Recombinant Human TIMP3 Proteins
- Known as:
- Recombinant Human TIMP3 Proteins
- Catalog number:
- RB-15-0001P-100
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Ray Biotech
- Gene target:
- Recombinant Human TIMP3 Proteins
Related genes to: Recombinant Human TIMP3 Proteins
- Gene:
- TIMP3 NIH gene
- Name:
- TIMP metallopeptidase inhibitor 3
- Previous symbol:
- SFD
- Synonyms:
- -
- Chromosome:
- 22q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 1993-04-12
- Date modifiied:
- 2014-11-19
Related products to: Recombinant Human TIMP3 Proteins
Related articles to: Recombinant Human TIMP3 Proteins
- Objective This study aimed to investigate the protective effect of a metformin (Met)-adipose-derived mesenchymal stem cell exosome (ADSC-Exo) complex (Met-Exo) against hepatic ischemia-reperfusion injury (IRI) and to determine whether this protection is mediated through the silent information regulator 1(SIRT1)-tissue inhibitor of metalloproteinase 3(TIMP3) axis. Methods Met-Exo was constructed and characterized by nanoparticle tracking analysis, Western blotting, and transmission electron microscopy (TEM). An in vitro model of hepatic IRI was established in mouse hepatocyte AML12 cells subjected to oxygen-glucose deprivation/re-oxygenation (OGD/R). Cell viability, apoptosis, and hepatocyte function markers (AST and ALT) were measured to compare the protective effects of Met-Exo, ADSC-Exo, and Met alone. A Transwell co-culture system was used to evaluate how macrophage polarization influences OGD/R-induced AML12 injury. AML12 cells were assigned to the following groups: Ctrl, OGD/R, Met, ADSC-Exo, Met-Exo, and macrophage-polarization groups (M0, M1, M1+Met-Exo, M1+pcDNA3.1, M1+pcDNA3.1-SIRT1, M1+pcDNA3.1-TIMP3). SIRT1 and TIMP3 protein levels in AML12 cells were determined by Western blot. Macrophage-polarization markers-inducible nitric-oxide synthase (iNOS) and arginase 1 (Arg1) were also quantified. In parallel, AML12 cells' viability, apoptosis, and hepatocellular function indices (AST& ALT) were assessed. A murine hepatic IRI model was constructed, and Met-Exo was administered to assess therapeutic efficacy in vivo. Results Met-Exo was successfully prepared. In vitro, Met-Exo attenuated OGD/R-induced hepatocyte injury, increased viability, reduced apoptosis, and lowered AST and ALT release. Met-Exo pre-treatment suppressed expression of the M1 marker iNOS and enhanced expression the M2 marker Arg1, thereby alleviating OGD/R damage in AML12 cells. OGD/R markedly decreased SIRT1 and TIMP3 expression in AML12 cells, whereas Met-Exo pre-treatment significantly up-regulated SIRT1 and consequently TIMP3 expression. In macrophage polarization experiments, M1 macrophages exacerbated AML12 injury, shown as decreased protein expression of SIRT1 and TIMP3, increased iNOS levels, reduced Arg1 levels, along with diminished AML12 cell viability, increased apoptosis, and elevated AST/ALT. Over-expression of either SIRT1 or TIMP3 reversed these detrimental effects, skewing macrophages toward the M2 phenotype and mitigating AML12 injury. In vivo, Met-Exo markedly ameliorated hepatic IRI in mice. Conclusion Met-Exo protects against hepatic IRI by activating the SIRT1-TIMP3 axis, thereby driving macrophage polarization toward the anti-inflammatory M2 phenotype, attenuating inflammation and apoptosis in hepatocytes subjected to OGD/R. - Source: PubMed
Jiang AiwenPu JiekunZhao XuepingZhang YiNiu CongChen Yong - Tissue inhibitor of metalloproteinase 3 (TIMP-3) is a broad-spectrum inhibitor of matrix metalloproteinases (MMPs) and ADAM/ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family enzymes that regulate extracellular matrix (ECM) homeostasis. Because these enzymes play key roles in articular cartilage turnover, TIMP-3-mediated inhibition protects against cartilage degradation, a hallmark of osteoarthritis (OA), and has been explored as a therapeutic target. Nonetheless, unexpected detrimental effects of TIMP-3 on bone mass and structure have been reported in transgenic mice overexpressing TIMP-3 in cartilage. Mechanistically, TIMP-3 binds catabolic enzymes and blocks their active sites but also interacts with low-density lipoprotein receptor-related protein 1 (LRP-1) and sulfated proteoglycans in the ECM, processes that regulate its half-life through a balance between endocytosis and ECM retention and may influence cell signaling. - Source: PubMed
Publication date: 2026/03/11
Mengozzi ManuelaTowler BenKwabiah JordanRazmandeh FawadSimoes FabioMullen Lisa - In the published manuscript [...]. - Source: PubMed
Publication date: 2026/03/16
Bhola NeelamBareja ChanchalJaiswal Amit KSaluja Daman - - Source: PubMed
Publication date: 2026/03/26
Ruan YuanDing SichengHuang YingxuanZhang Ningning - Diabetic foot ulcers (DFUs) are among the most severe and challenging complications associated with diabetes mellitus, primarily due to chronic inflammation, oxidative stress, and impaired tissue regeneration. To develop and evaluate oleuropein-loaded hyalurosomes (OLE-HLs) as a unique topical nanocarrier system for wound healing using an experimental diabetic rat model. OLE-HLs were synthesized using a modified thin-film hydration method, and the nano-formulation was characterized by measuring the size and potential, followed by TEM, encapsulation efficiency, FTIR, in vitro release studies, and cell cytotoxicity assay. The wound-healing efficacy was evaluated in vitro, using scratch assay and in vivo, via studying the wound closure rate, oxidative stress markers, pro-inflammatory cytokines, TGFβ1 gene expression, and histopathological alterations, complemented by immunohistochemical analysis. OLE-HLs exhibited a mean particle size of 254.64 ± 9.84 nm, a zeta potential of - 25.12 ± 2.18 mV, and an encapsulation efficiency of 89.61 ± 1.82%, while TEM revealed spherical, uniformly sized, and well-dispersed vesicles, confirming stability and homogeneity. FTIR analysis verified successful oleuropein encapsulation and compatibility within the hyalurosomal system. The formulation displayed a biphasic release profile, with 26.47 ± 0.86% released in the first hour and 76.72 ± 2.45% within 24 h. Cytotoxicity assays showed enhanced bioactivity (IC: 269.63 µg/mL) compared with free OLE (644.81 µg/mL). The scratching assay model was validated by the in vivo model, where OLE-HLs significantly promoted wound healing by reducing oxidative stress, as shown by increased GSH and GST levels and decreased MPO activity. It also suppressed inflammatory mediators (IL-6, IL-17, TNF-α, MMP-13, ADAMTS-5) and enhanced TIMP-3 expression. Additionally, regulation of TGFβ1 expression and improved histopathological and immunohistochemical features collectively supported better tissue repair. These data suggest that OLE-HLs notably promote diabetic foot ulcer healing by modulating inflammation, oxidative stress, and cellular regeneration, thereby warranting further clinical investigation. - Source: PubMed
Publication date: 2026/03/26
Elgendy Ahmed IEl-Gendy Ahmed OAboud Heba MAbo El-Ela Fatma IZanaty Mohamed I