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anti timp1  (R&D Systems)


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    R&D Systems anti timp1
    Anti Timp1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 61 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mouse+anti+timp+1+antibody/Mouse+TIMP-1+Antibody/pm40209863-130-25-26
    Average 94 stars, based on 61 article reviews
    anti timp1 - by Bioz Stars, 2026-09
    94/100 stars

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    Membrane:

    Article Title: Tissue inhibitor of matrix metalloproteinases-1 loaded poly(lactic-co-glycolic acid) nanoparticles for delivery across the blood–brain barrier
    Article Snippet: .. For detection, the membrane was incubated overnight in 1:200 dilution of mouse anti-TIMP-1 antibody (AF980; R&D Systems, Minneapolis, MN, USA), and rabbit polyclonal 6× Histag antibody (ab9108; Abcam, Cambridge, UK) in TBST at 4°C. .. The membrane was washed three times with TBST and incubated with horseradish peroxidaseconjugated secondary antibody, and the bands were visualized using ECL Plus reagent (GE Healthcare Bio-Sciences, Uppsala, Sweden) substrate solution.

    Article Title: Tissue inhibitor of matrix metalloproteinases-1 loaded poly(lactic-co-glycolic acid) nanoparticles for delivery across the blood–brain barrier
    Article Snippet: .. For detection, the membrane was incubated overnight in 1:200 dilution of mouse anti-TIMP-1 antibody (AF980; R&D Systems, Minneapolis, MN, USA), and rabbit polyclonal 6× Histag antibody (ab9108; Abcam, Cambridge, UK) in TBST at 4°C. .. The membrane was washed three times with TBST and incubated with horseradish peroxidase-conjugated secondary antibody, and the bands were visualized using ECL Plus reagent (GE Healthcare Bio-Sciences, Uppsala, Sweden) substrate solution.

    Incubation:

    Article Title: Tissue inhibitor of matrix metalloproteinases-1 loaded poly(lactic-co-glycolic acid) nanoparticles for delivery across the blood–brain barrier
    Article Snippet: .. For detection, the membrane was incubated overnight in 1:200 dilution of mouse anti-TIMP-1 antibody (AF980; R&D Systems, Minneapolis, MN, USA), and rabbit polyclonal 6× Histag antibody (ab9108; Abcam, Cambridge, UK) in TBST at 4°C. .. The membrane was washed three times with TBST and incubated with horseradish peroxidaseconjugated secondary antibody, and the bands were visualized using ECL Plus reagent (GE Healthcare Bio-Sciences, Uppsala, Sweden) substrate solution.

    Article Title: Tissue inhibitor of matrix metalloproteinases-1 loaded poly(lactic-co-glycolic acid) nanoparticles for delivery across the blood–brain barrier
    Article Snippet: .. For detection, the membrane was incubated overnight in 1:200 dilution of mouse anti-TIMP-1 antibody (AF980; R&D Systems, Minneapolis, MN, USA), and rabbit polyclonal 6× Histag antibody (ab9108; Abcam, Cambridge, UK) in TBST at 4°C. .. The membrane was washed three times with TBST and incubated with horseradish peroxidase-conjugated secondary antibody, and the bands were visualized using ECL Plus reagent (GE Healthcare Bio-Sciences, Uppsala, Sweden) substrate solution.



