snap surface alexa fluor 647  (New England Biolabs)


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    Name:
    SNAP Surface Alexa Fluor 647
    Description:
    SNAP Surface Alexa Fluor 647 50 nmol
    Catalog Number:
    S9136S
    Price:
    380
    Category:
    Fluorochromes
    Size:
    50 nmol
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    Structured Review

    New England Biolabs snap surface alexa fluor 647
    SNAP Surface Alexa Fluor 647
    SNAP Surface Alexa Fluor 647 50 nmol
    https://www.bioz.com/result/snap surface alexa fluor 647/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    snap surface alexa fluor 647 - by Bioz Stars, 2021-09
    95/100 stars

    Images

    1) Product Images from "Correlative Light- and Electron Microscopy with chemical tags"

    Article Title: Correlative Light- and Electron Microscopy with chemical tags

    Journal: Journal of structural biology

    doi: 10.1016/j.jsb.2014.03.018

    Live-cell imaging and post-embedding fluorescence at different UA levels. (a, b) Live-cell imaging of L-cells stably expressing SNAPf-NCadherin labeled with Alexa Fluor 647. The cell–cell junctions are visualized in the red channel. The auto-fluorescence
    Figure Legend Snippet: Live-cell imaging and post-embedding fluorescence at different UA levels. (a, b) Live-cell imaging of L-cells stably expressing SNAPf-NCadherin labeled with Alexa Fluor 647. The cell–cell junctions are visualized in the red channel. The auto-fluorescence

    Techniques Used: Live Cell Imaging, Fluorescence, Stable Transfection, Expressing, Labeling

    ia-SEM CLEM of NCadherin in L-cells. (a) Fluorescence image of L-cells stably expressing SNAPf-NCadherin labeled with Alexa Fluor 647 after high-pressure freezing and freeze substitution with 2% UA. The box outlines the 32 μm × 17 μm
    Figure Legend Snippet: ia-SEM CLEM of NCadherin in L-cells. (a) Fluorescence image of L-cells stably expressing SNAPf-NCadherin labeled with Alexa Fluor 647 after high-pressure freezing and freeze substitution with 2% UA. The box outlines the 32 μm × 17 μm

    Techniques Used: IA, Fluorescence, Stable Transfection, Expressing, Labeling

    2) Product Images from "Super-resolution imaging reveals the nanoscale organization of metabotropic glutamate receptors at presynaptic active zones"

    Article Title: Super-resolution imaging reveals the nanoscale organization of metabotropic glutamate receptors at presynaptic active zones

