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Tokyo Chemical Industry biotin peg2 nhs ester
Biotin Peg2 Nhs Ester, 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
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Labeling:

Article Title: KLP-6 is a kinesin superfamily protein resistant to ADP inhibition.
Article Snippet: .. Tubulin was labeled with Biotin-PEG2-NHS ester (Tokyo Chemical Industry, Tokyo, Japan) and AZDye647 NHS ester (Fluoroprobes, Scottsdale, AZ, USA) as described 61. ..

Article Title: Human spastin functions as an ATPase-independent microtubule nucleator via ring-stack formation
Article Snippet: For preparation of GMPCPP tubulin, tubulin was polymerized with 0.1 mM GMPCPP (NU-405L, Jena Bioscience), and the microtubule pellet was resuspended and depolymerized in PEM containing 0.1 mM GMPCPP. .. For labeling, polymerized microtubules were mixed with AF 568 NHS ester (#14820, Lumiprobe), AF 647 NHS ester (#16820, Lumiprobe) or Biotin-LC-LC-NHS (#B6096, Tokyo Chemical Industry) dissolved in dimethyl sulfoxide (DMSO), and non-reacted dye was removed by two cycles of centrifugation/resuspension or by the polymerization/depolymerization cycle during the abovementioned tubulin purification. ..

Synthesized:

Article Title: IL-1 delineates squalene-based adjuvant efficacy and reactogenicity in a cell-type-specific manner
Article Snippet: Oil-in-water emulsion adjuvant A-910823 and A-910823 excluding α-tocopherol (A-910823 without α-tocopherol) were prepared at Shionogi & Co., Ltd. (Osaka, Japan) by high-pressure homogenization, as described previously , , . .. BODIPY-labeled A-910823 (A-910823-BODIPY), containing 0.1% BODIPY-labeled α-tocopherol of the total α-tocopherol content, was prepared by Shionogi & Co., Ltd. BODIPY-labeled α-tocopherol was synthesized by covalently modifying the hydroxyl groups of α-tocopherol using 6-(Boc-amino) hexyl bromide (#89171, Sigma-Aldrich, Burlington, MA, USA) and BDP FL NHS ester (#D5555, Tokyo Chemical Industry Co., Ltd., Tokyo, Japan). ..

High Performance Liquid Chromatography:

Article Title: Synthesis and Preclinical Evaluation of a Novel [225Ac]Ac–PEG6–Macropa–PAM4 for Targeted Alpha Therapy of Pancreatic Cancer
Article Snippet: Pancreatic cancer, and specifically pancreatic ductal adenocarcinoma (PDAC), is considered to be one of the most aggressive and therapy-resistant cancers, with features such as delayed diagnosis, high growth rates, and unfavorable survival rates [1].. Standard therapies like chemotherapy and external beam radiation are hampered by the dense desmoplastic stroma, hypoxia, and poor vascularization that characterize the PDAC microenvironment.. These challenges profoundly limit drug delivery and diminish therapeutic response, which necessitates the imperative development of new and more efficient treatment strategies [2, 3].

Centrifugation:

Article Title: Human spastin functions as an ATPase-independent microtubule nucleator via ring-stack formation
Article Snippet: For preparation of GMPCPP tubulin, tubulin was polymerized with 0.1 mM GMPCPP (NU-405L, Jena Bioscience), and the microtubule pellet was resuspended and depolymerized in PEM containing 0.1 mM GMPCPP. .. For labeling, polymerized microtubules were mixed with AF 568 NHS ester (#14820, Lumiprobe), AF 647 NHS ester (#16820, Lumiprobe) or Biotin-LC-LC-NHS (#B6096, Tokyo Chemical Industry) dissolved in dimethyl sulfoxide (DMSO), and non-reacted dye was removed by two cycles of centrifugation/resuspension or by the polymerization/depolymerization cycle during the abovementioned tubulin purification. ..