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    Fig. 11. Schematic diagram of EZH2-mediated <t>TIMP1</t> suppression in GABAergic interneurons driving spinal microglia activation through MMP-9-TLR2/4-NLRP3 signaling in neuropathic pain. TIMP1 deficiency in spinal GABAergic interneurons contributes to the activation of MMP-9 in the spinal cord, which, in turn, acti vates microglia and induces IL-1β maturation via an TLR2/4-NLRP3 dependent pathway. The suppression of Timp1 is linked to epigenetic silencing mechanisms in neuropathic pain. Substance P, released from primary sensory neurons, triggers the transcriptional suppression of Timp1 in spinal GABAergic interneurons by upregulating EZH2 expression and increasing H3K27me3 enrichment at the Timp1 promoter.
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    Fig. 11. Schematic diagram of EZH2-mediated <t>TIMP1</t> suppression in GABAergic interneurons driving spinal microglia activation through MMP-9-TLR2/4-NLRP3 signaling in neuropathic pain. TIMP1 deficiency in spinal GABAergic interneurons contributes to the activation of MMP-9 in the spinal cord, which, in turn, acti vates microglia and induces IL-1β maturation via an TLR2/4-NLRP3 dependent pathway. The suppression of Timp1 is linked to epigenetic silencing mechanisms in neuropathic pain. Substance P, released from primary sensory neurons, triggers the transcriptional suppression of Timp1 in spinal GABAergic interneurons by upregulating EZH2 expression and increasing H3K27me3 enrichment at the Timp1 promoter.
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    Fig. 11. Schematic diagram of EZH2-mediated <t>TIMP1</t> suppression in GABAergic interneurons driving spinal microglia activation through MMP-9-TLR2/4-NLRP3 signaling in neuropathic pain. TIMP1 deficiency in spinal GABAergic interneurons contributes to the activation of MMP-9 in the spinal cord, which, in turn, acti vates microglia and induces IL-1β maturation via an TLR2/4-NLRP3 dependent pathway. The suppression of Timp1 is linked to epigenetic silencing mechanisms in neuropathic pain. Substance P, released from primary sensory neurons, triggers the transcriptional suppression of Timp1 in spinal GABAergic interneurons by upregulating EZH2 expression and increasing H3K27me3 enrichment at the Timp1 promoter.
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    Fig. 11. Schematic diagram of EZH2-mediated <t>TIMP1</t> suppression in GABAergic interneurons driving spinal microglia activation through MMP-9-TLR2/4-NLRP3 signaling in neuropathic pain. TIMP1 deficiency in spinal GABAergic interneurons contributes to the activation of MMP-9 in the spinal cord, which, in turn, acti vates microglia and induces IL-1β maturation via an TLR2/4-NLRP3 dependent pathway. The suppression of Timp1 is linked to epigenetic silencing mechanisms in neuropathic pain. Substance P, released from primary sensory neurons, triggers the transcriptional suppression of Timp1 in spinal GABAergic interneurons by upregulating EZH2 expression and increasing H3K27me3 enrichment at the Timp1 promoter.
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    Fig. 11. Schematic diagram of EZH2-mediated <t>TIMP1</t> suppression in GABAergic interneurons driving spinal microglia activation through MMP-9-TLR2/4-NLRP3 signaling in neuropathic pain. TIMP1 deficiency in spinal GABAergic interneurons contributes to the activation of MMP-9 in the spinal cord, which, in turn, acti vates microglia and induces IL-1β maturation via an TLR2/4-NLRP3 dependent pathway. The suppression of Timp1 is linked to epigenetic silencing mechanisms in neuropathic pain. Substance P, released from primary sensory neurons, triggers the transcriptional suppression of Timp1 in spinal GABAergic interneurons by upregulating EZH2 expression and increasing H3K27me3 enrichment at the Timp1 promoter.
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    Image Search Results


    Fig. 11. Schematic diagram of EZH2-mediated TIMP1 suppression in GABAergic interneurons driving spinal microglia activation through MMP-9-TLR2/4-NLRP3 signaling in neuropathic pain. TIMP1 deficiency in spinal GABAergic interneurons contributes to the activation of MMP-9 in the spinal cord, which, in turn, acti vates microglia and induces IL-1β maturation via an TLR2/4-NLRP3 dependent pathway. The suppression of Timp1 is linked to epigenetic silencing mechanisms in neuropathic pain. Substance P, released from primary sensory neurons, triggers the transcriptional suppression of Timp1 in spinal GABAergic interneurons by upregulating EZH2 expression and increasing H3K27me3 enrichment at the Timp1 promoter.

    Journal: Brain, behavior, and immunity

    Article Title: EZH2-mediated suppression of TIMP1 in spinal GABAergic interneurons drives microglial activation via MMP-9-TLR2/4-NLRP3 signaling in neuropathic pain.

    doi: 10.1016/j.bbi.2025.04.007

    Figure Lengend Snippet: Fig. 11. Schematic diagram of EZH2-mediated TIMP1 suppression in GABAergic interneurons driving spinal microglia activation through MMP-9-TLR2/4-NLRP3 signaling in neuropathic pain. TIMP1 deficiency in spinal GABAergic interneurons contributes to the activation of MMP-9 in the spinal cord, which, in turn, acti vates microglia and induces IL-1β maturation via an TLR2/4-NLRP3 dependent pathway. The suppression of Timp1 is linked to epigenetic silencing mechanisms in neuropathic pain. Substance P, released from primary sensory neurons, triggers the transcriptional suppression of Timp1 in spinal GABAergic interneurons by upregulating EZH2 expression and increasing H3K27me3 enrichment at the Timp1 promoter.

    Article Snippet: The primary antibodies were specific for β-actin (ABclonal, AC026, 1:10000, Wuhan, China), Histone H3 (ABclonal, A2348, 1:1000, Wuhan, China), TriMethyl-Histone H3-K27 (H3K27me3) (ABclonal, A2363, 1:1000, Wuhan, China), EZH2 (ABclonal, A16846, 1:1000, Wuhan, China), tissue inhibitor of metalloproteinase 1 (TIMP1) (R&D Systems, AF980, 0.1 μg/mL), TIMP1 (immunoway, YT4658, 1:500), MMP-9 (ABclonal, A0289, 1:1000, Wuhan, China), IL1β (ABmart, P50520-1R1, 1:800, Shanghai, China), NLRP3 (Adipogen, AG-20B0014-C100, 1:500), caspase-1 (p20; Adipogen, AG-20B-0042-C100, 1:500), NF-κB p65 (ABclonal, A2547, 1:1000, Wuhan, China), phospho-NF-κB p65 (ABclonal, AP0124, 1:1000, Wuhan, China), TLR2 (proteintech, 66645–1-Ig, 1:500) and TLR4 (proteintech, 66350–1-Ig, 1:1000).

    Techniques: Activation Assay, Expressing