    Journal: Science Advances

    doi: 10.1126/sciadv.aay7193

    Analysis of mGluR4 stoichiometry by single-molecule microscopy. ( A ) Schematic view of the mGluR4 construct carrying an N-terminal SNAP-tag (SNAP-mGluR4), which was used for the analysis. The construct was transiently expressed in CHO cells at low densities, corresponding to 0.45 ± 0.08 (SD) fluorescently labeled mGluR4s/μm 2 , and labeled at 1:1 stoichiometry with a saturating concentration of an Alexa Fluor 647 benzylguanine derivative, which binds covalently and irreversibly to the SNAP-tag. Cells were sequentially fixed and imaged by TIRF microscopy. ( B ) Representative TIRF image of a fixed CHO cell expressing the SNAP-mGluR4 construct. Dots represent individual receptor particles, which were identified with an automated single-particle detection algorithm. ( C ) Representative distribution of the intensity of mGluR4 particles in a cell expressing the SNAP-mGluR4 construct. Data were fitted with a mixed Gaussian model. The result of a mixed Gaussian fitting after partial photobleaching (dotted black line) was used to precisely estimate the intensity of single fluorophores in each image sequence. a.u., arbitrary units. ( D ) Relative abundance of monomers, dimers, and higher-order oligomers or nanoclusters detected by the analysis. Data are means ± SEM of 11 cells from three independent experiments (12,012 particles). ( E ) Estimation of the number of primary antibodies binding to one mGluR4. CHO cells transiently transfected to express wild-type mGluR4 at low densities—0.55 ± 0.07 (SD) fluorescently labeled mGluR4s/μm 2 —were incubated with either a limiting dilution (1:10 6 ) or a saturating concentration (1:100) of the primary antibody against mGluR4 and labeled with an Alexa Fluor 647–conjugated secondary antibody. Cells were then imaged and analyzed as in (B) and (C). Representative images and results of 20 (17,257) and 22 (13,553) cells from three independent experiments, respectively (number of particles in brackets), are shown.
    Figure Legend Snippet: Analysis of mGluR4 stoichiometry by single-molecule microscopy. ( A ) Schematic view of the mGluR4 construct carrying an N-terminal SNAP-tag (SNAP-mGluR4), which was used for the analysis. The construct was transiently expressed in CHO cells at low densities, corresponding to 0.45 ± 0.08 (SD) fluorescently labeled mGluR4s/μm 2 , and labeled at 1:1 stoichiometry with a saturating concentration of an Alexa Fluor 647 benzylguanine derivative, which binds covalently and irreversibly to the SNAP-tag. Cells were sequentially fixed and imaged by TIRF microscopy. ( B ) Representative TIRF image of a fixed CHO cell expressing the SNAP-mGluR4 construct. Dots represent individual receptor particles, which were identified with an automated single-particle detection algorithm. ( C ) Representative distribution of the intensity of mGluR4 particles in a cell expressing the SNAP-mGluR4 construct. Data were fitted with a mixed Gaussian model. The result of a mixed Gaussian fitting after partial photobleaching (dotted black line) was used to precisely estimate the intensity of single fluorophores in each image sequence. a.u., arbitrary units. ( D ) Relative abundance of monomers, dimers, and higher-order oligomers or nanoclusters detected by the analysis. Data are means ± SEM of 11 cells from three independent experiments (12,012 particles). ( E ) Estimation of the number of primary antibodies binding to one mGluR4. CHO cells transiently transfected to express wild-type mGluR4 at low densities—0.55 ± 0.07 (SD) fluorescently labeled mGluR4s/μm 2 —were incubated with either a limiting dilution (1:10 6 ) or a saturating concentration (1:100) of the primary antibody against mGluR4 and labeled with an Alexa Fluor 647–conjugated secondary antibody. Cells were then imaged and analyzed as in (B) and (C). Representative images and results of 20 (17,257) and 22 (13,553) cells from three independent experiments, respectively (number of particles in brackets), are shown.

    Techniques Used: Microscopy, Construct, Labeling, Concentration Assay, Expressing, Sequencing, Binding Assay, Transfection, Incubation

    3) Product Images from "Cell specific photoswitchable agonist for reversible control of endogenous dopamine receptors"

    Article Title: Cell specific photoswitchable agonist for reversible control of endogenous dopamine receptors

