col3a1 (Collagen, type III, alpha 1), <t>Ddr2</t> (Discoidin domain-containing receptor 2), Fn1 (Fibronectin), Pdgfra (Platelet-derived growth factor receptorα). H , I , Immunostaining ( H ) and quantification ( I ) of POSTN expression in control group and allograft group, the area of POSTN expression in the control group as the criterion (1.0). The images within the dashed box are displayed in the second row. Number of mice in each group: n = 4 (Control), n = 4 (Allo-1 w), n = 7 (Allo-2 w); one-way ANOVA test. J , Immuno-staining of POSTN and LYVE1, Collagen I and LYVE1, DDR2 and LYVE1 in two groups. The images within the dashed box are displayed in the second row. Scale bars, 100 µm (H,J). Allo: allograft; FB: fibroblast.
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Image Search Results


Figure 1. The IJM region is necessary for collagen-induced DDR2 activation. (a) Overall topology and alignment of the transmembrane (TM) domain and the intracellular juxtamembrane region (IJM) of DDR1a and DDR2. The IJM was divided into three regions: JM1, JM2 and JM3. (b) Schematic diagram of various DDR2 constructs used in our study. (c) HEK293T cells transiently transfected with plasmids encoding the full-length DDR2 and F-DJM1-JM2 mutant were stimulated by Type I collagen for 60 min. Tyrosine phosphorylation of the F-DJM1-JM2 mutant was inhibited compared to that of the full-length DDR2. (d) HEK293T cells were transfected with plasmids encoding full-length DDR2, F- DJM1 and F-DJM2 and were stimulated by collagen. The F-DJM2 mutant showed a significant decrease in tyrosine phosphorylation. **p < 0.01, Student’s t-test.

Journal: International journal of cancer

Article Title: The intracellular juxtamembrane domain of discoidin domain receptor 2 (DDR2) is essential for receptor activation and DDR2-mediated cancer progression.

doi: 10.1002/ijc.28901

Figure Lengend Snippet: Figure 1. The IJM region is necessary for collagen-induced DDR2 activation. (a) Overall topology and alignment of the transmembrane (TM) domain and the intracellular juxtamembrane region (IJM) of DDR1a and DDR2. The IJM was divided into three regions: JM1, JM2 and JM3. (b) Schematic diagram of various DDR2 constructs used in our study. (c) HEK293T cells transiently transfected with plasmids encoding the full-length DDR2 and F-DJM1-JM2 mutant were stimulated by Type I collagen for 60 min. Tyrosine phosphorylation of the F-DJM1-JM2 mutant was inhibited compared to that of the full-length DDR2. (d) HEK293T cells were transfected with plasmids encoding full-length DDR2, F- DJM1 and F-DJM2 and were stimulated by collagen. The F-DJM2 mutant showed a significant decrease in tyrosine phosphorylation. **p < 0.01, Student’s t-test.

Article Snippet: The antibodies used in our study were as follows: mouse anti-myc (sc-40; Santa Cruz Biotechnology, Santa Cruz, CA), rabbit anti-HA (sc-805; Santa Cruz Biotechnology), rabbit anti-DDR1 (sc-532; Santa Cruz Biotechnol- ogy), goat anti-DDR2 (sc-7555; Santa Cruz Biotechnology), anti-human DDR2 (AF2538; R&D Systems, Minneapolis, MN), anti-phosphotyrosine (clone 4G10; Upstate Biotechnology, Lake Placid, NY) and peroxidase- and fluoresceinconjugated goat anti-mouse IgG (Jackson ImmunoResearch Laboratories, West Grove, PA).

Techniques: Activation Assay, Construct, Transfection, Mutagenesis, Phospho-proteomics

Figure 2. DDR2 dimerizes via the JM2 of the IJM region. (a and b) HEK293T cells were transiently cotransfected with plasmids encoding TM- JM1-JM2-myc and TM-JM1-JM2-HA. Immunoprecipitation and Western blot analysis showed that the cytoplasmic domains of DDR2 bind to each other via the intact TM-JM1-JM2 domain and form homodimers. Asterisks indicate the expected size of TM-JM1-JM2. (c) HEK293T cells were transfected with plasmids encoding F-DJM1 and F-DJM2 mutants. A crosslinking assay showed that dimers of F-DJM1 were not changed compared to full-length DDR2, whereas dimers were significantly decreased for F-DJM2.

