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compound 1 3  (Tokyo Chemical Industry)

 
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    Structured Review

    Tokyo Chemical Industry compound 1 3
    Compound 1 3, supplied by Tokyo Chemical Industry, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/compound+3/compound/us12624237-412-2-8
    Average 86 stars, based on 1 article reviews
    compound 1 3 - by Bioz Stars, 2026-10
    86/100 stars

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    other:

    Article Title: Slow Magnetic Relaxation of Ni(III) Complexes toward Molecular Spin Qubits
    Article Snippet: Molecule-based magnetic materials are promising candidates for molecular spin qubits, which utilize spin relaxation behavior.. Various kinds of transition metal complexes with S=1/2 have been reported to act as spin qubits with long spin-spin relaxation times (T2).. However, the spin qubit properties of low-spin Ni(III) complexes are not as well known since Ni(III) compounds are often unstable.

    Article Title: Optical limiting property of a liquid malononitrile derivative on 800 nm laser pulses
    Article Snippet: A new liquid malononitrile derivative (LBDBP) has been synthesized by incorporating four tetraethylene glycol groups into the prototype scaffold of 2-[Bis-(40-diethylamino-biphenyl-4-yl)-methylene]-malononitrile (BDBP).. The linear photophysical properties, optical/thermal stabilities and optical limiting behaviors of LBDBP and BDBP have been investigated.. The results show that LBDBP has equivalent optical/thermal stability but much better solubility compared with BDBP.

    Article Title: Triisopropylsilylethynyl-Functionalized Anthracene-Based Hole Transport Materials for Efficient Hybrid Lead Halide Perovskite Solar Cells
    Article Snippet: Compound 3 in the synthetic scheme was purchased from TCI.

    Article Title: Rare-earth complex and uses thereof
    Article Snippet: Compound 3 (1.0 g, 2.0 mmol) (purchased from Tokyo Chemical Industries, Co., Ltd.) was melted in CH2Cl2, and H2O2 (30%, 4.5 mL) was dropped therein while cooling the mixture at 0° C. This mixture was stirred for 2 hours.

    Article Title: Chemical synthesis of oligosaccharide derivatives with partial structure of β1-3/1-6 glucan, using monomeric units for the formation of β1-3 and β1-6 glucosidic linkages.
    Article Snippet: β1-3/1-6 Glucans, known for their diverse structures, comprise a β1-3-linked main chain and β1-6-linked short branches.. Laminarin, a β1-3/1-6 glucan extracted from brown seaweed, for instance, includes β1-6 linkages even in the main chain.. The diverse structures provide various beneficial functions for the glucan.

    Article Title: Synthesis, antiproliferative activity and autophagic flux inhibition of new arylsparteine derivatives
    Article Snippet: New series of arylsparteine derivatives were synthesized and evaluated for their cytotoxic activity against four human cancer cell lines (cervical epithelial carcinoma cells Hela, breast cancer cells MCF-7, lung cancer cells A549, and glioma cells U87 MG) and one normal fibroblast cell line.. Structure-activity relationship revealed that introduction of 4-quinolinyl moiety to sparteine afforded a hybrid compound 10 with considerable antiproliferative activity against all tested cancer cell lines.. Compound 10, the most active agent in this study possessed IC50 values of 5.97 ± 1.1 and 9.52 ± 0.3 μM against A549 and Hela cancer cell lines, respectively.


    Nuclear Magnetic Resonance:

    Article Title: Gas generating agent, pressure-sensitive adhesive composition and pressure-sensitive adhesive sheet
    Article Snippet: .. NMR chemical shift ppm (multiplicity, proton number): 4.35-4.40 (t, 2H), 3.55-3.60 (t, 2H), 3.0-3.10 (t, 2H), 2.40-2.60 (m, 3H) As a comparative compound 3, 5-mercapto-1-phenyl-1H tetrazole (manufactured by Tokyo Chemical Industry Co., Ltd.) was prepared. .. [Evaluation] The value of the molar absorption coefficient was obtained as follows: 0.1 mM of the obtained compound was dissolved in ethyl acetate; an absorption spectrum in a wavelength range of from 230 nm to 800 nm was measured by use of a ultraviolet-visible spectrophotometer (ultraviolet-visible spectrophotometer UV2700 manufactured by Shimadzu Corporation); using the absorbance in the obtained absorption spectrum, the molar absorption coefficient was calculated by the following formula: ε=A/c×d (where ε is molar absorption coefficient; A is absorbance; c is mol concentration; and d is cell thickness).