    Journal: Nature Communications

    doi: 10.1038/s41467-021-25003-w

    Activation of D1Rs in MSNs of the DMS with MP-D1 ago enhances movement. A D1R and its close homolog D5R are widely expressed in the brain (left panel) and are present in multiple cell types in the dorsal striatum (dStr; right panel). D1R is also expressed in the terminals of some glutamatergic afferents that innervate the striatum. DMS-dMSN D1Rs were selectively targeted with MP-D1 ago (red), which is composed of the membrane-anchor M EAAAK:ERE and P-D1 ago . B The M was virally delivered to DMS-dMSNs. Its expression (red = HA-tag staining) can be seen within the dStr. P-D1 ago and light were delivered the dStr with a reversible infusion/optical cannula. grey bar = 100 µm. blue = DAPI staining. Representative of brains from n = 7 mice. C The M is present at the surface of dStr-dMSNs according to its ability to bind the impermeant SNAP-tag binding dye SNAP-Surface Alexa Fluor 647. Labeling was not observed in the absence of the M or dye. mVenus (green) is an indicator of viral infection. grey bars = 50 µM. Representative of brains from n = 3 mice. D D1-Cre mice injected with an AAV encoding mVenus or the M and mVenus received bilateral dStr-infusions (1 µL) of either vehicle or the inactive form of P-D1 ago (cis; 100 µM) three hours prior to being placed in an open field. Locomotor activity of MP-D1 ago mice was measured in an open field. UV light and blue light were delivered to both sides of the brain. E The speed of mice with MP-D1 ago in dStr-dMSNs increased in response to a brief flash (450 nm, ~6 mW, 1 s) of blue light and returned to baseline after a brief flash (375 nm, ~9 mW, 1 s) of UV light. The behavioral response was not observed in mice lacking the M and/or P-D1 ago (400 nL infusion in each hemisphere). F The speed of each mouse was averaged over the following two-minute periods: (i) just before exposure to blue light ( UV pre ), (ii) three minutes after exposure to blue light ( blue ), (iii) and one minute after exposure to the second flash of UV light ( UV post ). See Supplementary Fig. 15a for more detail. Shown is a summary of the speed of - M or + M mice treated with vehicle or P-D1 ago mice during the UV pre , blue , and UV post periods. RM one-way ANOVA, F-values from left to right: 0.2, 0.4, 0.1, 15.4, Bonferroni, * p
    Figure Legend Snippet: Activation of D1Rs in MSNs of the DMS with MP-D1 ago enhances movement. A D1R and its close homolog D5R are widely expressed in the brain (left panel) and are present in multiple cell types in the dorsal striatum (dStr; right panel). D1R is also expressed in the terminals of some glutamatergic afferents that innervate the striatum. DMS-dMSN D1Rs were selectively targeted with MP-D1 ago (red), which is composed of the membrane-anchor M EAAAK:ERE and P-D1 ago . B The M was virally delivered to DMS-dMSNs. Its expression (red = HA-tag staining) can be seen within the dStr. P-D1 ago and light were delivered the dStr with a reversible infusion/optical cannula. grey bar = 100 µm. blue = DAPI staining. Representative of brains from n = 7 mice. C The M is present at the surface of dStr-dMSNs according to its ability to bind the impermeant SNAP-tag binding dye SNAP-Surface Alexa Fluor 647. Labeling was not observed in the absence of the M or dye. mVenus (green) is an indicator of viral infection. grey bars = 50 µM. Representative of brains from n = 3 mice. D D1-Cre mice injected with an AAV encoding mVenus or the M and mVenus received bilateral dStr-infusions (1 µL) of either vehicle or the inactive form of P-D1 ago (cis; 100 µM) three hours prior to being placed in an open field. Locomotor activity of MP-D1 ago mice was measured in an open field. UV light and blue light were delivered to both sides of the brain. E The speed of mice with MP-D1 ago in dStr-dMSNs increased in response to a brief flash (450 nm, ~6 mW, 1 s) of blue light and returned to baseline after a brief flash (375 nm, ~9 mW, 1 s) of UV light. The behavioral response was not observed in mice lacking the M and/or P-D1 ago (400 nL infusion in each hemisphere). F The speed of each mouse was averaged over the following two-minute periods: (i) just before exposure to blue light ( UV pre ), (ii) three minutes after exposure to blue light ( blue ), (iii) and one minute after exposure to the second flash of UV light ( UV post ). See Supplementary Fig. 15a for more detail. Shown is a summary of the speed of - M or + M mice treated with vehicle or P-D1 ago mice during the UV pre , blue , and UV post periods. RM one-way ANOVA, F-values from left to right: 0.2, 0.4, 0.1, 15.4, Bonferroni, * p

    Techniques Used: Activation Assay, Expressing, Staining, Mouse Assay, Binding Assay, Labeling, Infection, Injection, Activity Assay

    4) Product Images from "Antigen-Induced Allosteric Changes in a Human IgG1 Fc Increase Low-Affinity Fcγ Receptor Binding"

    Article Title: Antigen-Induced Allosteric Changes in a Human IgG1 Fc Increase Low-Affinity Fcγ Receptor Binding