Purification:

Article Title: Human spastin functions as an ATPase-independent microtubule nucleator via ring-stack formation
Article Snippet: For preparation of GMPCPP tubulin, tubulin was polymerized with 0.1 mM GMPCPP (NU-405L, Jena Bioscience), and the microtubule pellet was resuspended and depolymerized in PEM containing 0.1 mM GMPCPP. .. For labeling, polymerized microtubules were mixed with AF 568 NHS ester (#14820, Lumiprobe), AF 647 NHS ester (#16820, Lumiprobe) or Biotin-LC-LC-NHS (#B6096, Tokyo Chemical Industry) dissolved in dimethyl sulfoxide (DMSO), and non-reacted dye was removed by two cycles of centrifugation/resuspension or by the polymerization/depolymerization cycle during the abovementioned tubulin purification. ..



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Characterization of IHMT-15137 as a potent and selective BMX inhibitor. a Chemical structure of IHMT-15137 and its reversible analog IHMT-15138. b Determination of the IC 50 values of IHMT-15137, IHMT-15138 and ibrutinib against the BMX protein via the ADP-Glo kinase assay. c Anti-proliferative activity of IHMT-15137, IHMT-15138 and ibrutinib against TEL-BaF3-BMX cells determined by the CTG assay. d CETSA analysis of the effects of IHMT-15137 on BMX protein stability in H446DDPR and H69AR cell lysates: temperature- and dose-dependent stabilization of BMX by IHMT-15137. The right panels show the results of the quantitative analysis of the BMX protein levels from the Western blots. e DARTS assay confirmation of the direct binding of IHMT-15137 to BMX by assessing the stability of BMX against pronase-mediated proteolysis in H446DDPR and H69AR cell lysates. f Inhibitory effects of IHMT-15137 and IHMT-15138 on BMX phosphorylation (Tyr566) in TEL-BaF3-BMX cells after 4 h of treatment, as determined by Western blotting. g Inhibitory effects of 12 h of IHMT-15137 treatment on BMX phosphorylation (Tyr566) and its downstream signaling pathways in H446DDPR and H69AR cells. h Molecular docking analysis of the irreversible binding mode of IHMT-15137 with BMX (PDB ID: 3SXR). i Effect of IHMT-15137 on <t>Biotin-PEG2-C2-iodoacetamide</t> labeling of BMX via a competitive biotin-iodoacetamide assay. Data were presented as mean ± SEM ( n = 3)
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Characterization of IHMT-15137 as a potent and selective BMX inhibitor. a Chemical structure of IHMT-15137 and its reversible analog IHMT-15138. b Determination of the IC 50 values of IHMT-15137, IHMT-15138 and ibrutinib against the BMX protein via the ADP-Glo kinase assay. c Anti-proliferative activity of IHMT-15137, IHMT-15138 and ibrutinib against TEL-BaF3-BMX cells determined by the CTG assay. d CETSA analysis of the effects of IHMT-15137 on BMX protein stability in H446DDPR and H69AR cell lysates: temperature- and dose-dependent stabilization of BMX by IHMT-15137. The right panels show the results of the quantitative analysis of the BMX protein levels from the Western blots. e DARTS assay confirmation of the direct binding of IHMT-15137 to BMX by assessing the stability of BMX against pronase-mediated proteolysis in H446DDPR and H69AR cell lysates. f Inhibitory effects of IHMT-15137 and IHMT-15138 on BMX phosphorylation (Tyr566) in TEL-BaF3-BMX cells after 4 h of treatment, as determined by Western blotting. g Inhibitory effects of 12 h of IHMT-15137 treatment on BMX phosphorylation (Tyr566) and its downstream signaling pathways in H446DDPR and H69AR cells. h Molecular docking analysis of the irreversible binding mode of IHMT-15137 with BMX (PDB ID: 3SXR). i Effect of IHMT-15137 on <t>Biotin-PEG2-C2-iodoacetamide</t> labeling of BMX via a competitive biotin-iodoacetamide assay. Data were presented as mean ± SEM ( n = 3)