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    (A) Schematic representation of major tryptophan (Trp)-derived metabolic pathways, including the kynurenine pathway (center), the indole-3-pyruvic acid (IPA)–indole-3-acetic acid (IAA) pathway, and the tryptamine– serotonin–melatonin branch (top). Solid, dashed, and double boxes indicate metabolites reported in animals, plants, or both, respectively. Enzymes are indicated at each step: IDO1/IDO2 (indoleamine 2,3-dioxygenase), TDO (tryptophan 2,3-dioxygenase), AFMID (arylformamidase), KAT (kynurenine aminotransferase), TDC (tryptophan decarboxylase), TAA1/TAR (tryptophan aminotransferase), KYNU (kynureninase), KMO (kynurenine 3-monooxygenase), HAAO (3-hydroxyanthranilate 3,4-dioxygenase), ACMSD (α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase), and QPRT (quinolinate phosphoribosyltransferase). Inhibitor targets are indicated at the corresponding steps: JM6 and RO 61-8048 inhibit KMO, <t>and</t> <t>PF-04859989</t> inhibits KAT. (B) Chemical structures of the kynurenine pathway metabolites quantified in this study: kynurenine, kynurenic acid (KYNA), and 3-hydroxyanthranilic acid (3-HAA). (C) Chemical structures of the inhibitors used in this study. Core structural differences between JM6 and RO 61-8048 are highlighted in red.
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    compound 1 3  (Tokyo Chemical Industry)
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    (A) Schematic representation of major tryptophan (Trp)-derived metabolic pathways, including the kynurenine pathway (center), the indole-3-pyruvic acid (IPA)–indole-3-acetic acid (IAA) pathway, and the tryptamine– serotonin–melatonin branch (top). Solid, dashed, and double boxes indicate metabolites reported in animals, plants, or both, respectively. Enzymes are indicated at each step: IDO1/IDO2 (indoleamine 2,3-dioxygenase), TDO (tryptophan 2,3-dioxygenase), AFMID (arylformamidase), KAT (kynurenine aminotransferase), TDC (tryptophan decarboxylase), TAA1/TAR (tryptophan aminotransferase), KYNU (kynureninase), KMO (kynurenine 3-monooxygenase), HAAO (3-hydroxyanthranilate 3,4-dioxygenase), ACMSD (α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase), and QPRT (quinolinate phosphoribosyltransferase). Inhibitor targets are indicated at the corresponding steps: JM6 and RO 61-8048 inhibit KMO, <t>and</t> <t>PF-04859989</t> inhibits KAT. (B) Chemical structures of the kynurenine pathway metabolites quantified in this study: kynurenine, kynurenic acid (KYNA), and 3-hydroxyanthranilic acid (3-HAA). (C) Chemical structures of the inhibitors used in this study. Core structural differences between JM6 and RO 61-8048 are highlighted in red.
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    Image Search Results


    (A) Schematic representation of major tryptophan (Trp)-derived metabolic pathways, including the kynurenine pathway (center), the indole-3-pyruvic acid (IPA)–indole-3-acetic acid (IAA) pathway, and the tryptamine– serotonin–melatonin branch (top). Solid, dashed, and double boxes indicate metabolites reported in animals, plants, or both, respectively. Enzymes are indicated at each step: IDO1/IDO2 (indoleamine 2,3-dioxygenase), TDO (tryptophan 2,3-dioxygenase), AFMID (arylformamidase), KAT (kynurenine aminotransferase), TDC (tryptophan decarboxylase), TAA1/TAR (tryptophan aminotransferase), KYNU (kynureninase), KMO (kynurenine 3-monooxygenase), HAAO (3-hydroxyanthranilate 3,4-dioxygenase), ACMSD (α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase), and QPRT (quinolinate phosphoribosyltransferase). Inhibitor targets are indicated at the corresponding steps: JM6 and RO 61-8048 inhibit KMO, and PF-04859989 inhibits KAT. (B) Chemical structures of the kynurenine pathway metabolites quantified in this study: kynurenine, kynurenic acid (KYNA), and 3-hydroxyanthranilic acid (3-HAA). (C) Chemical structures of the inhibitors used in this study. Core structural differences between JM6 and RO 61-8048 are highlighted in red.