    Journal: Structure (London, England : 1993)

    doi: 10.1016/j.str.2020.03.001

    Single molecule analysis of FcγR-mAb interactions by fluorescence correlation spectroscopy. Fraction of FcγRs bound to monomeric mAbs alone or previously engaged with their specific antigens. FcγRs were labeled with Alexa-Fluor 647 and their coefficient of diffusion were first determined. Then the receptors were incubated with mAbs wt or LALA (respectively C11 Panels A-B, N5-i5 Panels C-D) alone (Blue bars with a diffusion coefficient of 45 um 2 /sec) or previously engaged in the binding to their specific antigens (FLSC) (Red bars with a diffusion coefficient of 34 um 2 .
    Figure Legend Snippet: Single molecule analysis of FcγR-mAb interactions by fluorescence correlation spectroscopy. Fraction of FcγRs bound to monomeric mAbs alone or previously engaged with their specific antigens. FcγRs were labeled with Alexa-Fluor 647 and their coefficient of diffusion were first determined. Then the receptors were incubated with mAbs wt or LALA (respectively C11 Panels A-B, N5-i5 Panels C-D) alone (Blue bars with a diffusion coefficient of 45 um 2 /sec) or previously engaged in the binding to their specific antigens (FLSC) (Red bars with a diffusion coefficient of 34 um 2 .

    Techniques Used: Fluorescence, Spectroscopy, Labeling, Diffusion-based Assay, Incubation, Binding Assay

    5) Product Images from "A peptide tag-specific nanobody enables high-quality labeling for dSTORM imaging"

    Article Title: A peptide tag-specific nanobody enables high-quality labeling for dSTORM imaging

    Journal: Nature Communications

    doi: 10.1038/s41467-018-03191-2

    Comparison and characterization of BC2-nanobody (BC2-Nb) formats for wide-field and dSTORM imaging. a Schematic illustration of the BC2-Nb dye-conjugation strategies. Monovalent and bivalent BC2-Nbs were either conjugated with Alexa Fluor 647 (AF647) via N-hydroxysuccinimide (NHS) ester (left panel) or linked to AF647 by enzymatic sortase coupling (right panel). Wide-field imaging of chemically fixed HeLa cells expressing mCherry-vimentin BC2T (mCherry-VIM BC2T ) stained with modified BC2-Nbs. Monovalent versions of the BC2-Nbs (NHS- and sortase-coupled) are depicted on the left panel, corresponding bivBC2-Nbs are displayed on the right side. Stainings with NHS-conjugated nanobodies are shown in two different image contrasts, the upper half in the same brightness and contrast as the sortase-coupled nanobodies; in the lower half with an adjusted contrast. Scale bars, 25 µm. b Representative dSTORM images of chemically fixed HeLa cells expressing vimentin BC2T , stained with the monomeric NHS-conjugated BC2-Nb AF647 (NHS) (left) and the sortase-coupled bivBC2-Nb AF647 (sort) (right). Scale bars, images 5 µm, insets 1 µm. Image reconstruction details are given in Methods section. c Assessment of staining quality in wide-field fluorescence imaging. Labeling of the different nanobody formats was quantified by calculating the ratio of the signal intensity of mCherry-VIM BC2T expressing cells to non-transfected cells (background), (BC2-Nb AF647 (NHS) : n = 115; bivBC2-Nb AF647 (NHS) : n = 134; BC2-Nb AF647 (sort) : n = 150; bivBC2-Nb AF647 (sort) : n ). d Assessment of bivBC2-Nb AF647 staining of endogenous β-catenin. Bar chart summarizes measured nanobody per µm 2 values for untransfected chemically fixed HeLa cells stained with GFP-Nb AF647 or bivBC2-Nb AF647 in comparison to chemically fixed HeLa cells transiently expressing BC2T LC3B stained with bivBC2-Nb AF647 , errors given as standard deviation (S.D.), N ). e )
    Figure Legend Snippet: Comparison and characterization of BC2-nanobody (BC2-Nb) formats for wide-field and dSTORM imaging. a Schematic illustration of the BC2-Nb dye-conjugation strategies. Monovalent and bivalent BC2-Nbs were either conjugated with Alexa Fluor 647 (AF647) via N-hydroxysuccinimide (NHS) ester (left panel) or linked to AF647 by enzymatic sortase coupling (right panel). Wide-field imaging of chemically fixed HeLa cells expressing mCherry-vimentin BC2T (mCherry-VIM BC2T ) stained with modified BC2-Nbs. Monovalent versions of the BC2-Nbs (NHS- and sortase-coupled) are depicted on the left panel, corresponding bivBC2-Nbs are displayed on the right side. Stainings with NHS-conjugated nanobodies are shown in two different image contrasts, the upper half in the same brightness and contrast as the sortase-coupled nanobodies; in the lower half with an adjusted contrast. Scale bars, 25 µm. b Representative dSTORM images of chemically fixed HeLa cells expressing vimentin BC2T , stained with the monomeric NHS-conjugated BC2-Nb AF647 (NHS) (left) and the sortase-coupled bivBC2-Nb AF647 (sort) (right). Scale bars, images 5 µm, insets 1 µm. Image reconstruction details are given in Methods section. c Assessment of staining quality in wide-field fluorescence imaging. Labeling of the different nanobody formats was quantified by calculating the ratio of the signal intensity of mCherry-VIM BC2T expressing cells to non-transfected cells (background), (BC2-Nb AF647 (NHS) : n = 115; bivBC2-Nb AF647 (NHS) : n = 134; BC2-Nb AF647 (sort) : n = 150; bivBC2-Nb AF647 (sort) : n ). d Assessment of bivBC2-Nb AF647 staining of endogenous β-catenin. Bar chart summarizes measured nanobody per µm 2 values for untransfected chemically fixed HeLa cells stained with GFP-Nb AF647 or bivBC2-Nb AF647 in comparison to chemically fixed HeLa cells transiently expressing BC2T LC3B stained with bivBC2-Nb AF647 , errors given as standard deviation (S.D.), N ). e )

    Techniques Used: Imaging, Conjugation Assay, Expressing, Staining, Modification, Fluorescence, Labeling, Transfection, Standard Deviation

    6) Product Images from "Correlative Light- and Electron Microscopy with chemical tags"

    Article Title: Correlative Light- and Electron Microscopy with chemical tags

    Journal: Journal of structural biology

    doi: 10.1016/j.jsb.2014.03.018

    Live-cell imaging and post-embedding fluorescence at different UA levels. (a, b) Live-cell imaging of L-cells stably expressing SNAPf-NCadherin labeled with Alexa Fluor 647. The cell–cell junctions are visualized in the red channel. The auto-fluorescence
    Figure Legend Snippet: Live-cell imaging and post-embedding fluorescence at different UA levels. (a, b) Live-cell imaging of L-cells stably expressing SNAPf-NCadherin labeled with Alexa Fluor 647. The cell–cell junctions are visualized in the red channel. The auto-fluorescence

    Techniques Used: Live Cell Imaging, Fluorescence, Stable Transfection, Expressing, Labeling

    ia-SEM CLEM of NCadherin in L-cells. (a) Fluorescence image of L-cells stably expressing SNAPf-NCadherin labeled with Alexa Fluor 647 after high-pressure freezing and freeze substitution with 2% UA. The box outlines the 32 μm × 17 μm
    Figure Legend Snippet: ia-SEM CLEM of NCadherin in L-cells. (a) Fluorescence image of L-cells stably expressing SNAPf-NCadherin labeled with Alexa Fluor 647 after high-pressure freezing and freeze substitution with 2% UA. The box outlines the 32 μm × 17 μm

    Techniques Used: IA, Fluorescence, Stable Transfection, Expressing, Labeling

    Related Articles

    other:

    Article Title: Subtype selective fluorescent ligands based on ICI 118,551 to study the human β2‐adrenoceptor in CRISPR/Cas9 genome‐edited HEK293T cells at low expression levels
    Article Snippet: SNAP‐Surface®, Alexa Fluor® 488 and Alexa Fluor 647 were obtained from New England Biolabs.

    Labeling:

    Article Title: Protective pan-ebolavirus combination therapy by two multifunctional human antibodies
    Article Snippet: .. The new cell line, designated EBOV GPkik-293FS eGFP CCR5-SNAP, expresses EBOV-Kikwit GP on the plasma membrane, eGFP in the cytoplasm and the SNAP-tag CCR5, which can be specifically labeled with SNAP-Surface AF647 (NEB), on the cell surface ( ). ..

