oregon green 488 maleimide Search Results


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    Thermo Fisher oregon green488 maleimide
    Fluorescence anisotropy of LRP4488 or pYLRP4488 binding to Fe65. LRP4488 (●) or pYLRP4488 (■) conjugated to Oregon <t>Green</t> 488 <t>maleimide</t> (Invitrogen) was incubated with 0.1–100 μM Fe65 WW-PID1-PID2 236-662 (A) or 0.1–100 μM Fe65 WW-PID1 236-512 (B). Anisotropy values at each Fe65 concentration were determined using a DTX 880 Multimode Dectector Beckman Coulter plate reader with excitation filter at 485 nm and two emission filters at 535 nm equipped with polarizers. Data were fit with KaleidaGraph 4.0 software using a Michaelis-Menten curve fit. pYLRP4488 bound Fe65 WW-PID1-PID2 with K D = 48.3+/−7.3 μM and pYLRP4488 bound Fe65 WW-PID1 with K D = 66.7 +/− 6.2 μM.
    Oregon Green488 Maleimide, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 56 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher 2 7 difluorofluorescein maleimide
    Fluorescence anisotropy of LRP4488 or pYLRP4488 binding to Fe65. LRP4488 (●) or pYLRP4488 (■) conjugated to Oregon <t>Green</t> 488 <t>maleimide</t> (Invitrogen) was incubated with 0.1–100 μM Fe65 WW-PID1-PID2 236-662 (A) or 0.1–100 μM Fe65 WW-PID1 236-512 (B). Anisotropy values at each Fe65 concentration were determined using a DTX 880 Multimode Dectector Beckman Coulter plate reader with excitation filter at 485 nm and two emission filters at 535 nm equipped with polarizers. Data were fit with KaleidaGraph 4.0 software using a Michaelis-Menten curve fit. pYLRP4488 bound Fe65 WW-PID1-PID2 with K D = 48.3+/−7.3 μM and pYLRP4488 bound Fe65 WW-PID1 with K D = 66.7 +/− 6.2 μM.
    2 7 Difluorofluorescein Maleimide, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher tetramethylrhodamine conjugated transferrin
    Fluorescence anisotropy of LRP4488 or pYLRP4488 binding to Fe65. LRP4488 (●) or pYLRP4488 (■) conjugated to Oregon <t>Green</t> 488 <t>maleimide</t> (Invitrogen) was incubated with 0.1–100 μM Fe65 WW-PID1-PID2 236-662 (A) or 0.1–100 μM Fe65 WW-PID1 236-512 (B). Anisotropy values at each Fe65 concentration were determined using a DTX 880 Multimode Dectector Beckman Coulter plate reader with excitation filter at 485 nm and two emission filters at 535 nm equipped with polarizers. Data were fit with KaleidaGraph 4.0 software using a Michaelis-Menten curve fit. pYLRP4488 bound Fe65 WW-PID1-PID2 with K D = 48.3+/−7.3 μM and pYLRP4488 bound Fe65 WW-PID1 with K D = 66.7 +/− 6.2 μM.
    Tetramethylrhodamine Conjugated Transferrin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Fluorescence anisotropy of LRP4488 or pYLRP4488 binding to Fe65. LRP4488 (●) or pYLRP4488 (■) conjugated to Oregon Green 488 maleimide (Invitrogen) was incubated with 0.1–100 μM Fe65 WW-PID1-PID2 236-662 (A) or 0.1–100 μM Fe65 WW-PID1 236-512 (B). Anisotropy values at each Fe65 concentration were determined using a DTX 880 Multimode Dectector Beckman Coulter plate reader with excitation filter at 485 nm and two emission filters at 535 nm equipped with polarizers. Data were fit with KaleidaGraph 4.0 software using a Michaelis-Menten curve fit. pYLRP4488 bound Fe65 WW-PID1-PID2 with K D = 48.3+/−7.3 μM and pYLRP4488 bound Fe65 WW-PID1 with K D = 66.7 +/− 6.2 μM.

    Journal: Biochemistry

    Article Title: Protein Interactions between Fe65, the LDL receptor-related protein and the amyloid precursor protein

    doi: 10.1021/bi200508f

    Figure Lengend Snippet: Fluorescence anisotropy of LRP4488 or pYLRP4488 binding to Fe65. LRP4488 (●) or pYLRP4488 (■) conjugated to Oregon Green 488 maleimide (Invitrogen) was incubated with 0.1–100 μM Fe65 WW-PID1-PID2 236-662 (A) or 0.1–100 μM Fe65 WW-PID1 236-512 (B). Anisotropy values at each Fe65 concentration were determined using a DTX 880 Multimode Dectector Beckman Coulter plate reader with excitation filter at 485 nm and two emission filters at 535 nm equipped with polarizers. Data were fit with KaleidaGraph 4.0 software using a Michaelis-Menten curve fit. pYLRP4488 bound Fe65 WW-PID1-PID2 with K D = 48.3+/−7.3 μM and pYLRP4488 bound Fe65 WW-PID1 with K D = 66.7 +/− 6.2 μM.