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Characterization of IHMT-15137 as a potent and selective BMX inhibitor. a Chemical structure of IHMT-15137 and its reversible analog IHMT-15138. b Determination of the IC 50 values of IHMT-15137, IHMT-15138 and ibrutinib against the BMX protein via the ADP-Glo kinase assay. c Anti-proliferative activity of IHMT-15137, IHMT-15138 and ibrutinib against TEL-BaF3-BMX cells determined by the CTG assay. d CETSA analysis of the effects of IHMT-15137 on BMX protein stability in H446DDPR and H69AR cell lysates: temperature- and dose-dependent stabilization of BMX by IHMT-15137. The right panels show the results of the quantitative analysis of the BMX protein levels from the Western blots. e DARTS assay confirmation of the direct binding of IHMT-15137 to BMX by assessing the stability of BMX against pronase-mediated proteolysis in H446DDPR and H69AR cell lysates. f Inhibitory effects of IHMT-15137 and IHMT-15138 on BMX phosphorylation (Tyr566) in TEL-BaF3-BMX cells after 4 h of treatment, as determined by Western blotting. g Inhibitory effects of 12 h of IHMT-15137 treatment on BMX phosphorylation (Tyr566) and its downstream signaling pathways in H446DDPR and H69AR cells. h Molecular docking analysis of the irreversible binding mode of IHMT-15137 with BMX (PDB ID: 3SXR). i Effect of IHMT-15137 on <t>Biotin-PEG2-C2-iodoacetamide</t> labeling of BMX via a competitive biotin-iodoacetamide assay. Data were presented as mean ± SEM ( n = 3)
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Characterization of IHMT-15137 as a potent and selective BMX inhibitor. a Chemical structure of IHMT-15137 and its reversible analog IHMT-15138. b Determination of the IC 50 values of IHMT-15137, IHMT-15138 and ibrutinib against the BMX protein via the ADP-Glo kinase assay. c Anti-proliferative activity of IHMT-15137, IHMT-15138 and ibrutinib against TEL-BaF3-BMX cells determined by the CTG assay. d CETSA analysis of the effects of IHMT-15137 on BMX protein stability in H446DDPR and H69AR cell lysates: temperature- and dose-dependent stabilization of BMX by IHMT-15137. The right panels show the results of the quantitative analysis of the BMX protein levels from the Western blots. e DARTS assay confirmation of the direct binding of IHMT-15137 to BMX by assessing the stability of BMX against pronase-mediated proteolysis in H446DDPR and H69AR cell lysates. f Inhibitory effects of IHMT-15137 and IHMT-15138 on BMX phosphorylation (Tyr566) in TEL-BaF3-BMX cells after 4 h of treatment, as determined by Western blotting. g Inhibitory effects of 12 h of IHMT-15137 treatment on BMX phosphorylation (Tyr566) and its downstream signaling pathways in H446DDPR and H69AR cells. h Molecular docking analysis of the irreversible binding mode of IHMT-15137 with BMX (PDB ID: 3SXR). i Effect of IHMT-15137 on <t>Biotin-PEG2-C2-iodoacetamide</t> labeling of BMX via a competitive biotin-iodoacetamide assay. Data were presented as mean ± SEM ( n = 3)
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Characterization of IHMT-15137 as a potent and selective BMX inhibitor. a Chemical structure of IHMT-15137 and its reversible analog IHMT-15138. b Determination of the IC 50 values of IHMT-15137, IHMT-15138 and ibrutinib against the BMX protein via the ADP-Glo kinase assay. c Anti-proliferative activity of IHMT-15137, IHMT-15138 and ibrutinib against TEL-BaF3-BMX cells determined by the CTG assay. d CETSA analysis of the effects of IHMT-15137 on BMX protein stability in H446DDPR and H69AR cell lysates: temperature- and dose-dependent stabilization of BMX by IHMT-15137. The right panels show the results of the quantitative analysis of the BMX protein levels from the Western blots. e DARTS assay confirmation of the direct binding of IHMT-15137 to BMX by assessing the stability of BMX against pronase-mediated proteolysis in H446DDPR and H69AR cell lysates. f Inhibitory effects of IHMT-15137 and IHMT-15138 on BMX phosphorylation (Tyr566) in TEL-BaF3-BMX cells after 4 h of treatment, as determined by Western blotting. g Inhibitory effects of 12 h of IHMT-15137 treatment on BMX phosphorylation (Tyr566) and its downstream signaling pathways in H446DDPR and H69AR cells. h Molecular docking analysis of the irreversible binding mode of IHMT-15137 with BMX (PDB ID: 3SXR). i Effect of IHMT-15137 on <t>Biotin-PEG2-C2-iodoacetamide</t> labeling of BMX via a competitive biotin-iodoacetamide assay. Data were presented as mean ± SEM ( n = 3)
