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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: Modular photostable fluorescent DNA blocks dissect the effects of pathogenic mutant kinesin on collective transport
Article Snippet: .. Tubulin was purified from porcine brain as described.48 Tubulin was labeled with biotin-PEG2-NHS ester (Tokyo Chemical Industry, Tokyo, Japan) and AZDye647 NHS ester (Fluoroprobes, Scottsdale, AZ, USA) as described.49 To polymerize Taxol-stabilized microtubules labeled with biotin and AZDye647, 30 mM unlabeled tubulin, 1.5 mM biotin-labeled tubulin, and 1.5 mM AZDye647-labeled tubulin were mixed in BRB80 buffer (80 mM PIPES, 1 mM MgCl2, and 1 mM EGTA) supplemented with 1 mM GTP and incubated for 15 min at 37 C. Then, an equal amount of BRB80 supplemented with 40 mM Taxol was added and further incubated for more than 15 min. ..

Purification:

Article Title: Modular photostable fluorescent DNA blocks dissect the effects of pathogenic mutant kinesin on collective transport
Article Snippet: .. Tubulin was purified from porcine brain as described.48 Tubulin was labeled with biotin-PEG2-NHS ester (Tokyo Chemical Industry, Tokyo, Japan) and AZDye647 NHS ester (Fluoroprobes, Scottsdale, AZ, USA) as described.49 To polymerize Taxol-stabilized microtubules labeled with biotin and AZDye647, 30 mM unlabeled tubulin, 1.5 mM biotin-labeled tubulin, and 1.5 mM AZDye647-labeled tubulin were mixed in BRB80 buffer (80 mM PIPES, 1 mM MgCl2, and 1 mM EGTA) supplemented with 1 mM GTP and incubated for 15 min at 37 C. Then, an equal amount of BRB80 supplemented with 40 mM Taxol was added and further incubated for more than 15 min. ..

Article Title: A simple procedure for preparing biotinylated immunoglobulin M from hybridoma culture medium.
Article Snippet: We previously reported a chromatography system for purifying immunoglobulin M (IgM) using N,N,N′,N′-ethylenediaminetetrakis(methylenephosphonic acid)-modified zirconia particles that selectively absorb immunoglobulins.. Here, we report a simple procedure for preparing biotinylated IgM from hybridoma culture medium using this zirconia-based chromatography system.. The culture medium of an IgM-producing hybridoma cell line was used as the starting sample solution, and the IgM in the medium was concentrated and partially purified by zirconia chromatography.

Incubation:

Article Title: Modular photostable fluorescent DNA blocks dissect the effects of pathogenic mutant kinesin on collective transport
Article Snippet: .. Tubulin was purified from porcine brain as described.48 Tubulin was labeled with biotin-PEG2-NHS ester (Tokyo Chemical Industry, Tokyo, Japan) and AZDye647 NHS ester (Fluoroprobes, Scottsdale, AZ, USA) as described.49 To polymerize Taxol-stabilized microtubules labeled with biotin and AZDye647, 30 mM unlabeled tubulin, 1.5 mM biotin-labeled tubulin, and 1.5 mM AZDye647-labeled tubulin were mixed in BRB80 buffer (80 mM PIPES, 1 mM MgCl2, and 1 mM EGTA) supplemented with 1 mM GTP and incubated for 15 min at 37 C. Then, an equal amount of BRB80 supplemented with 40 mM Taxol was added and further incubated for more than 15 min. ..

other:

Article Title: Modular photostable fluorescent DNA blocks dissect the effects of pathogenic mutant kinesin on collective transport
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 .

Article Title: Peptide nucleic acid-immobilised paper combined with multiplex recombinase polymerase amplification for the ultrasensitive and rapid detection of rifampicin-resistant tuberculosis.
Article Snippet: Biotin-PEG2-amine (0.4 pmol in 0.2 μL of 0.05 M sodium carbonate buffer, pH 10; Tokyo Chemical Industry Co., Ltd., Japan) was immobilised in the control area, which is positioned at the top of the strip.

Article Title: Design of Remote-Controllable Diels-Alder Platform on Magnetic Nanoparticles via Layer-by-Layer Assembly for AC Magnetic Field-Triggered Drug Release.
Article Snippet: Diels−Alder chemistry was exploited to develop a remote-controllable drug release platform on magnetic nanoparticles (MNPs).. For this purpose, MNPs were decorated with anionic poly(styrenesulfonic acid-co-furfuryl methacrylate) (poly(SS-coFMA)) and cationic poly(allylamine hydrochloride) by layer-by-layer assembly.. The decorated MNPs successfully underwent DA reaction to produce covalent bonding between FMA (diene) and maleimide (dienophile)-terminated model drug.

Saline:

Article Title: A simple procedure for preparing biotinylated immunoglobulin M from hybridoma culture medium.
Article Snippet: We previously reported a chromatography system for purifying immunoglobulin M (IgM) using N,N,N′,N′-ethylenediaminetetrakis(methylenephosphonic acid)-modified zirconia particles that selectively absorb immunoglobulins.. Here, we report a simple procedure for preparing biotinylated IgM from hybridoma culture medium using this zirconia-based chromatography system.. The culture medium of an IgM-producing hybridoma cell line was used as the starting sample solution, and the IgM in the medium was concentrated and partially purified by zirconia chromatography.

Concentration Assay:

Article Title: A simple procedure for preparing biotinylated immunoglobulin M from hybridoma culture medium.
Article Snippet: We previously reported a chromatography system for purifying immunoglobulin M (IgM) using N,N,N′,N′-ethylenediaminetetrakis(methylenephosphonic acid)-modified zirconia particles that selectively absorb immunoglobulins.. Here, we report a simple procedure for preparing biotinylated IgM from hybridoma culture medium using this zirconia-based chromatography system.. The culture medium of an IgM-producing hybridoma cell line was used as the starting sample solution, and the IgM in the medium was concentrated and partially purified by zirconia chromatography.

Droplet Countercurrent Chromatography:

Article Title: Compound comprising self-immolative group and ligand-drug conjugate comprising same
Article Snippet: .. Compound Q-2a (Mal-PEG2-acid, CAS NO. 1374666-32-6, TCI, 100 mg, 0.388 mmol) was dissolved in MC (5 mL) under a nitrogen atmosphere at 0° C., and then NHS (49.2 mg, 0.427 mmol) and DCC (88.2 mg, 0.427 mmol) were added, and the mixture was stirred for 15 hours. ..



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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