biotinylated polyclonal antibodies against human timp2  (R&D Systems)

Journal: Cureus

Article Title: Abnormal Trophoblast Invasion in Early-Onset Preeclampsia: The Involvement of Cystathionine β-Synthase, Specificity Protein 1 and microRNA-22

doi: 10.7759/cureus.104353

Figure Lengend Snippet: mRNA expression of matrix metalloproteinases (MMPs) 2, 9 (a) and tissue inhibitors of metalloproteinase (TIMPs) 1, 2 (b) in the placental tissue samples from pregnancies complicated by early-onset preeclampsia (EOPE). Bar diagrams represent the relative mRNA expression of MMPs 2, 9 (a) and TIMPs 1,2 (b) in placentae from EOPE and normotensive, non-proteinuric controls. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was used as a positive control. Data presented as mean ± SEM. Wilcoxon matched-pairs signed rank (MMPs 2, 9, TIMP-1) and paired t (TIMP-2) tests were applied, *p≤0.05 was considered statistically significant, *p≤0.05, **p≤0.01, ***p≤0.001, ****p≤0.0001, ns: not significant.

Article Snippet: Overnight incubation was done with primary antibodies (MMP-2 (Abcam) at a dilution of 1:1000, MMP-9 (Abcam) at a dilution of 1:1000, TIMP-1 (Thermo) at a dilution of 1:200, TIMP-2 (Novus Biologicals) at a dilution of 1:200, CBS (Abcam) at a dilution of 1:1000 and Sp1 (Merck) at a dilution of 1:400] at 4°C.

Techniques: Expressing, Positive Control

Journal: Cureus

Article Title: Abnormal Trophoblast Invasion in Early-Onset Preeclampsia: The Involvement of Cystathionine β-Synthase, Specificity Protein 1 and microRNA-22

doi: 10.7759/cureus.104353

Figure Lengend Snippet: Protein expression of matrix metalloproteinases (MMPs) 2, 9, and their feedback inhibitor tissue inhibitors of metalloproteinase (TIMPs) 1, 2 as analysed by immunohistochemistry (IHC). Representative IHC images of placentae from early-onset preeclampsia (EOPE) (a, e, i, m) and normotensive, non-proteinuric controls (b, f, j, n) showing MMP-2, MMP-9, TIMP-1 and TIMP-2 localization in syncytiotrophoblasts, stromal component, and blood vessels. Positive controls for MMP-2 (human placenta (c)), MMP-9 (human spleen (g)), TIMP-1 (rat brain (k)) and TIMP-2 (human pancreas (o)). Negative controls for MMP-2 (d), MMP-9 (h), TIMP-1 (l) and TIMP-2 (p), Scale Bar: 50 µm.

Article Snippet: Overnight incubation was done with primary antibodies (MMP-2 (Abcam) at a dilution of 1:1000, MMP-9 (Abcam) at a dilution of 1:1000, TIMP-1 (Thermo) at a dilution of 1:200, TIMP-2 (Novus Biologicals) at a dilution of 1:200, CBS (Abcam) at a dilution of 1:1000 and Sp1 (Merck) at a dilution of 1:400] at 4°C.

Techniques: Expressing, Immunohistochemistry

Journal: Cureus

Article Title: Abnormal Trophoblast Invasion in Early-Onset Preeclampsia: The Involvement of Cystathionine β-Synthase, Specificity Protein 1 and microRNA-22

doi: 10.7759/cureus.104353

Figure Lengend Snippet: Protein expression of matrix metalloproteinases (MMPs) 2, 9 and tissue inhibitors of metalloproteinase (TIMPs) 1, 2 as analysed by immunofluorescence (IF) in EOPE and normotensive controls. Representative IF images of placentae from EOPE and normotensive, non-proteinuric controls showing MMP-2 (a, c (FITC stained), b, d (merged)], MMP-9 (e, g (FITC stained), f, h (merged)), TIMP-1 (i, k (TRITC stained), j, l (merged)) and TIMP-2 (m, o (FITC stained), n, p (merged)) localization in syncytiotrophoblasts, stromal component and blood vessels. Nuclei were stained by 4′,6-diamidino-2-phenylindole (DAPI); Scale Bar: 50 µm, FITC: Fluorescein isothiocyanate, TRITC: Tetramethylrhodamine isothiocyanate.

Article Snippet: Overnight incubation was done with primary antibodies (MMP-2 (Abcam) at a dilution of 1:1000, MMP-9 (Abcam) at a dilution of 1:1000, TIMP-1 (Thermo) at a dilution of 1:200, TIMP-2 (Novus Biologicals) at a dilution of 1:200, CBS (Abcam) at a dilution of 1:1000 and Sp1 (Merck) at a dilution of 1:400] at 4°C.

Techniques: Expressing, Immunofluorescence, Staining

Journal: Cureus

Article Title: Abnormal Trophoblast Invasion in Early-Onset Preeclampsia: The Involvement of Cystathionine β-Synthase, Specificity Protein 1 and microRNA-22

doi: 10.7759/cureus.104353

Figure Lengend Snippet: Immunoblot of matrix metalloproteinases (MMPs) 2, 9 (a, b) and tissue inhibitors of metalloproteinase (TIMPs) 1, 2 (c, d) in the placentae from early-onset preeclampsia (EOPE) as compared to normotensive, non-proteinuric control placentae. Representative images of immunoblot showing the protein expression of MMP-2 (a), MMP-9 (b), TIMP-1 (c) and TIMP-2 (d) in placental tissues of EOPE and normotensive, non-proteinuric controls. Bar diagrams represent the normalized values of MMPs 2, 9 (e) and TIMPs 1, 2 (f) with respect to β-actin (loading control). Data presented as mean ± SEM. Statistical analysis was done using the Wilcoxon matched-pairs signed rank (MMPs 2, 9, TIMP-1) and paired t (TIMP-2) tests; *p≤0.05 was considered statistically significant. *p≤0.05, **p≤0.01, ***p≤0.001, ****p≤0.0001, ns: not significant

Article Snippet: Overnight incubation was done with primary antibodies (MMP-2 (Abcam) at a dilution of 1:1000, MMP-9 (Abcam) at a dilution of 1:1000, TIMP-1 (Thermo) at a dilution of 1:200, TIMP-2 (Novus Biologicals) at a dilution of 1:200, CBS (Abcam) at a dilution of 1:1000 and Sp1 (Merck) at a dilution of 1:400] at 4°C.

Techniques: Western Blot, Control, Expressing

Journal: medRxiv

Article Title: Brain-rejuvenating factor TIMP2 is associated with brain health and neuroprotective lifestyle in aged subjects

doi: 10.64898/2025.12.24.25342952

Figure Lengend Snippet: Plasma TIMP2 was analyzed by SomaLogic in three independent human cohorts, with goals to (A) examine translational relevance of TIMP2 in human brain aging and (B) link TIMP2 to known brain rejuvenation behaviors. Given observed associations in humans, we examined causal relationships between lifestyle enrichment and TIMP2 in mouse models. We tested whether (C) exposure to an enriched environment influenced plasma TIMP2 and (D) the pro-neurogenic effects of environmental enrichment on the adult hippocampus were dependent on the presence of TIMP2.

Article Snippet: Following electrophoresis, gels were transferred to nitrocellulose membranes, and blots were probed with anti-TIMP2 antibody (1:500, Cell Signaling, cat. #5738S) and developed as previously described ( ).

Techniques: Clinical Proteomics

Journal: medRxiv

Article Title: Brain-rejuvenating factor TIMP2 is associated with brain health and neuroprotective lifestyle in aged subjects

doi: 10.64898/2025.12.24.25342952

Figure Lengend Snippet: Plasma TIMP2 is positively associated with global cognition (A,B) and total gray matter volumes (C,D) in both UCSF and Stanford cohorts.

Article Snippet: Following electrophoresis, gels were transferred to nitrocellulose membranes, and blots were probed with anti-TIMP2 antibody (1:500, Cell Signaling, cat. #5738S) and developed as previously described ( ).

Techniques: Clinical Proteomics

Journal: medRxiv

Article Title: Brain-rejuvenating factor TIMP2 is associated with brain health and neuroprotective lifestyle in aged subjects

doi: 10.64898/2025.12.24.25342952

Figure Lengend Snippet: Longitudinal TIMP2 data in ROSMAP (E) show that change in TIMP2 (Timepoint 2 - Timepoint 1) is normally distributed (F) and that decreases in plasma TIMP2 are associated with steeper cognitive declines over time, particularly in memory (G,H) .

Article Snippet: Following electrophoresis, gels were transferred to nitrocellulose membranes, and blots were probed with anti-TIMP2 antibody (1:500, Cell Signaling, cat. #5738S) and developed as previously described ( ).

Techniques: Clinical Proteomics

Journal: medRxiv

Article Title: Brain-rejuvenating factor TIMP2 is associated with brain health and neuroprotective lifestyle in aged subjects

doi: 10.64898/2025.12.24.25342952

Figure Lengend Snippet: (A) Higher levels of physical activity associated with higher plasma TIMP2 concentrations in the UCSF cohort and (B) changes in engagement in multi-domain lifestyle factors associated with changes in plasma TIMP2 concentrations over time in the longitudinal ROSMAP cohort.

Article Snippet: Following electrophoresis, gels were transferred to nitrocellulose membranes, and blots were probed with anti-TIMP2 antibody (1:500, Cell Signaling, cat. #5738S) and developed as previously described ( ).

Techniques: Activity Assay, Clinical Proteomics

Journal: medRxiv

Article Title: Brain-rejuvenating factor TIMP2 is associated with brain health and neuroprotective lifestyle in aged subjects

doi: 10.64898/2025.12.24.25342952

Figure Lengend Snippet: (A) Schematic diagram of the enriched environment (EE) or standard environment (SE) paradigm for wildtype (WT) mice using actual images of sample enrichment or standard configurations, after which blood is collected for plasma immunoblotting experiments. (B) TIMP2 immunoblotting (top) from plasma of WT mice exposed to EE and SE paradigm with Ponceau S stain (bottom) (N = 5 female mice per group; 2–3 months of age) with (C) corresponding quantification. * P <0.05, Student’s t test. (D) Schematic diagram of the EE and SE workflow used for WT and TIMP2 KO mice to examine adult hippocampal neurogenesis by confocal imaging. (E) Representative confocal images of brain sections containing dentate gyrus (DG) from WT and TIMP2 KO female mice that were stained with antibodies for doublecortin (DCX) exposed to SE or EE with (F) corresponding quantification of the total number of DCX⁺ cells in DG in each group (N = 7–11 mice per group, 2–3 months of age; 2-way ANOVA, Sidak’s test for multiple comparisons; * P < 0.05; n.s., not significant. Data represent mean ± SEM, with individual mice represented by points.

Article Snippet: Following electrophoresis, gels were transferred to nitrocellulose membranes, and blots were probed with anti-TIMP2 antibody (1:500, Cell Signaling, cat. #5738S) and developed as previously described ( ).

Techniques: Clinical Proteomics, Western Blot, Staining, Imaging

Journal: Molecular Therapy Oncology

Article Title: Perturbed CD81 in lung-cancer-derived extracellular vesicles modifies its function in cancer pathophysiology

doi: 10.1016/j.omton.2025.201037

Figure Lengend Snippet: Characterization of EVs and changes in cargo packaging of CD81 silenced EV Characterization of EVs from H1299- and A549-cell-isolated naive and siRNA-mediated CD81 knockdown and analyses of si-CD81 EVs package (A) Nanoparticle analysis of EVs and TEM image of EV shows the bilayer structure of EV. (B) Western blot analysis was performed to evaluate the membrane and intraluminal proteins characteristic of EVs. The markers analyzed included CD63, CD9, and the endoplasmic reticulum marker GRP94. (C) Selected genes from array analysis that were confirmed by PCR with their fold change values. Protein-protein interaction between differentially expressed genes and CD81. (D) String analysis showed the protein-protein interaction (PPI) network of 12 proteins. The lines connecting the proteins depict “known” or “predicted” interactions. The thickness of the line corresponds to the strength of the interaction between the proteins. (E) Confirmation of CD81-protein interaction with TIMP2 through co-immunoprecipitation.

Article Snippet: Xenograft tumors were paraffin-embedded and immunostained with antibodies against TIMP2 (sc-21735, 1:100; Santa Cruz), integrin β1 (mouse, sc-9970, 1:100; Santa Cruz), ERK 1/2 (sc-514302, 1:100; Santa Cruz), GSK-3 α/β (sc-7291, 1:100; Santa Cruz), MMP9 (sc-393859, 1:100; Santa Cruz), and MMP2 (sc-13594, 1:100; Santa Cruz).

Techniques: Isolation, Knockdown, Western Blot, Membrane, Marker, Immunoprecipitation