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monosodium urate crystals  (InvivoGen)


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    InvivoGen monosodium urate crystals
    Monosodium Urate Crystals, supplied by InvivoGen, used in various techniques. Bioz Stars score: 96/100, based on 328 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/monosodium+urate+crystals/MSU+Crystals/pm42215451-233-20-28
    Average 96 stars, based on 328 article reviews
    monosodium urate crystals - by Bioz Stars, 2026-09
    96/100 stars

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    Related Articles

    other:

    Article Title: Perturbation of azurophilic granule integrity drives NLRP3-independent IL-1β processing and release in neutrophils.
    Article Snippet: Ultra-pure LPS (E. coli K12), monosodium urate crystals, and MCC950 were from Invivogen (San Diego, California, USA).

    Article Title: Non-decameric NLRP3 reveals a TGN/MTOC-distal pathway of inflammasome activation.
    Article Snippet: Phorbol 12-myristate 13-acetate (PMA, tlr-pma), LPS ultrapure from Escherichia coli K12 (LPSEK, tlr-peklps), nigericin sodium salt (tlr-nig), imiquimod (tlrl-imq) and monosodium urate crystals (MSU, tlr-msu) were obtained from InvivoGen.

    Article Title: MG53 protects against intestinal inflammation by inhibiting NLRP3 inflammasome activation
    Article Snippet: Lipopolysaccharide (LPS) from Escherichia coli 0111: B4 (tlrl-eblps), Nigericin sodium salt (tlrl-nig), adenosine 5′-triphosphate disodium salt (ATP, tlrl-atpl) and monosodium urate crystals (MSU, tlrl-msu) were from InvivoGen.

    Activation Assay:

    Article Title: Glutamine limits NLRP3 inflammasome activation and pyroptosis in macrophages by sustaining the IRG1/itaconate axis.
    Article Snippet: doi:10.1111/febs.70119 Aberrant activation of NACHT, LRR, and PYD domains-containing protein 3 (NLRP3) inflammasome increases the release of mature proinflammatory cytokines interleukin (IL)-1β and IL-18, and enhances pyroptosis; thereby necessitating tight regulation of the NLRP3 inflammasome.. Dysfunctional glutamine metabolism contributes to the pathogenesis of multiple inflammatory disorders, and the precise mechanism remains to be elucidated.. Here, we provide evidence that glutamine deprivation enhances NLRP3 inflammasome activation in macrophages.

    Cell Culture:

    Article Title: The scaffolding and activation of NLRP3 on acidic vesicles depends on their biophysical properties and is independent of intermediate filaments
    Article Snippet: Inflammasomes are nucleated by receptors that become activated upon cellular stresses including ionic dyshomeostasis.. Rather than forming in the cytosol, recent evidence suggests that inflammasomes are nucleated at specific sites in the cell including on cytoskeletal polymers and the membrane surfaces of organelles.. The NLRP3 inflammasome, which is formed upon the loss of cytosolic K, had been proposed to form on intermediate filaments as well as on vesicles along the endocytic pathway.

    Modification:

    Article Title: The scaffolding and activation of NLRP3 on acidic vesicles depends on their biophysical properties and is independent of intermediate filaments
    Article Snippet: Inflammasomes are nucleated by receptors that become activated upon cellular stresses including ionic dyshomeostasis.. Rather than forming in the cytosol, recent evidence suggests that inflammasomes are nucleated at specific sites in the cell including on cytoskeletal polymers and the membrane surfaces of organelles.. The NLRP3 inflammasome, which is formed upon the loss of cytosolic K, had been proposed to form on intermediate filaments as well as on vesicles along the endocytic pathway.

    Transfection:

    Article Title: The scaffolding and activation of NLRP3 on acidic vesicles depends on their biophysical properties and is independent of intermediate filaments
    Article Snippet: Inflammasomes are nucleated by receptors that become activated upon cellular stresses including ionic dyshomeostasis.. Rather than forming in the cytosol, recent evidence suggests that inflammasomes are nucleated at specific sites in the cell including on cytoskeletal polymers and the membrane surfaces of organelles.. The NLRP3 inflammasome, which is formed upon the loss of cytosolic K, had been proposed to form on intermediate filaments as well as on vesicles along the endocytic pathway.