Journal: International journal of cancer

Article Title: The intracellular juxtamembrane domain of discoidin domain receptor 2 (DDR2) is essential for receptor activation and DDR2-mediated cancer progression.

doi: 10.1002/ijc.28901

Figure Lengend Snippet: Figure 2. DDR2 dimerizes via the JM2 of the IJM region. (a and b) HEK293T cells were transiently cotransfected with plasmids encoding TM- JM1-JM2-myc and TM-JM1-JM2-HA. Immunoprecipitation and Western blot analysis showed that the cytoplasmic domains of DDR2 bind to each other via the intact TM-JM1-JM2 domain and form homodimers. Asterisks indicate the expected size of TM-JM1-JM2. (c) HEK293T cells were transfected with plasmids encoding F-DJM1 and F-DJM2 mutants. A crosslinking assay showed that dimers of F-DJM1 were not changed compared to full-length DDR2, whereas dimers were significantly decreased for F-DJM2.

Article Snippet: The antibodies used in our study were as follows: mouse anti-myc (sc-40; Santa Cruz Biotechnology, Santa Cruz, CA), rabbit anti-HA (sc-805; Santa Cruz Biotechnology), rabbit anti-DDR1 (sc-532; Santa Cruz Biotechnol- ogy), goat anti-DDR2 (sc-7555; Santa Cruz Biotechnology), anti-human DDR2 (AF2538; R&D Systems, Minneapolis, MN), anti-phosphotyrosine (clone 4G10; Upstate Biotechnology, Lake Placid, NY) and peroxidase- and fluoresceinconjugated goat anti-mouse IgG (Jackson ImmunoResearch Laboratories, West Grove, PA).

Techniques: Immunoprecipitation, Western Blot, Transfection

Figure 3. JM2 has a dominant-negative effect on DDR2 activation. (a and b) HEK293T cells were cotransfected with plasmids encoding full- length DDR2-myc and TM-JM1-JM2-HA. Immunoprecipitation and Western blotting showed that the full-length DDR2 and TM-JM1-JM2 bind to each other to form heterodimers. The immunoprecipitates obtained with anti-IgG antibodies were used as a negative control. (c) H1299 cells transfected with plasmids encoding full-length DDR2 and TM-JM1-JM2 and HeLa cells were lysed, and the whole cell lysates (W) were separated into the plasma membrane (P) and cytosol (C) fractions. EGFR and a-tubulin were used as positive controls for the plasma mem- brane and cytosol fractions, respectively. Endogenous full-length DDR2 (HeLa cells), forced-expressed full-length DDR2 and TM-JM1-JM2 pro- teins were appropriately localized in the plasma membrane. (d) HEK293T cells were transfected with plasmids encoding a C-terminally myc- tagged full-length DDR2 and TM-JM1-JM2. Only under the permeabilized condition, full-length DDR2-myc and TM-JM1-JM2-myc were visual- ized, indicating that the C-termini of these proteins were located in the cytosol and not extracellular space. Full-length DDR2 was used as a positive control. Bar, 50 mm. (e) HEK293T cells were cotransfected with plasmids encoding full-length DDR2 (500 ng) and an increasing amount of TM-JM1-JM2 (100, 300 and 500 ng) as indicated and then stimulated with collagen. Tyrosine phosphorylation gradually decreased with an increasing amount of TM-JM1-JM2. (f) HeLa cells were transiently transfected with a plasmid encoding TM-JM1-JM2 and were then stimulated. Tyrosine phosphorylation was significantly decreased in endogenous DDR2. **p < 0.01, Student’s t-test. [Color figure can be viewed in the online issue, which is available at wileyonlinelibrary.com.]

Journal: International journal of cancer

Article Title: The intracellular juxtamembrane domain of discoidin domain receptor 2 (DDR2) is essential for receptor activation and DDR2-mediated cancer progression.