    Journal: bioRxiv

    Article Title: Auxin is metabolized through kynurenine in Hypericum perforatum L

    doi: 10.64898/2026.05.18.726114

    Figure Lengend Snippet: (A) Schematic representation of major tryptophan (Trp)-derived metabolic pathways, including the kynurenine pathway (center), the indole-3-pyruvic acid (IPA)–indole-3-acetic acid (IAA) pathway, and the tryptamine– serotonin–melatonin branch (top). Solid, dashed, and double boxes indicate metabolites reported in animals, plants, or both, respectively. Enzymes are indicated at each step: IDO1/IDO2 (indoleamine 2,3-dioxygenase), TDO (tryptophan 2,3-dioxygenase), AFMID (arylformamidase), KAT (kynurenine aminotransferase), TDC (tryptophan decarboxylase), TAA1/TAR (tryptophan aminotransferase), KYNU (kynureninase), KMO (kynurenine 3-monooxygenase), HAAO (3-hydroxyanthranilate 3,4-dioxygenase), ACMSD (α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase), and QPRT (quinolinate phosphoribosyltransferase). Inhibitor targets are indicated at the corresponding steps: JM6 and RO 61-8048 inhibit KMO, and PF-04859989 inhibits KAT. (B) Chemical structures of the kynurenine pathway metabolites quantified in this study: kynurenine, kynurenic acid (KYNA), and 3-hydroxyanthranilic acid (3-HAA). (C) Chemical structures of the inhibitors used in this study. Core structural differences between JM6 and RO 61-8048 are highlighted in red.

    Article Snippet: The compound (R)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one (PF-04859989) was identified by a high-throughput screen of the Pfizer compound library as a high-affinity inhibitor of human kynurenine aminotransferase (KAT; ).

    Techniques: Derivative Assay

    ( A) Representative images of explants cultured on MSO (control), kynurenine (KYN), indole-3-acetic acid (IAA), and IAA combined with inhibitors (IAA + JM6, IAA + PF-04859989 [PF], and IAA + RO 61-8048 [RO]). Scale bar = 1 cm (B) Rooting frequency, (C) internodal length (cm per node), (D) root number, and (E) maximum root length (cm) of explants under each treatment. For rooting frequency (B), bars represent mean proportion rooted ± SE. For (C–E), boxplots represent median (center line), interquartile range (box), and range (whiskers). Differences relative to the MSO control were evaluated using Dunnett-adjusted contrasts (p < 0.05; n = 12–18 per treatment).

    Journal: bioRxiv

    Article Title: Auxin is metabolized through kynurenine in Hypericum perforatum L

    doi: 10.64898/2026.05.18.726114

    Figure Lengend Snippet: ( A) Representative images of explants cultured on MSO (control), kynurenine (KYN), indole-3-acetic acid (IAA), and IAA combined with inhibitors (IAA + JM6, IAA + PF-04859989 [PF], and IAA + RO 61-8048 [RO]). Scale bar = 1 cm (B) Rooting frequency, (C) internodal length (cm per node), (D) root number, and (E) maximum root length (cm) of explants under each treatment. For rooting frequency (B), bars represent mean proportion rooted ± SE. For (C–E), boxplots represent median (center line), interquartile range (box), and range (whiskers). Differences relative to the MSO control were evaluated using Dunnett-adjusted contrasts (p < 0.05; n = 12–18 per treatment).

    Article Snippet: The compound (R)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one (PF-04859989) was identified by a high-throughput screen of the Pfizer compound library as a high-affinity inhibitor of human kynurenine aminotransferase (KAT; ).

    Techniques: Cell Culture, Control

    (A–C) Representative extracted ion chromatograms (EICs) of PF-04859989 (A), RO 61-8048 (B), and JM6 (KMO inhibitor II) (C) detected in plant tissue by LC–HRMS. Each panel shows the precursor ion trace at the expected m/z and retention time. (D–F) Relative abundance of PF (D), RO (E), and JM6 (F) in roots and shoots following treatment with MSO (control), inhibitor alone, or IAA + inhibitor. Peak areas are shown as log□□-transformed values. Boxplots represent median (center line), interquartile range (box), and range (whiskers). Signals corresponding to each inhibitor were observed in treated tissues and were not detected in MSO controls. Detection was also observed in IAA co-application treatments.