    Saline:

    Article Title: The scaffolding and activation of NLRP3 on acidic vesicles depends on their biophysical properties and is independent of intermediate filaments
    Article Snippet: Inflammasomes are nucleated by receptors that become activated upon cellular stresses including ionic dyshomeostasis.. Rather than forming in the cytosol, recent evidence suggests that inflammasomes are nucleated at specific sites in the cell including on cytoskeletal polymers and the membrane surfaces of organelles.. The NLRP3 inflammasome, which is formed upon the loss of cytosolic K, had been proposed to form on intermediate filaments as well as on vesicles along the endocytic pathway.



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    Image Search Results


    Effect of depleting discrete protein subsets on the ability of SD-supts to induce NETs. Human neutrophils adherent to poly-L-lysine-coated coverslips were stimulated with 1 mg/mL monosodium urate (MSU) for 2.5 h. The culture supernatant was collected and depleted of the original stimulus, yielding a stimulus-depleted culture supernatant (SD-supt). These SD-supts were then pre-cleared and immunoprecipitated using pan-histone (“histones”) or pan-S100 proteins (“S100”) antibodies as described in Methods. Alternatively, SD-supts were pre-cleared, mixed with rh sRAGE, and immunoprecipitated using anti-sRAGE antibodies (“sRAGE”). The resulting supernatants from immunodepleted SD-supts were stored and later used as a NET stimulus. Human neutrophils adherent to poly-L-lysine-coated coverslips were incubated for 4 h at 37 °C in the absence of stimuli (“unstim”) or in the presence of SD-supts that had been only pre-cleared (“isotype”) or immunodepleted of S100 proteins, histones, or sRAGE-bound proteins. NET formation was then assessed by microscopy and standardized NET indices were calculated. A representative experiment is shown (right panel), along with compiled data (mean ± s.e.m.) from at least 3 independent experiments. **, p < 0.01; ***, p< 0.001 vs the positive control; using Student’s paired t test.

    Journal: Frontiers in Immunology

    Article Title: A feedback loop sustaining neutrophil extracellular trap formation involves S100 proteins, histones, TLR2 and RAGE, and is restrained by albumin

    doi: 10.3389/fimmu.2026.1774475

    Figure Lengend Snippet: Effect of depleting discrete protein subsets on the ability of SD-supts to induce NETs. Human neutrophils adherent to poly-L-lysine-coated coverslips were stimulated with 1 mg/mL monosodium urate (MSU) for 2.5 h. The culture supernatant was collected and depleted of the original stimulus, yielding a stimulus-depleted culture supernatant (SD-supt). These SD-supts were then pre-cleared and immunoprecipitated using pan-histone (“histones”) or pan-S100 proteins (“S100”) antibodies as described in Methods. Alternatively, SD-supts were pre-cleared, mixed with rh sRAGE, and immunoprecipitated using anti-sRAGE antibodies (“sRAGE”). The resulting supernatants from immunodepleted SD-supts were stored and later used as a NET stimulus. Human neutrophils adherent to poly-L-lysine-coated coverslips were incubated for 4 h at 37 °C in the absence of stimuli (“unstim”) or in the presence of SD-supts that had been only pre-cleared (“isotype”) or immunodepleted of S100 proteins, histones, or sRAGE-bound proteins. NET formation was then assessed by microscopy and standardized NET indices were calculated. A representative experiment is shown (right panel), along with compiled data (mean ± s.e.m.) from at least 3 independent experiments. **, p < 0.01; ***, p< 0.001 vs the positive control; using Student’s paired t test.

    Article Snippet: Among neutrophil stimuli, monosodium urate (MSU) (tlrl-msu) and ultra-pure peptidoglycan (PGN) were from Invivogen (#tlrl-pgnb3); TNFα (#210-TA) and GM-CSF (#7954-GM) were from R&D Systems; and N-formyl-methionyl-phenylalanine (fMLP) was from Millipore Sigma (#F3506).

    Techniques: Immunoprecipitation, Incubation, Microscopy, Positive Control