doi: 10.1002/ijc.28901

Figure Lengend Snippet: Figure 3. JM2 has a dominant-negative effect on DDR2 activation. (a and b) HEK293T cells were cotransfected with plasmids encoding full- length DDR2-myc and TM-JM1-JM2-HA. Immunoprecipitation and Western blotting showed that the full-length DDR2 and TM-JM1-JM2 bind to each other to form heterodimers. The immunoprecipitates obtained with anti-IgG antibodies were used as a negative control. (c) H1299 cells transfected with plasmids encoding full-length DDR2 and TM-JM1-JM2 and HeLa cells were lysed, and the whole cell lysates (W) were separated into the plasma membrane (P) and cytosol (C) fractions. EGFR and a-tubulin were used as positive controls for the plasma mem- brane and cytosol fractions, respectively. Endogenous full-length DDR2 (HeLa cells), forced-expressed full-length DDR2 and TM-JM1-JM2 pro- teins were appropriately localized in the plasma membrane. (d) HEK293T cells were transfected with plasmids encoding a C-terminally myc- tagged full-length DDR2 and TM-JM1-JM2. Only under the permeabilized condition, full-length DDR2-myc and TM-JM1-JM2-myc were visual- ized, indicating that the C-termini of these proteins were located in the cytosol and not extracellular space. Full-length DDR2 was used as a positive control. Bar, 50 mm. (e) HEK293T cells were cotransfected with plasmids encoding full-length DDR2 (500 ng) and an increasing amount of TM-JM1-JM2 (100, 300 and 500 ng) as indicated and then stimulated with collagen. Tyrosine phosphorylation gradually decreased with an increasing amount of TM-JM1-JM2. (f) HeLa cells were transiently transfected with a plasmid encoding TM-JM1-JM2 and were then stimulated. Tyrosine phosphorylation was significantly decreased in endogenous DDR2. **p < 0.01, Student’s t-test. [Color figure can be viewed in the online issue, which is available at wileyonlinelibrary.com.]

Article Snippet: The antibodies used in our study were as follows: mouse anti-myc (sc-40; Santa Cruz Biotechnology, Santa Cruz, CA), rabbit anti-HA (sc-805; Santa Cruz Biotechnology), rabbit anti-DDR1 (sc-532; Santa Cruz Biotechnol- ogy), goat anti-DDR2 (sc-7555; Santa Cruz Biotechnology), anti-human DDR2 (AF2538; R&D Systems, Minneapolis, MN), anti-phosphotyrosine (clone 4G10; Upstate Biotechnology, Lake Placid, NY) and peroxidase- and fluoresceinconjugated goat anti-mouse IgG (Jackson ImmunoResearch Laboratories, West Grove, PA).

Techniques: Dominant Negative Mutation, Activation Assay, Immunoprecipitation, Western Blot, Negative Control, Transfection, Clinical Proteomics, Membrane, Positive Control, Phospho-proteomics, Plasmid Preparation

Figure 4. JM2 regulates the collagen-binding affinity of DDR2. (a and b) HEK293T cells transiently transfected with various DDR2 constructs were harvested, and protein expression was verified by Western blot- ting (a). Collagen-binding affinities were reduced in F-DJM2, F-DJM1- JM2 and extra mutants but not the F-DJM1 mutant in a dose- dependent manner (b). Nontransfected (NC) and TM-JM1-JM2 samples were used as negative controls. **p< 0.01, Student’s t-test.

Journal: International journal of cancer

Article Title: The intracellular juxtamembrane domain of discoidin domain receptor 2 (DDR2) is essential for receptor activation and DDR2-mediated cancer progression.

doi: 10.1002/ijc.28901

Figure Lengend Snippet: Figure 4. JM2 regulates the collagen-binding affinity of DDR2. (a and b) HEK293T cells transiently transfected with various DDR2 constructs were harvested, and protein expression was verified by Western blot- ting (a). Collagen-binding affinities were reduced in F-DJM2, F-DJM1- JM2 and extra mutants but not the F-DJM1 mutant in a dose- dependent manner (b). Nontransfected (NC) and TM-JM1-JM2 samples were used as negative controls. **p< 0.01, Student’s t-test.

Article Snippet: The antibodies used in our study were as follows: mouse anti-myc (sc-40; Santa Cruz Biotechnology, Santa Cruz, CA), rabbit anti-HA (sc-805; Santa Cruz Biotechnology), rabbit anti-DDR1 (sc-532; Santa Cruz Biotechnol- ogy), goat anti-DDR2 (sc-7555; Santa Cruz Biotechnology), anti-human DDR2 (AF2538; R&D Systems, Minneapolis, MN), anti-phosphotyrosine (clone 4G10; Upstate Biotechnology, Lake Placid, NY) and peroxidase- and fluoresceinconjugated goat anti-mouse IgG (Jackson ImmunoResearch Laboratories, West Grove, PA).