    Journal: bioRxiv

    Article Title: Auxin is metabolized through kynurenine in Hypericum perforatum L

    doi: 10.64898/2026.05.18.726114

    Figure Lengend Snippet: (A–C) Representative extracted ion chromatograms (EICs) of PF-04859989 (A), RO 61-8048 (B), and JM6 (KMO inhibitor II) (C) detected in plant tissue by LC–HRMS. Each panel shows the precursor ion trace at the expected m/z and retention time. (D–F) Relative abundance of PF (D), RO (E), and JM6 (F) in roots and shoots following treatment with MSO (control), inhibitor alone, or IAA + inhibitor. Peak areas are shown as log□□-transformed values. Boxplots represent median (center line), interquartile range (box), and range (whiskers). Signals corresponding to each inhibitor were observed in treated tissues and were not detected in MSO controls. Detection was also observed in IAA co-application treatments.

    Article Snippet: The compound (R)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one (PF-04859989) was identified by a high-throughput screen of the Pfizer compound library as a high-affinity inhibitor of human kynurenine aminotransferase (KAT; ).

    Techniques: Control, Transformation Assay

    Concentrations of (A, D) kynurenic acid (KYNA), (B, E) kynurenine (KYN), and (C, F) 3-hydroxyanthranilic acid (3-HAA) in shoots (A–C) and roots (D–F) of explants cultured on MSO (control), IAA, or IAA combined with kynurenine pathway inhibitors (IAA + JM6, IAA + PF-04859989, and IAA + RO 61-8048). Concentrations are shown as log□□ (ng g −1 FW). Boxplots represent median (center line), interquartile range (box), and range (whiskers). For shoots (A–C), different letters indicate significant differences among treatments (one-way ANOVA followed by Tukey’s HSD, p < 0.05; n = 3). For roots (D–F), differences relative to the MSO control were evaluated using Dunnett-adjusted contrasts (p < 0.05; n = 3).

    Journal: bioRxiv

    Article Title: Auxin is metabolized through kynurenine in Hypericum perforatum L

    doi: 10.64898/2026.05.18.726114

    Figure Lengend Snippet: Concentrations of (A, D) kynurenic acid (KYNA), (B, E) kynurenine (KYN), and (C, F) 3-hydroxyanthranilic acid (3-HAA) in shoots (A–C) and roots (D–F) of explants cultured on MSO (control), IAA, or IAA combined with kynurenine pathway inhibitors (IAA + JM6, IAA + PF-04859989, and IAA + RO 61-8048). Concentrations are shown as log□□ (ng g −1 FW). Boxplots represent median (center line), interquartile range (box), and range (whiskers). For shoots (A–C), different letters indicate significant differences among treatments (one-way ANOVA followed by Tukey’s HSD, p < 0.05; n = 3). For roots (D–F), differences relative to the MSO control were evaluated using Dunnett-adjusted contrasts (p < 0.05; n = 3).

    Article Snippet: The compound (R)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one (PF-04859989) was identified by a high-throughput screen of the Pfizer compound library as a high-affinity inhibitor of human kynurenine aminotransferase (KAT; ).

    Techniques: Cell Culture, Control

    Indole-3-acetic acid (IAA) is primarily synthesized from tryptophan through the indole-3-pyruvate (IPyA) pathway via tryptophan aminotransferase (TAA) and YUCCA flavin monooxygenase (YUC). Free IAA may be regulated through conjugation, catabolism, oxidative transformation and through feedback effects on tryptophan-derived metabolism. Kynurenine pathway metabolism proceeds through N-formyl-kynurenine and kynurenine, which occupies a central branch point between kynurenic acid formation via kynurenine aminotransferase (KAT) and downstream oxidative metabolism toward 3-hydroxyanthranilic acid (3-HAA) via kynurenine monooxygenase (KMO). Reactive oxygen species (ROS), temperature, drought, iron, and Fe 2+ are shown as potential stress and redox inputs that may influence auxin and kynurenine-associated metabolism. The pharmacological inhibitors used in this study are shown at their proposed targets: PF-04859989 at KAT, and RO-61-8048 and JM6 at kynurenine monooxygenase (KMO). Dashed arrows indicate proposed interactions linking auxin catabolism or oxidative transformation with kynurenine-associated metabolite accumulation and potential feedback on tryptophan-dependent auxin biosynthesis.