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Characterization of IHMT-15137 as a potent and selective BMX inhibitor. a Chemical structure of IHMT-15137 and its reversible analog IHMT-15138. b Determination of the IC 50 values of IHMT-15137, IHMT-15138 and ibrutinib against the BMX protein via the ADP-Glo kinase assay. c Anti-proliferative activity of IHMT-15137, IHMT-15138 and ibrutinib against TEL-BaF3-BMX cells determined by the CTG assay. d CETSA analysis of the effects of IHMT-15137 on BMX protein stability in H446DDPR and H69AR cell lysates: temperature- and dose-dependent stabilization of BMX by IHMT-15137. The right panels show the results of the quantitative analysis of the BMX protein levels from the Western blots. e DARTS assay confirmation of the direct binding of IHMT-15137 to BMX by assessing the stability of BMX against pronase-mediated proteolysis in H446DDPR and H69AR cell lysates. f Inhibitory effects of IHMT-15137 and IHMT-15138 on BMX phosphorylation (Tyr566) in TEL-BaF3-BMX cells after 4 h of treatment, as determined by Western blotting. g Inhibitory effects of 12 h of IHMT-15137 treatment on BMX phosphorylation (Tyr566) and its downstream signaling pathways in H446DDPR and H69AR cells. h Molecular docking analysis of the irreversible binding mode of IHMT-15137 with BMX (PDB ID: 3SXR). i Effect of IHMT-15137 on <t>Biotin-PEG2-C2-iodoacetamide</t> labeling of BMX via a competitive biotin-iodoacetamide assay. Data were presented as mean ± SEM ( n = 3)
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Characterization of IHMT-15137 as a potent and selective BMX inhibitor. a Chemical structure of IHMT-15137 and its reversible analog IHMT-15138. b Determination of the IC 50 values of IHMT-15137, IHMT-15138 and ibrutinib against the BMX protein via the ADP-Glo kinase assay. c Anti-proliferative activity of IHMT-15137, IHMT-15138 and ibrutinib against TEL-BaF3-BMX cells determined by the CTG assay. d CETSA analysis of the effects of IHMT-15137 on BMX protein stability in H446DDPR and H69AR cell lysates: temperature- and dose-dependent stabilization of BMX by IHMT-15137. The right panels show the results of the quantitative analysis of the BMX protein levels from the Western blots. e DARTS assay confirmation of the direct binding of IHMT-15137 to BMX by assessing the stability of BMX against pronase-mediated proteolysis in H446DDPR and H69AR cell lysates. f Inhibitory effects of IHMT-15137 and IHMT-15138 on BMX phosphorylation (Tyr566) in TEL-BaF3-BMX cells after 4 h of treatment, as determined by Western blotting. g Inhibitory effects of 12 h of IHMT-15137 treatment on BMX phosphorylation (Tyr566) and its downstream signaling pathways in H446DDPR and H69AR cells. h Molecular docking analysis of the irreversible binding mode of IHMT-15137 with BMX (PDB ID: 3SXR). i Effect of IHMT-15137 on <t>Biotin-PEG2-C2-iodoacetamide</t> labeling of BMX via a competitive biotin-iodoacetamide assay. Data were presented as mean ± SEM ( n = 3)
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Characterization of IHMT-15137 as a potent and selective BMX inhibitor. a Chemical structure of IHMT-15137 and its reversible analog IHMT-15138. b Determination of the IC 50 values of IHMT-15137, IHMT-15138 and ibrutinib against the BMX protein via the ADP-Glo kinase assay. c Anti-proliferative activity of IHMT-15137, IHMT-15138 and ibrutinib against TEL-BaF3-BMX cells determined by the CTG assay. d CETSA analysis of the effects of IHMT-15137 on BMX protein stability in H446DDPR and H69AR cell lysates: temperature- and dose-dependent stabilization of BMX by IHMT-15137. The right panels show the results of the quantitative analysis of the BMX protein levels from the Western blots. e DARTS assay confirmation of the direct binding of IHMT-15137 to BMX by assessing the stability of BMX against pronase-mediated proteolysis in H446DDPR and H69AR cell lysates. f Inhibitory effects of IHMT-15137 and IHMT-15138 on BMX phosphorylation (Tyr566) in TEL-BaF3-BMX cells after 4 h of treatment, as determined by Western blotting. g Inhibitory effects of 12 h of IHMT-15137 treatment on BMX phosphorylation (Tyr566) and its downstream signaling pathways in H446DDPR and H69AR cells. h Molecular docking analysis of the irreversible binding mode of IHMT-15137 with BMX (PDB ID: 3SXR). i Effect of IHMT-15137 on Biotin-PEG2-C2-iodoacetamide labeling of BMX via a competitive biotin-iodoacetamide assay. Data were presented as mean ± SEM ( n = 3)

Journal: Signal Transduction and Targeted Therapy

Article Title: BMX inhibition overcomes small cell lung cancer chemoresistance by stabilizing E2F1 via ERK1/2-Cyclin D1/CDK4/6 axis

doi: 10.1038/s41392-026-02644-1

Figure Lengend Snippet: Characterization of IHMT-15137 as a potent and selective BMX inhibitor. a Chemical structure of IHMT-15137 and its reversible analog IHMT-15138. b Determination of the IC 50 values of IHMT-15137, IHMT-15138 and ibrutinib against the BMX protein via the ADP-Glo kinase assay. c Anti-proliferative activity of IHMT-15137, IHMT-15138 and ibrutinib against TEL-BaF3-BMX cells determined by the CTG assay. d CETSA analysis of the effects of IHMT-15137 on BMX protein stability in H446DDPR and H69AR cell lysates: temperature- and dose-dependent stabilization of BMX by IHMT-15137. The right panels show the results of the quantitative analysis of the BMX protein levels from the Western blots. e DARTS assay confirmation of the direct binding of IHMT-15137 to BMX by assessing the stability of BMX against pronase-mediated proteolysis in H446DDPR and H69AR cell lysates. f Inhibitory effects of IHMT-15137 and IHMT-15138 on BMX phosphorylation (Tyr566) in TEL-BaF3-BMX cells after 4 h of treatment, as determined by Western blotting. g Inhibitory effects of 12 h of IHMT-15137 treatment on BMX phosphorylation (Tyr566) and its downstream signaling pathways in H446DDPR and H69AR cells. h Molecular docking analysis of the irreversible binding mode of IHMT-15137 with BMX (PDB ID: 3SXR). i Effect of IHMT-15137 on Biotin-PEG2-C2-iodoacetamide labeling of BMX via a competitive biotin-iodoacetamide assay. Data were presented as mean ± SEM ( n = 3)

Article Snippet: Subsequently, the samples were incubated with 8 mM Biotin‐PEG2‐C2‐iodoacetamide (TargetMol, Shanghai, China; Cat. No. T17565 ) for 4 h at room temperature in the dark.

Techniques: Kinase Assay, Activity Assay, CTG Assay, Western Blot, Binding Assay, Phospho-proteomics, Protein-Protein interactions, Labeling