Techniques: Binding Assay, Transfection, Construct, Expressing, Western Blot, Mutagenesis

Figure 5. Colony formation and proliferation of tumor cells are suppressed by overexpression of JM2. (a and b) Formalin-fixed tissue micro- array slides were used in immunohistochemistry experiments. DDR2 was overexpressed in bladder, testis, lung, kidney, prostate and stom- ach cancers. Bar, 50 mm. (c) Stable TM-JM1-JM2–expressing H1299 cells were stimulated by collagen and then harvested. Immunoprecipitation and Western blot analysis showed that tyrosine phosphorylation of DDR2 was decreased by TM-JM1-JM2 overexpres- sion (labeled JM1/2), but phosphorylation of DDR1 was unaffected. (d) A colony-forming assay of H1299 cells showed that the number and projected area of colonies were decreased by TM-JM1-JM2 overexpression. Bar, 100 mm. (e) Proliferation of H1299 cells was assessed by cell counting (left) and an MTT assay (right). Cell proliferation was inhibited by TM-JM1-JM2 overexpression. **p < 0.01, Student’s t-test; control, nontransfected cells; Mock, empty vector stably transfected cells; JM1/2, TM-JM1-JM2 stably transfected cells. [Color figure can be viewed in the online issue, which is available at wileyonlinelibrary.com.]

Journal: International journal of cancer

Article Title: The intracellular juxtamembrane domain of discoidin domain receptor 2 (DDR2) is essential for receptor activation and DDR2-mediated cancer progression.

doi: 10.1002/ijc.28901

Figure Lengend Snippet: Figure 5. Colony formation and proliferation of tumor cells are suppressed by overexpression of JM2. (a and b) Formalin-fixed tissue micro- array slides were used in immunohistochemistry experiments. DDR2 was overexpressed in bladder, testis, lung, kidney, prostate and stom- ach cancers. Bar, 50 mm. (c) Stable TM-JM1-JM2–expressing H1299 cells were stimulated by collagen and then harvested. Immunoprecipitation and Western blot analysis showed that tyrosine phosphorylation of DDR2 was decreased by TM-JM1-JM2 overexpres- sion (labeled JM1/2), but phosphorylation of DDR1 was unaffected. (d) A colony-forming assay of H1299 cells showed that the number and projected area of colonies were decreased by TM-JM1-JM2 overexpression. Bar, 100 mm. (e) Proliferation of H1299 cells was assessed by cell counting (left) and an MTT assay (right). Cell proliferation was inhibited by TM-JM1-JM2 overexpression. **p < 0.01, Student’s t-test; control, nontransfected cells; Mock, empty vector stably transfected cells; JM1/2, TM-JM1-JM2 stably transfected cells. [Color figure can be viewed in the online issue, which is available at wileyonlinelibrary.com.]

Article Snippet: The antibodies used in our study were as follows: mouse anti-myc (sc-40; Santa Cruz Biotechnology, Santa Cruz, CA), rabbit anti-HA (sc-805; Santa Cruz Biotechnology), rabbit anti-DDR1 (sc-532; Santa Cruz Biotechnol- ogy), goat anti-DDR2 (sc-7555; Santa Cruz Biotechnology), anti-human DDR2 (AF2538; R&D Systems, Minneapolis, MN), anti-phosphotyrosine (clone 4G10; Upstate Biotechnology, Lake Placid, NY) and peroxidase- and fluoresceinconjugated goat anti-mouse IgG (Jackson ImmunoResearch Laboratories, West Grove, PA).

Techniques: Over Expression, Microarray, Immunohistochemistry, Expressing, Immunoprecipitation, Western Blot, Phospho-proteomics, Labeling, Cell Counting, MTT Assay, Control, Plasmid Preparation, Stable Transfection, Transfection

Fibroblasts Display Activated Phenotype in Allograft Heart. A , t-SNE plot of fibroblast populations of control group ( BALB/c ) and allograft-2 w group. Cd34.high.FB, high expression of FB; ECM.FB, enriched genes and functions related to ECM organization; JF.high.FB, high expression of Jun and Fos ; IFN.FB, high expression of genes related to interferon. B , Pie plot showing the percentage of cell composition in two groups (inside: control; outside: allo-2 w). C , Dot plot shows selected GO terms enriched in fibroblast sub-clusters. D , Violin plot showing the combination expression level (right) of selected activated fibroblast genes (left) in sub-population from two groups. E , Bar plot showing the percentage of activated fibroblasts and other fibroblasts in two datasets. The activated fibroblasts were identified according to combination expression level of genes in Figure d. F , Ridgeline chart showing the expression score of fibrosis-related score in fibroblasts from two groups. G , mRNA quantification of activated fibroblast-associated genes in the hearts from two groups, mRNA expression in the control group as the criterion (1.0). Number of mice in each group: n = 9 (Control), n = 6 (Allo-2 w); unpaired t-test. Postn (Periostin), Col1a1 (Collagen, type I, alpha 1), Col3a1 (Collagen, type III, alpha 1), Ddr2 (Discoidin domain-containing receptor 2), Fn1 (Fibronectin), Pdgfra (Platelet-derived growth factor receptorα). H , I , Immunostaining ( H ) and quantification ( I ) of POSTN expression in control group and allograft group, the area of POSTN expression in the control group as the criterion (1.0). The images within the dashed box are displayed in the second row. Number of mice in each group: n = 4 (Control), n = 4 (Allo-1 w), n = 7 (Allo-2 w); one-way ANOVA test. J , Immuno-staining of POSTN and LYVE1, Collagen I and LYVE1, DDR2 and LYVE1 in two groups. The images within the dashed box are displayed in the second row. Scale bars, 100 µm (H,J). Allo: allograft; FB: fibroblast.

Journal: Theranostics

Article Title: Fibroblasts facilitate lymphatic vessel formation in transplanted heart

doi: 10.7150/thno.92103

Figure Lengend Snippet: Fibroblasts Display Activated Phenotype in Allograft Heart. A , t-SNE plot of fibroblast populations of control group ( BALB/c ) and allograft-2 w group. Cd34.high.FB, high expression of FB; ECM.FB, enriched genes and functions related to ECM organization; JF.high.FB, high expression of Jun and Fos ; IFN.FB, high expression of genes related to interferon. B , Pie plot showing the percentage of cell composition in two groups (inside: control; outside: allo-2 w). C , Dot plot shows selected GO terms enriched in fibroblast sub-clusters. D , Violin plot showing the combination expression level (right) of selected activated fibroblast genes (left) in sub-population from two groups. E , Bar plot showing the percentage of activated fibroblasts and other fibroblasts in two datasets. The activated fibroblasts were identified according to combination expression level of genes in Figure d. F , Ridgeline chart showing the expression score of fibrosis-related score in fibroblasts from two groups. G , mRNA quantification of activated fibroblast-associated genes in the hearts from two groups, mRNA expression in the control group as the criterion (1.0). Number of mice in each group: n = 9 (Control), n = 6 (Allo-2 w); unpaired t-test. Postn (Periostin), Col1a1 (Collagen, type I, alpha 1), Col3a1 (Collagen, type III, alpha 1), Ddr2 (Discoidin domain-containing receptor 2), Fn1 (Fibronectin), Pdgfra (Platelet-derived growth factor receptorα). H , I , Immunostaining ( H ) and quantification ( I ) of POSTN expression in control group and allograft group, the area of POSTN expression in the control group as the criterion (1.0). The images within the dashed box are displayed in the second row. Number of mice in each group: n = 4 (Control), n = 4 (Allo-1 w), n = 7 (Allo-2 w); one-way ANOVA test. J , Immuno-staining of POSTN and LYVE1, Collagen I and LYVE1, DDR2 and LYVE1 in two groups. The images within the dashed box are displayed in the second row. Scale bars, 100 µm (H,J). Allo: allograft; FB: fibroblast.

Article Snippet: Primary antibodies were applied in this study as listed: LYVE1 (abcam, ab14917, 1:300), VEGFR3 (R&D Systems, AF349, 1:50), tdTomato (Rockland, 600-401-379, 1:500), Periostin (R&D system, AF2955, 1:50), Collagen Type I (Proteintech, 67288-1-Ig, 1:100 ), DDR2 (discoidin domain receptor 2, R&D Systems, MAB25381, 1:100), PDGFRα (R&D Systems, AF1062, 1:50), PCNA (Abclonal, A0264, 1:500), KI67 (abcam, ab16667, 1:500), VEGFD (Proteintech, 26915-1-AP, 1:50), Midkine (Proteintech, 11009-1-AP, 1:50), SEMA3C (R&D Systems,MAB1728, 1:50), PTN (abcam, ab79411, 1:50), NRP2 (Neuropilin-2, CST, D39A5, 1:50), NCL (nucleolin, Santa cruz, sc-8031, 1:50), Vimentin (abcam, ab8978, 1:100), Fibronectin (abcam, ab2413, 1:50), CD31 (R&D, AF3628, 1:50), CD31 (abcam, ab28364, 1:50), SMA-FITC (Sigma, F3777, 1:300), p-AKT(Santa cruz, sc-514032, 1:50), p-ERK (Santa cruz, sc-7383, 1:50), CD45 (R&D Systems, AF114, 1:50), TNF-α(Proteintech, 60291-1-Ig, 1:50), IL1β (Abclonal, a19635, 1:50), IL6 (Proteintech, 66146-1-Ig, 1:50).

Techniques: Control, Expressing, Derivative Assay, Immunostaining