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mouse monoclonal anti human timp 3 antibody  (R&D Systems)


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    R&D Systems mouse monoclonal anti human timp 3 antibody
    Mouse Monoclonal Anti Human Timp 3 Antibody, supplied by R&D Systems, 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/product/mouse+monoclonal+anti+human+timp+3+antibody/Human+TIMP-3+Antibody/pmc03759388-97-10-15
    Average 90 stars, based on 1 article reviews
    mouse monoclonal anti human timp 3 antibody - by Bioz Stars, 2026-10
    90/100 stars

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    Article Title: IKKα/CHUK Regulates Extracellular Matrix Remodeling Independent of Its Kinase Activity to Facilitate Articular Chondrocyte Differentiation
    Article Snippet: TIMP-3 protein in 1-week pellet cultures was detected using a mouse monoclonal anti-human TIMP-3 antibody (R&D Systems).



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    The immunohistochemical stains for matrix metalloproteinase (MMP)-3, -7, and -9 and tissue inhibitor of matrix metalloproteinase (TIMP)-1 in the Helicobacter pylori- ( H. pylori- ) infected group, in the nonsteroidal anti-inflammatory drug- (NSAID-) related group, and in the combined H. pylori -infection and NSAID-use group, in superficial epithelial cells and inflammatory cells of the lamina propria of gastric tissues (600x). H. pylori- infected gastric ulcers express higher MMP-7, MMP-9, and TIMP-1 than NSAID-related ulcers. Arrows indicate positive staining.

    Journal: The Scientific World Journal

    Article Title: Expressions of MMPs and TIMP-1 in Gastric Ulcers May Differentiate H. pylori -Infected from NSAID-Related Ulcers

    doi: 10.1100/2012/539316

    Figure Lengend Snippet: The immunohistochemical stains for matrix metalloproteinase (MMP)-3, -7, and -9 and tissue inhibitor of matrix metalloproteinase (TIMP)-1 in the Helicobacter pylori- ( H. pylori- ) infected group, in the nonsteroidal anti-inflammatory drug- (NSAID-) related group, and in the combined H. pylori -infection and NSAID-use group, in superficial epithelial cells and inflammatory cells of the lamina propria of gastric tissues (600x). H. pylori- infected gastric ulcers express higher MMP-7, MMP-9, and TIMP-1 than NSAID-related ulcers. Arrows indicate positive staining.

    Article Snippet: Tissue immunohistochemical staining was performed using mouse monoclonal antibodies of anti-human-MMP-3, -7, -9, or TIMP-1 (Chemicon International, Inc., Temecula, CA, USA).

    Techniques: Immunohistochemical staining, Infection, Staining

    Box plots of the distributions and median scores of MMP-7, and -9 and TIMP-1 in the superficial epithelium of gastric ulcer tissues and nonulcer tissues in different groups, respectively. The P values compared scores according to patients in the H. pylori -infected, NSAID-related, and combined H. pylori -infection and NSAID-use groups by Mann-Whitney U test, and also compared scores according to ulcer tissues and nonulcer tissues by Wilcoxon signed-rank test. In the box plots, the 75th and 25th percentiles are represented by the top and bottom of the box, respectively. The horizontal lines refer to the medians. Abbreviations are as in .

    Journal: The Scientific World Journal

    Article Title: Expressions of MMPs and TIMP-1 in Gastric Ulcers May Differentiate H. pylori -Infected from NSAID-Related Ulcers

    doi: 10.1100/2012/539316

    Figure Lengend Snippet: Box plots of the distributions and median scores of MMP-7, and -9 and TIMP-1 in the superficial epithelium of gastric ulcer tissues and nonulcer tissues in different groups, respectively. The P values compared scores according to patients in the H. pylori -infected, NSAID-related, and combined H. pylori -infection and NSAID-use groups by Mann-Whitney U test, and also compared scores according to ulcer tissues and nonulcer tissues by Wilcoxon signed-rank test. In the box plots, the 75th and 25th percentiles are represented by the top and bottom of the box, respectively. The horizontal lines refer to the medians. Abbreviations are as in .

    Article Snippet: Tissue immunohistochemical staining was performed using mouse monoclonal antibodies of anti-human-MMP-3, -7, -9, or TIMP-1 (Chemicon International, Inc., Temecula, CA, USA).