    Journal: bioRxiv

    Article Title: Auxin is metabolized through kynurenine in Hypericum perforatum L

    doi: 10.64898/2026.05.18.726114

    Figure Lengend Snippet: Indole-3-acetic acid (IAA) is primarily synthesized from tryptophan through the indole-3-pyruvate (IPyA) pathway via tryptophan aminotransferase (TAA) and YUCCA flavin monooxygenase (YUC). Free IAA may be regulated through conjugation, catabolism, oxidative transformation and through feedback effects on tryptophan-derived metabolism. Kynurenine pathway metabolism proceeds through N-formyl-kynurenine and kynurenine, which occupies a central branch point between kynurenic acid formation via kynurenine aminotransferase (KAT) and downstream oxidative metabolism toward 3-hydroxyanthranilic acid (3-HAA) via kynurenine monooxygenase (KMO). Reactive oxygen species (ROS), temperature, drought, iron, and Fe 2+ are shown as potential stress and redox inputs that may influence auxin and kynurenine-associated metabolism. The pharmacological inhibitors used in this study are shown at their proposed targets: PF-04859989 at KAT, and RO-61-8048 and JM6 at kynurenine monooxygenase (KMO). Dashed arrows indicate proposed interactions linking auxin catabolism or oxidative transformation with kynurenine-associated metabolite accumulation and potential feedback on tryptophan-dependent auxin biosynthesis.

    Article Snippet: The compound (R)-3-amino-1-hydroxy-3,4-dihydroquinolin-2(1H)-one (PF-04859989) was identified by a high-throughput screen of the Pfizer compound library as a high-affinity inhibitor of human kynurenine aminotransferase (KAT; ).

    Techniques: Synthesized, Conjugation Assay, Transformation Assay, Derivative Assay

    The combination of RCM1-NP FA and venetoclax decreases tumor growth and enhances caspase-mediated apoptosis in a murine RMS model. (A) Schematic diagram of tumor cells inoculation and treatment. The figure is created in BioRender. Merjaneh, N. (2024) https://BioRender.com/z67t342 . (B) Combination therapy significantly reduced tumor burden compared with vehicle. The mean vehicle tumor volume on day 21 was 685 mm 3 , compared with the average tumor volume of the combination therapy of 361 mm 3 . The maximum tumor diameter was 17.3×11.5 mm and the corresponding maximum tumor volume was 1,144 mm 3 . Tumor volume was measured at different time points during the experiment (P≤0.01; n=12). (C) Combination therapy inhibited proliferation, as indicated by the decreased number of Ki67-positive cells. Combination therapy increased apoptosis, shown by the increased number of (D) BAX-positive cells and (E) the number of caspase3-positive cells compared with single agents and/or vehicle. A total of five random fields per sample were used to quantify the number of Ki67, BAX and cleaved caspase 3 positive cells per group. Values are shown as mean ± SD. Scale bar, 10 μ m. * P≤0.05, ** P≤0.01, **** P≤0.0001. RMS, rhabdomyosarcoma.

    Journal: International Journal of Oncology

    Article Title: FOXM1 inhibitor, RCM-1, enhances venetoclax mediated apoptosis through downregulation of ATP2B4 in rhabdomyosarcoma

    doi: 10.3892/ijo.2026.5865

    Figure Lengend Snippet: The combination of RCM1-NP FA and venetoclax decreases tumor growth and enhances caspase-mediated apoptosis in a murine RMS model. (A) Schematic diagram of tumor cells inoculation and treatment. The figure is created in BioRender. Merjaneh, N. (2024) https://BioRender.com/z67t342 . (B) Combination therapy significantly reduced tumor burden compared with vehicle. The mean vehicle tumor volume on day 21 was 685 mm 3 , compared with the average tumor volume of the combination therapy of 361 mm 3 . The maximum tumor diameter was 17.3×11.5 mm and the corresponding maximum tumor volume was 1,144 mm 3 . Tumor volume was measured at different time points during the experiment (P≤0.01; n=12). (C) Combination therapy inhibited proliferation, as indicated by the decreased number of Ki67-positive cells. Combination therapy increased apoptosis, shown by the increased number of (D) BAX-positive cells and (E) the number of caspase3-positive cells compared with single agents and/or vehicle. A total of five random fields per sample were used to quantify the number of Ki67, BAX and cleaved caspase 3 positive cells per group. Values are shown as mean ± SD. Scale bar, 10 μ m. * P≤0.05, ** P≤0.01, **** P≤0.0001. RMS, rhabdomyosarcoma.

    Article Snippet: The small molecule compound RCM1 (2-[2-oxo-2-(thiophen-2-yl) ethyl]sulfanyl-4,6-di(thiophen-2-yl) pyridine-3-carbonitrile) was synthesized by Vitas-M Laboratory (95% purity) and dissolved in DMSO for in vitro studies.

    Techniques: