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incyclinide metastat  (MetaStat Inc)

 
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    MetaStat Inc incyclinide metastat
    Incyclinide Metastat, supplied by MetaStat Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/incyclinide metastat/product/MetaStat Inc
    Average 90 stars, based on 1 article reviews
    incyclinide metastat - by Bioz Stars, 2026-02
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    (A) Shown is the general structure of the tetracyclines with the keto-enol system (pink) at C11 & C12 that is responsible for the chelation of Zn 2+ and other divalent ions. Structural modifications in 12-aminominocycline and R464 disrupt the chelation center (blue & orange circles). (B) Colorimetric assay measuring the % remaining Zn 2+ as a function of tetracycline concentration, indicative of the chelation effect of each tetracycline. 12-aminominocycline does not chelate ions at concentrations up to 1800 µM, whereas 300 µM is required for R464. Other tetracyclines tested (grey) include: 4-epiminocycline, minocycline, <t>Col-3,</t> Doxycycline, Tigecycline, & Evaracycline. EDTA was used as a positive control. (C) Bar graph shows the % remaining recombinant MMP9 activity after tetracycline treatment (100 µM). The assay measures proteolytic cleavage of a fluorogenic substrate, released upon cleavage. NNGH is a broad-spectrum inhibitor of matrix metalloproteinases and was used as a positive control. Significance was determined by one-way ANOVA with Dunnett’s multiple comparisons, where *** = p < 0.001 and **** = p < 0.0001. Error bars indicate mean ± SD from three independent trials. (D) Dose response curve of four neuroprotective tetracyclines. Tetracyclines with IC 50 greater than 300 µM are indicated as “not determined” (n.d.).
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    (A) Shown is the general structure of the tetracyclines with the keto-enol system (pink) at C11 & C12 that is responsible for the chelation of Zn 2+ and other divalent ions. Structural modifications in 12-aminominocycline and R464 disrupt the chelation center (blue & orange circles). (B) Colorimetric assay measuring the % remaining Zn 2+ as a function of tetracycline concentration, indicative of the chelation effect of each tetracycline. 12-aminominocycline does not chelate ions at concentrations up to 1800 µM, whereas 300 µM is required for R464. Other tetracyclines tested (grey) include: 4-epiminocycline, minocycline, <t>Col-3,</t> Doxycycline, Tigecycline, & Evaracycline. EDTA was used as a positive control. (C) Bar graph shows the % remaining recombinant MMP9 activity after tetracycline treatment (100 µM). The assay measures proteolytic cleavage of a fluorogenic substrate, released upon cleavage. NNGH is a broad-spectrum inhibitor of matrix metalloproteinases and was used as a positive control. Significance was determined by one-way ANOVA with Dunnett’s multiple comparisons, where *** = p < 0.001 and **** = p < 0.0001. Error bars indicate mean ± SD from three independent trials. (D) Dose response curve of four neuroprotective tetracyclines. Tetracyclines with IC 50 greater than 300 µM are indicated as “not determined” (n.d.).
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    (A) Shown is the general structure of the tetracyclines with the keto-enol system (pink) at C11 & C12 that is responsible for the chelation of Zn 2+ and other divalent ions. Structural modifications in 12-aminominocycline and R464 disrupt the chelation center (blue & orange circles). (B) Colorimetric assay measuring the % remaining Zn 2+ as a function of tetracycline concentration, indicative of the chelation effect of each tetracycline. 12-aminominocycline does not chelate ions at concentrations up to 1800 µM, whereas 300 µM is required for R464. Other tetracyclines tested (grey) include: 4-epiminocycline, minocycline, <t>Col-3,</t> Doxycycline, Tigecycline, & Evaracycline. EDTA was used as a positive control. (C) Bar graph shows the % remaining recombinant MMP9 activity after tetracycline treatment (100 µM). The assay measures proteolytic cleavage of a fluorogenic substrate, released upon cleavage. NNGH is a broad-spectrum inhibitor of matrix metalloproteinases and was used as a positive control. Significance was determined by one-way ANOVA with Dunnett’s multiple comparisons, where *** = p < 0.001 and **** = p < 0.0001. Error bars indicate mean ± SD from three independent trials. (D) Dose response curve of four neuroprotective tetracyclines. Tetracyclines with IC 50 greater than 300 µM are indicated as “not determined” (n.d.).
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    incyclinide (aka metastat)  (MetaStat Inc)
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    (A) Shown is the general structure of the tetracyclines with the keto-enol system (pink) at C11 & C12 that is responsible for the chelation of Zn 2+ and other divalent ions. Structural modifications in 12-aminominocycline and R464 disrupt the chelation center (blue & orange circles). (B) Colorimetric assay measuring the % remaining Zn 2+ as a function of tetracycline concentration, indicative of the chelation effect of each tetracycline. 12-aminominocycline does not chelate ions at concentrations up to 1800 µM, whereas 300 µM is required for R464. Other tetracyclines tested (grey) include: 4-epiminocycline, minocycline, <t>Col-3,</t> Doxycycline, Tigecycline, & Evaracycline. EDTA was used as a positive control. (C) Bar graph shows the % remaining recombinant MMP9 activity after tetracycline treatment (100 µM). The assay measures proteolytic cleavage of a fluorogenic substrate, released upon cleavage. NNGH is a broad-spectrum inhibitor of matrix metalloproteinases and was used as a positive control. Significance was determined by one-way ANOVA with Dunnett’s multiple comparisons, where *** = p < 0.001 and **** = p < 0.0001. Error bars indicate mean ± SD from three independent trials. (D) Dose response curve of four neuroprotective tetracyclines. Tetracyclines with IC 50 greater than 300 µM are indicated as “not determined” (n.d.).
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    (A) Shown is the general structure of the tetracyclines with the keto-enol system (pink) at C11 & C12 that is responsible for the chelation of Zn 2+ and other divalent ions. Structural modifications in 12-aminominocycline and R464 disrupt the chelation center (blue & orange circles). (B) Colorimetric assay measuring the % remaining Zn 2+ as a function of tetracycline concentration, indicative of the chelation effect of each tetracycline. 12-aminominocycline does not chelate ions at concentrations up to 1800 µM, whereas 300 µM is required for R464. Other tetracyclines tested (grey) include: 4-epiminocycline, minocycline, Col-3, Doxycycline, Tigecycline, & Evaracycline. EDTA was used as a positive control. (C) Bar graph shows the % remaining recombinant MMP9 activity after tetracycline treatment (100 µM). The assay measures proteolytic cleavage of a fluorogenic substrate, released upon cleavage. NNGH is a broad-spectrum inhibitor of matrix metalloproteinases and was used as a positive control. Significance was determined by one-way ANOVA with Dunnett’s multiple comparisons, where *** = p < 0.001 and **** = p < 0.0001. Error bars indicate mean ± SD from three independent trials. (D) Dose response curve of four neuroprotective tetracyclines. Tetracyclines with IC 50 greater than 300 µM are indicated as “not determined” (n.d.).

    Journal: bioRxiv

    Article Title: Atypical tetracyclines promote longevity and ferroptotic neuroprotection via translation attenuation

    doi: 10.64898/2026.01.09.698733

    Figure Lengend Snippet: (A) Shown is the general structure of the tetracyclines with the keto-enol system (pink) at C11 & C12 that is responsible for the chelation of Zn 2+ and other divalent ions. Structural modifications in 12-aminominocycline and R464 disrupt the chelation center (blue & orange circles). (B) Colorimetric assay measuring the % remaining Zn 2+ as a function of tetracycline concentration, indicative of the chelation effect of each tetracycline. 12-aminominocycline does not chelate ions at concentrations up to 1800 µM, whereas 300 µM is required for R464. Other tetracyclines tested (grey) include: 4-epiminocycline, minocycline, Col-3, Doxycycline, Tigecycline, & Evaracycline. EDTA was used as a positive control. (C) Bar graph shows the % remaining recombinant MMP9 activity after tetracycline treatment (100 µM). The assay measures proteolytic cleavage of a fluorogenic substrate, released upon cleavage. NNGH is a broad-spectrum inhibitor of matrix metalloproteinases and was used as a positive control. Significance was determined by one-way ANOVA with Dunnett’s multiple comparisons, where *** = p < 0.001 and **** = p < 0.0001. Error bars indicate mean ± SD from three independent trials. (D) Dose response curve of four neuroprotective tetracyclines. Tetracyclines with IC 50 greater than 300 µM are indicated as “not determined” (n.d.).

    Article Snippet: Tetracyclines: Minocycline (MP Biomedicals, Cat#155718), 4-epiminocycline (Toronto Research Chemicals, Cat#TRC-E588540), Doxycycline (Sigma, Cat#D9891), Col-3 (Incyclinide, MedChemExpress, Cat#HY-13648), R464449 (Sigma-Aldrich, Cat#R464449), 12-aminominocycline (Toronto Research Chemicals, Cat#TRC-A618285), Tigecycline (LKT Laboratories, Cat#T3324).

    Techniques: Colorimetric Assay, Concentration Assay, Positive Control, Recombinant, Activity Assay