    Techniques: Infection, MANN-WHITNEY

    Box plots of the distributions and median scores of MMP-3, MMP-9, and TIMP-1 in inflammatory cells of the lamina propria of gastric ulcer tissues and nonulcer tissues in different groups, respectively. The P values compared scores according to patients in the H. pylori -infected, NSAID-related, and combined H. pylori -infection and NSAID-use groups by Mann-Whitney U test and also compared scores according to ulcer tissues and nonulcer tissues by Wilcoxon signed-rank test. In the box plots, the 75th and 25th percentiles are represented by the top and bottom of the box, respectively. The horizontal lines refer to the medians. Abbreviations are as in .

    Journal: The Scientific World Journal

    Article Title: Expressions of MMPs and TIMP-1 in Gastric Ulcers May Differentiate H. pylori -Infected from NSAID-Related Ulcers

    doi: 10.1100/2012/539316

    Figure Lengend Snippet: Box plots of the distributions and median scores of MMP-3, MMP-9, and TIMP-1 in inflammatory cells of the lamina propria of gastric ulcer tissues and nonulcer tissues in different groups, respectively. The P values compared scores according to patients in the H. pylori -infected, NSAID-related, and combined H. pylori -infection and NSAID-use groups by Mann-Whitney U test and also compared scores according to ulcer tissues and nonulcer tissues by Wilcoxon signed-rank test. In the box plots, the 75th and 25th percentiles are represented by the top and bottom of the box, respectively. The horizontal lines refer to the medians. Abbreviations are as in .

    Article Snippet: Tissue immunohistochemical staining was performed using mouse monoclonal antibodies of anti-human-MMP-3, -7, -9, or TIMP-1 (Chemicon International, Inc., Temecula, CA, USA).

    Techniques: Infection, MANN-WHITNEY

    TIMP-1 is a substrate of caspase-12. A, typical Western blot against TIMP-1 following incubation of 5 ng of caspase-12 with 3 ng of TIMP-1 for various time periods. B, MMP-3 enzyme activity of 5 ng of cMMP-3 measured in the presence of 3 ng of TIMP-1 with or without prior overnight exposure to 5 ng of caspase-12. **, p < 0.01; ***, p < 0.001 versus cMMP-3; +++, p < 0.001 versus cMMP3 plus TIMP-1 (2).

    Journal: The Journal of Biological Chemistry

    Article Title: Matrix Metalloproteinase-3 Is Increased and Participates in Neuronal Apoptotic Signaling Downstream of Caspase-12 during Endoplasmic Reticulum Stress *

    doi: 10.1074/jbc.M109.093799

    Figure Lengend Snippet: TIMP-1 is a substrate of caspase-12. A, typical Western blot against TIMP-1 following incubation of 5 ng of caspase-12 with 3 ng of TIMP-1 for various time periods. B, MMP-3 enzyme activity of 5 ng of cMMP-3 measured in the presence of 3 ng of TIMP-1 with or without prior overnight exposure to 5 ng of caspase-12. **, p < 0.01; ***, p < 0.001 versus cMMP-3; +++, p < 0.001 versus cMMP3 plus TIMP-1 (2).

    Article Snippet: Primary antibodies used were goat polyclonal anti-mouse MMP-3 antibody (R&D Systems Inc., Minneapolis, MN), goat polyclonal anti-human MMP-3 antibody (BioVision), goat polyclonal anti-mouse TIMP-1 antibody (R&D Systems Inc.), mouse monoclonal anti-human TIMP-1 antibody (Calbiochem), rabbit polyclonal anti-mouse caspase-12 antibody (Cell Signaling Technology Inc., Beverly, MA), and rabbit anti-mouse cleaved caspase-3 (Asp-175) antibody (Cell Signaling Technology Inc.).

    Techniques: Western Blot, Incubation, Activity Assay

    Caspase-12 can degrade TIMP-1 that is bound to MMP-3. A, typical Western blot against MMP-3 on lysate of CATH.a cells that has been exposed to caspase-12 and immunoprecipitated with TIMP-1 antibody. The intensity of the MMP-3 band was determined by densitometry and expressed as -fold induction relative to the untreated control. ***, p < 0.001 versus control. B, MMP-3 enzyme activity of cMMP-3·TIMP-1 complex with or without exposure to caspase-12; **, p < 0.01 versus cMMP-3 plus TIMP-1 (1).

    Journal: The Journal of Biological Chemistry

    Article Title: Matrix Metalloproteinase-3 Is Increased and Participates in Neuronal Apoptotic Signaling Downstream of Caspase-12 during Endoplasmic Reticulum Stress *

    doi: 10.1074/jbc.M109.093799

    Figure Lengend Snippet: Caspase-12 can degrade TIMP-1 that is bound to MMP-3. A, typical Western blot against MMP-3 on lysate of CATH.a cells that has been exposed to caspase-12 and immunoprecipitated with TIMP-1 antibody. The intensity of the MMP-3 band was determined by densitometry and expressed as -fold induction relative to the untreated control. ***, p < 0.001 versus control. B, MMP-3 enzyme activity of cMMP-3·TIMP-1 complex with or without exposure to caspase-12; **, p < 0.01 versus cMMP-3 plus TIMP-1 (1).

    Article Snippet: Primary antibodies used were goat polyclonal anti-mouse MMP-3 antibody (R&D Systems Inc., Minneapolis, MN), goat polyclonal anti-human MMP-3 antibody (BioVision), goat polyclonal anti-mouse TIMP-1 antibody (R&D Systems Inc.), mouse monoclonal anti-human TIMP-1 antibody (Calbiochem), rabbit polyclonal anti-mouse caspase-12 antibody (Cell Signaling Technology Inc., Beverly, MA), and rabbit anti-mouse cleaved caspase-3 (Asp-175) antibody (Cell Signaling Technology Inc.).

    Techniques: Western Blot, Immunoprecipitation, Activity Assay

    Cellular TIMP-1 is protective and decreases in response to ER stress. A, typical Western blot of TIMP-1 on lysate of CATH.a cells that has been exposed to 1 μm BFA for various time periods. B, typical Western blot against TIMP-1 on lysates of CATH.a cells transfected with caspase-12 siRNA (#1 or #2) or negative siRNA control (N) and subsequently treated with BFA. C, TIMP-1 Western blot on lysate of CATH.a cells that was pretreated with 1 μm Z-ATAD-FMK for 1 h followed by 1 μm BFA for 24 h. D and E, CATH.a cells transfected with TIMP-1 cDNA were exposed to BFA, extent of cell death was monitored by TUNEL staining, and TUNEL-positive cells were counted and expressed as the percentage of total cells (D), and MMP-3 enzyme activity was measured (E). *, p < 0.05; **, p < 0.01 versus respective untreated control; +, p < 0.05; ++, p < 0.01 versus mock transfected BFA-treated.

    Journal: The Journal of Biological Chemistry

    Article Title: Matrix Metalloproteinase-3 Is Increased and Participates in Neuronal Apoptotic Signaling Downstream of Caspase-12 during Endoplasmic Reticulum Stress *

    doi: 10.1074/jbc.M109.093799

    Figure Lengend Snippet: Cellular TIMP-1 is protective and decreases in response to ER stress. A, typical Western blot of TIMP-1 on lysate of CATH.a cells that has been exposed to 1 μm BFA for various time periods. B, typical Western blot against TIMP-1 on lysates of CATH.a cells transfected with caspase-12 siRNA (#1 or #2) or negative siRNA control (N) and subsequently treated with BFA. C, TIMP-1 Western blot on lysate of CATH.a cells that was pretreated with 1 μm Z-ATAD-FMK for 1 h followed by 1 μm BFA for 24 h. D and E, CATH.a cells transfected with TIMP-1 cDNA were exposed to BFA, extent of cell death was monitored by TUNEL staining, and TUNEL-positive cells were counted and expressed as the percentage of total cells (D), and MMP-3 enzyme activity was measured (E). *, p < 0.05; **, p < 0.01 versus respective untreated control; +, p < 0.05; ++, p < 0.01 versus mock transfected BFA-treated.

    Article Snippet: Primary antibodies used were goat polyclonal anti-mouse MMP-3 antibody (R&D Systems Inc., Minneapolis, MN), goat polyclonal anti-human MMP-3 antibody (BioVision), goat polyclonal anti-mouse TIMP-1 antibody (R&D Systems Inc.), mouse monoclonal anti-human TIMP-1 antibody (Calbiochem), rabbit polyclonal anti-mouse caspase-12 antibody (Cell Signaling Technology Inc., Beverly, MA), and rabbit anti-mouse cleaved caspase-3 (Asp-175) antibody (Cell Signaling Technology Inc.).

    Techniques: Western Blot, Transfection, TUNEL Assay, Staining, Activity Assay