anti human ddr2 (R&D Systems)

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R&D Systems anti human 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 Human Ddr2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tissue+microarray+based+immunohistochemistry+analysis/Human+DDR2+Antibody/pm24740739-36-37-40
Average 94 stars, based on 26 article reviews

anti human ddr2 - by Bioz Stars, 2026-10

94/100 stars

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1) Product Images from "The intracellular juxtamembrane domain of discoidin domain receptor 2 (DDR2) is essential for receptor activation and DDR2-mediated cancer progression."

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

Journal: International journal of cancer

doi: 10.1002/ijc.28901

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.

Figure Legend 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.

Techniques Used: 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.

Figure Legend 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.

Techniques Used: Immunoprecipitation, Western Blot, Transfection

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

Techniques Used: 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.

Figure Legend 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.

Techniques Used: 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.]

Figure Legend 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.]

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

Sequencing:

Article Title: Clustering, Spatial Distribution, and Phosphorylation of Discoidin Domain Receptors 1 and 2 in Response to Soluble Collagen I.
Article Snippet: Pepsin-digested bovine-dermal collagen (PureCol) and acid-extracted rat-tail collagen I were purchased from Advanced BioMatrix San Diego, CA, and Sigma Chemicals, St. Louis, MO, respectively. .. Mouse monoclonal (MAB25381) and goat polyclonal (AF2538) anti-DDR2 antibodies (raised against a peptide sequence in the DDR2 ECD) and rabbit monoclonal against phospho-DDR2 (DDR2-Y740, catalog no. MAB25382) were obtained from R&D Systems, Minneapolis, MN. .. Rabbit monoclonal antibodies recognizing phosphorylated DDR1b and DDR1c (DDR1b/c-Y513, catalog no. 14531), monoclonal antibody recognizing total DDR1 (D1G6, catalog no. 5583), polyclonal antibody recognizing phosphoDDR1 (DDR1-Y792, catalog no.11994), polyclonal antibody recognizing total DDR2 (catalog no.12133) andDyLightTM 554 Phalloidin (catalog no. 13054) were all purchased from Cell Signaling Technology, Danvers, MA.

Article Title: Clustering, Spatial Distribution and Phosphorylation of Discoidin Domain Receptors 1 and 2 in Response to Soluble Collagen Type I
Article Snippet: Collagen and Antibodies Pepsin-digested bovine-dermal collagen (PureCol) and acid-extracted rat-tail collagen I were purchased from Advanced BioMatrix San Diego, CA and Sigma Chemicals, St. Louis, MO, respectively. .. Mouse monoclonal (MAB25381) and goat polyclonal (AF2538) anti-DDR2 antibodies (raised against a peptide sequence in the DDR2 ECD) and rabbit monoclonal against phospho-DDR2 (DDR2-Y740, catalog # MAB25382) were obtained from R&D Systems, Minneapolis, MN. .. Rabbit monoclonal antibodies recognizing phosphorylated DDR1b and DDR1c (DDR1b/c-Y513), monoclonal antibody that recognize total DDR1 (D1G6), polyclonal antibody that recognize phospho-DDR1 (DDR1-Y792, catalog #11994), polyclonal antibody that recognize total DDR2 (catalog #12133) and DyLightTM 554 Phalloidin (catalog # 13054) were purchased from Cell Signaling Technology, Danvers, MA.

Membrane:

Article Title: The expression of two collagen receptor subfamilies, integrins and discoidin domains during osteogenic and chondrogenic differentiation of human mesenehymal stem cells
Article Snippet: BACKGROUND: Collagen receptors are characterized by binding to and being activated by collagens.. We know little about the molecular mechanism by which the integrins and discoidin domains (DDRs) recognize collagen.. OBJECTIVE: The aim of this study was to investigate the expression of two main collagen receptor subfamilies, integrins and DDRs, during osteogenic and chondrogenic differentiation of human mesenehymal stem cells (hMSCs).

Staining:

other:

Article Title: Vimentin tunes cell migration on collagen by controlling β1 integrin activation and clustering.
Article Snippet: Goat anti-DDR2 antibody (AF2538) was from R&D Systems (Minneapolis, MN).

Enzyme-linked Immunosorbent Assay:

Article Title: Periostin interaction with discoidin domain receptor-1 (DDR1) promotes cartilage degeneration
Article Snippet: .. All media and FBS were purchased from Thermo Fisher Scientific (Waltham, MA); proMMP-13 enzyme-linked immunosorbent assay (ELISA) kits from R&D systems (Minneapolis, MN); Phosphatase Inhibitor Cocktail [#5870; Cell signaling, Danvers, MA, USA] and protease inhibitor cocktail (#539131, Calbiochem, San Diego, CA, USA); The Wnt signaling inhibitor CCT031374 hydrobromide (cat. no. 4675/10, R&D Systems, Minneapolis, MN), antibodies to β-Catenin (D10A8; XP® Rabbit mAb #8480), α-Tubulin (11H10; Rabbit mAb#2125), Akt (#9272); Phospho-Akt (Ser473) (193H12; Rabbit mAb #4058), Phospho-DDR1 (Tyr792; #11994) and total DDR1 (D1G6; XP® Rabbit mAb #5583) from Cell Signaling Technology (Danvers, MA 01923); the antibodies to human Phospho-DDR2 (Y740; #1119D) and human DDR1 (AF2538) from R&D system (Minneapolis, MN); HRP-conjugated rabbit anti-goat (#305-036-047), HRP-conjugated goat anti-rabbit (#111-035-144), AffiniPure goat anti-human lgG, F(ab’)2 fragment specific (#109-005-097) and peroxidase affinipure goat anti-human lgG(H+L; #109-035-088) from Jackson ImmunoResearch (West Grove, PA, USA). ..

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anti human ddr2 (R&D Systems)

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1) Product Images from "The intracellular juxtamembrane domain of discoidin domain receptor 2 (DDR2) is essential for receptor activation and DDR2-mediated cancer progression."

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