    Article Snippet: To further establish the interaction between LRP-CT and Fe65, a truncated LRP-CT starting at position 4488 and ending at 4454 (LRP4488) was attached through an N-terminal cysteine to Oregon Green 488 maleimide (Invitrogen) and used in fluorescence anisotropy binding studies.

    Techniques: Fluorescence, Binding Assay, Incubation, Concentration Assay, Software

    Effect of AM9D treatment on metalloproteinase (MMP) expression in MDA-MB-231 cells . ( A ) Expression levels of MMP9 , MMP1 , MMP13 , MMP14 , MMP19 , and MMP21 , and BACT (ß-actin) mRNA in MDA-MB-231-transfected cells. MDA-MB-231 cells were transfected with Oregon Green 488-labeled DNAzymes, control DNAzyme or mock transfection reagents as described in Materials and methods. Positively transfected cells were identified by flow cytometry. Total RNA was isolated and MMP9 , MMP1 , MMP13 , MMP14 , MMP19 and MMP21 , and BACT (ß-actin) mRNA were amplified by reverse-transcription (RT)-PCR and the PCR products were subjected to agarose gel and visualized by ethidium bromide staining. Lane 1, AM9D; lane 2, control DNAzyme; lane 3, cells treated with DOTAP (N-[1-(2,3-Dioleoyloxy)]-N,N,N-trimethylammonium propane methylsulfate) transfection reagent only. ( B ) Gelatin zymography of culture media from transfected MDA-MB-231 cells. The cultured media from MDA-MB-231 cells transfected with AM9D (lane 1), control DNAzyme (lane 2), or treated with DOTAP alone (lane 3) were separated on 8% SDS polyacrylamide gel containing 1 mg/ml gelatin. ( C ) Histogram showing the percentage of carcinoma cells invading the ECMatrix™ matrigel matrix after treatment with AM9D compared to cells treated with control DNAzyme. Cells were transfected with Oregon Green 488 labeled-DNAzymes, sorted and cultured in a matrigel matrix invasion chamber as described in Materials and methods. * P

    Journal: Breast Cancer Research : BCR

    Article Title: Anti-matrix metalloproteinase-9 DNAzyme decreases tumor growth in the MMTV-PyMT mouse model of breast cancer

    doi: 10.1186/bcr3385

    Figure Lengend Snippet: Effect of AM9D treatment on metalloproteinase (MMP) expression in MDA-MB-231 cells . ( A ) Expression levels of MMP9 , MMP1 , MMP13 , MMP14 , MMP19 , and MMP21 , and BACT (ß-actin) mRNA in MDA-MB-231-transfected cells. MDA-MB-231 cells were transfected with Oregon Green 488-labeled DNAzymes, control DNAzyme or mock transfection reagents as described in Materials and methods. Positively transfected cells were identified by flow cytometry. Total RNA was isolated and MMP9 , MMP1 , MMP13 , MMP14 , MMP19 and MMP21 , and BACT (ß-actin) mRNA were amplified by reverse-transcription (RT)-PCR and the PCR products were subjected to agarose gel and visualized by ethidium bromide staining. Lane 1, AM9D; lane 2, control DNAzyme; lane 3, cells treated with DOTAP (N-[1-(2,3-Dioleoyloxy)]-N,N,N-trimethylammonium propane methylsulfate) transfection reagent only. ( B ) Gelatin zymography of culture media from transfected MDA-MB-231 cells. The cultured media from MDA-MB-231 cells transfected with AM9D (lane 1), control DNAzyme (lane 2), or treated with DOTAP alone (lane 3) were separated on 8% SDS polyacrylamide gel containing 1 mg/ml gelatin. ( C ) Histogram showing the percentage of carcinoma cells invading the ECMatrix™ matrigel matrix after treatment with AM9D compared to cells treated with control DNAzyme. Cells were transfected with Oregon Green 488 labeled-DNAzymes, sorted and cultured in a matrigel matrix invasion chamber as described in Materials and methods. * P

    Article Snippet: The cells were then serum-starved for 4 hours prior to transient transfection with Oregon Green™488-maleimide-labeled AM9D or control DNAzyme (24 μg) using Lipofectamine 2000 (Invitrogen).

    Techniques: Expressing, Multiple Displacement Amplification, Transfection, Labeling, Flow Cytometry, Cytometry, Isolation, Amplification, Reverse Transcription Polymerase Chain Reaction, Polymerase Chain Reaction, Agarose Gel Electrophoresis, Staining, Zymography, Cell Culture

    ATP-powered disassembly of SNAREs by NSF. A , schematic representation of bulk fluorescence-dequenching-based SNARE disassembly assay. Stars represent the fluorescent dye, Oregon Green 488. B , structure of the minimal neuronal SNARE complex (Protein Data Bank (PDB) 1N7S ) illustrating sites used for labeling with Oregon Green maleimide for the dequenching assay. Helices are colored using the scheme in panel A. Yellow spheres represent the cysteine residues used for labeling. C , SDS-PAGE gel of purified proteins used in this study. Proteins were suspended to 0.5 μg/μl in Laemmli sample buffer with DTT and either boiled (+) or not (−). 10 μl were loaded into each lane of an Any kD denaturing polyacrylamide gel (Bio-Rad). D , SDS-PAGE-based SNARE disassembly assay. E , fluorescence dequenching-based disassembly assay ( colored lines , left axis ). The black arrow indicates the addition of NSF at time 0. Red , typical disassembly assay. Yellow , same assay performed in the absence of α-SNAP. Green , disassembly assay performed in the presence of 10 m m EDTA. The blue curve shows a disassembly assay that was stopped at 40 s by the addition of 10 m m EDTA. For comparison, densitometry was performed on the gel in panel C and overlaid (black squares , right axis ). F , SNARE-dependent activation of NSF ATPase activity. Data shown are the average of three independent assays ± S.E. collected at 37 °C. Numbers shown above each bar represent the average rates. G , effect of ionic strength on ATP-driven SNARE disassembly by NSF. Black squares and blue squares , the effect of added NaCl on the disassembly rate ( black squares ) and SNARE-activated ATPase rate ( blue squares ) of NSF. For comparison, the effects of 100 and 200 m m KCl ( solid line ) and NaCH 3 COO ( dashed line ) on the disassembly rates are shown. All data shown are the average of triplicate assays with standard errors.

    Journal: The Journal of Biological Chemistry

    Article Title: Processive ATP-driven Substrate Disassembly by the N-Ethylmaleimide-sensitive Factor (NSF) Molecular Machine *

    doi: 10.1074/jbc.M113.476705

    Figure Lengend Snippet: ATP-powered disassembly of SNAREs by NSF. A , schematic representation of bulk fluorescence-dequenching-based SNARE disassembly assay. Stars represent the fluorescent dye, Oregon Green 488. B , structure of the minimal neuronal SNARE complex (Protein Data Bank (PDB) 1N7S ) illustrating sites used for labeling with Oregon Green maleimide for the dequenching assay. Helices are colored using the scheme in panel A. Yellow spheres represent the cysteine residues used for labeling. C , SDS-PAGE gel of purified proteins used in this study. Proteins were suspended to 0.5 μg/μl in Laemmli sample buffer with DTT and either boiled (+) or not (−). 10 μl were loaded into each lane of an Any kD denaturing polyacrylamide gel (Bio-Rad). D , SDS-PAGE-based SNARE disassembly assay. E , fluorescence dequenching-based disassembly assay ( colored lines , left axis ). The black arrow indicates the addition of NSF at time 0. Red , typical disassembly assay. Yellow , same assay performed in the absence of α-SNAP. Green , disassembly assay performed in the presence of 10 m m EDTA. The blue curve shows a disassembly assay that was stopped at 40 s by the addition of 10 m m EDTA. For comparison, densitometry was performed on the gel in panel C and overlaid (black squares , right axis ). F , SNARE-dependent activation of NSF ATPase activity. Data shown are the average of three independent assays ± S.E. collected at 37 °C. Numbers shown above each bar represent the average rates. G , effect of ionic strength on ATP-driven SNARE disassembly by NSF. Black squares and blue squares , the effect of added NaCl on the disassembly rate ( black squares ) and SNARE-activated ATPase rate ( blue squares ) of NSF. For comparison, the effects of 100 and 200 m m KCl ( solid line ) and NaCH 3 COO ( dashed line ) on the disassembly rates are shown. All data shown are the average of triplicate assays with standard errors.

    Article Snippet: SNAREs were co-expressed using the Duet expression system (Novagen), purified, and labeled with the self-quenching dye Oregon Green 488 maleimide (Invitrogen).

    Techniques: Fluorescence, Labeling, SDS Page, Purification, Activation Assay, Activity Assay