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monosodium urate msu tlrl msu  (InvivoGen)


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    InvivoGen monosodium urate msu tlrl msu
    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 <t>monosodium</t> urate <t>(MSU)</t> 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.
    Monosodium Urate Msu Tlrl Msu, 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/msu+tlrl+msu/MSU+Crystals/pmc13265349-68-3-13
    Average 96 stars, based on 328 article reviews
    monosodium urate msu tlrl msu - by Bioz Stars, 2026-09
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    1) Product Images from "A feedback loop sustaining neutrophil extracellular trap formation involves S100 proteins, histones, TLR2 and RAGE, and is restrained by albumin"

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

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2026.1774475

    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.
    Figure Legend 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.

    Techniques Used: Immunoprecipitation, Incubation, Microscopy, Positive Control

    Related Articles

    other:

    Article Title: Identification of D359-0396 as a novel inhibitor of the activation of NLRP3 inflammasome.
    Article Snippet: MSU (tlrl-msu) was from Invivogen.

    Article Title: Broxyquinoline targets NLRP3 to inhibit inflammasome activation and alleviate NLRP3-associated inflammatory diseases.
    Article Snippet: The NLR family pyrin domain-containing 3 (NLRP3) inflammasome is responsible for various pathogenic and non-pathogenic damage signals and plays a critical role in host defense against pathogens and physiological damage.. However, inflammasome activation and its subsequent effects also lead to a variety of inflammatory diseases.. In this study, we identified broxyquinoline, an FDA-approved antimicrobial drug, as a effective NLRP3 inflammasome inhibitor.

    Article Title: Cofilin-1 is a Redox-Sensitive Guard of the NLRP3 Inflammasome
    Article Snippet: Ultra-pure flagellin (tlrl-pstfla), ATP (tlrl-atpl), poly (dA:dT) (tlrl-patn), nigericin (tlrl-nig), MSU (tlrl-msu), and ultra-pure LPS (tlrl-3pelps) were obtained from InvivoGen.

    Article Title: SLC25A3 negatively regulates NLRP3 inflammasome activation by restricting the function of NLRP3
    Article Snippet: Puromycin (ant-pr-1), nigericin (tlrl-nig), MDP (tlrl-mdp), poly(dA:dT)/LyoVec (tlrl-patc), Val-boroPro (tlrl-vbp-10), MSU (tlrl-msu), and Alum (tlrl-alk) were purchased from InvivoGen Biotech Co, Ltd Salmonella typhimurium was reserved in our laboratory.

    Article Title: Targeting KAT2A inhibits inflammatory macrophage activation and rheumatoid arthritis through epigenetic and metabolic reprogramming
    Article Snippet: Nigericin (tlrl‐nig), ATP (tlrl‐atpl), and MSU (tlrl‐msu) were from InvivoGen.

    Article Title: GSK461364 Inhibits NLRP3 Inflammasome by Targeting NEK7 Phosphorylation
    Article Snippet: ATP (tlrl‐atpl), Ultra‐pure LPS (for cell, tlrl‐peklps), LPS(for mice, tlrl‐eklps), MSU (tlrl‐msu), Nigericin (tlrl‐nig), Pam3CSK4 (tlrl‐pms), FLA‐ST (tlrl‐stfla), and Poly(dA:dT) (tlrl‐patn) were purchased from Invivogen.

    Article Title: USP13 stabilizes NLRP3 to facilitate inflammasome activation by preventing TRIM31-mediated NLRP3 ubiquitination and degradation
    Article Snippet: Ultrapure LPS (tlrl-pb5lps), Pam3CSK4 (tlrl-pms), ATP (tlrl-atp), nigericin (tlrl-nig), MSU (tlrl-msu), flagellin (tlrl-epstfla), and poly(dA:dT) (tlrl-patn-1) were purchased from Invivogen.

    Article Title: GSK461364 Inhibits NLRP3 Inflammasome by Targeting NEK7 Phosphorylation.
    Article Snippet: Reagents: ATP (tlrl-atpl), Ultra-pure LPS (for cell, tlrl-peklps), LPS(for mice, tlrl-eklps), MSU (tlrl-msu), Nigericin (tlrl-nig), Pam3CSK4 (tlrlpms), FLA-ST (tlrl-stfla), and Poly(dA:dT) (tlrl-patn) were purchased from Invivogen.



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    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 <t>monosodium</t> urate <t>(MSU)</t> 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.
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    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 <t>monosodium</t> urate <t>(MSU)</t> 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.
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    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