    Incubation:

    Article Title: Dynamics of Ku and bacterial non-homologous end-joining characterized using single DNA molecule analysis
    Article Snippet: .. The fusion protein was functionalized with an Alexa-647 fluorophore by mixing 5 μM of protein and 10 μM SNAP-Surface® Alexa Fluor® 647 (NEB) in a total volume of 2 ml followed by incubation at room temperature for 3 h. The labelled protein was separated from non-reacted substrate by size exclusion chromatography using a Superdex 16/600 200 pg column (GE Healthcare), pre-equilibrated with Buffer B supplemented with 1 mM DTT. ..

    Article Title: GIPR antagonist antibodies conjugated to GLP-1 peptide are bispecific molecules that decrease weight in obese mice and monkeys
    Article Snippet: .. Briefly, cells were incubated with SNAP Surface-Alexa Fluor 647 substrate (New England Biolabs) for 30 minutes and washed to remove excess label. ..

    Article Title: Simple and versatile imaging of genomic loci in live mammalian cells and early pre-implantation embryos using CAS-LiveFISH
    Article Snippet: .. Fluorescent dCas9 labellingFor SNAP tag labelling, dCas9-SNAP protein samples were incubated with SNAP-Surface Alexa Fluor 647 (NEB S9136) at 37 °C for 30 min. For CLIP tag labelling, CLIP-Cell TMR star substrate or CLIP-Surface 488 substrate (NEB S9219 and S9232) was reacted with dCas9-CLIP proteins at 37 °C for 60 min. ..

    Size-exclusion Chromatography:

    Article Title: Dynamics of Ku and bacterial non-homologous end-joining characterized using single DNA molecule analysis
    Article Snippet: .. The fusion protein was functionalized with an Alexa-647 fluorophore by mixing 5 μM of protein and 10 μM SNAP-Surface® Alexa Fluor® 647 (NEB) in a total volume of 2 ml followed by incubation at room temperature for 3 h. The labelled protein was separated from non-reacted substrate by size exclusion chromatography using a Superdex 16/600 200 pg column (GE Healthcare), pre-equilibrated with Buffer B supplemented with 1 mM DTT. ..

    Cross-linking Immunoprecipitation:

    Article Title: Simple and versatile imaging of genomic loci in live mammalian cells and early pre-implantation embryos using CAS-LiveFISH
    Article Snippet: .. Fluorescent dCas9 labellingFor SNAP tag labelling, dCas9-SNAP protein samples were incubated with SNAP-Surface Alexa Fluor 647 (NEB S9136) at 37 °C for 30 min. For CLIP tag labelling, CLIP-Cell TMR star substrate or CLIP-Surface 488 substrate (NEB S9219 and S9232) was reacted with dCas9-CLIP proteins at 37 °C for 60 min. ..

    Mouse Assay:

    Article Title: Cell specific photoswitchable agonist for reversible control of endogenous dopamine receptors
    Article Snippet: .. In some cases, AAV-injected mice received a dStr-infusion of 100 µM SNAP-Surface Alexa Fluor 647 (400 nL per hemisphere; NEB) followed by intracardial perfusion 24–48 h later. ..

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  • 95
    New England Biolabs snap tag alexafluor 647
    Effect of Agonist Stimulation on Receptor Oligomerization (A) Schematic of experimental setup to investigate the effect of isoprenaline or VEGF 165 a on receptor oligomerization measured using NanoBRET. (B) Visualization of VEGFR2/β 2 -adrenoceptor oligomers by NanoBRET using a luminescence LV200 Olympus microscope. HEK293 cells were transiently co-transfected to express NLuc-tagged-VEGFR2 and SNAP-tagged β 2 -adrenoceptors. Sequential images were captured from unlabeled (top panels) or SNAP-surface <t>AF647-labeled</t> co-transfected cells (bottom panels). Sequential images were acquired by capturing DAPI channel, displayed in the left panels (donor detection; using a 438/24 nm emission filter, 5 s exposure time), followed by CY5 channel, displayed in the right panels (BRET-excited acceptor, using a 647 long-pass filter, 30 s exposure time). Scale bar represents 20 μm. (C and D) HEK293 cells were transiently transfected with 0.05 μg/well NLuc-VEGFR2 and 0.10 μg/well SNAP-β 2 -AR and treated for 1 h at 37°C with increasing concentrations of (C) VEGF 165 a or (D) isoprenaline. Bar C corresponds to untreated (control) condition. Data are means ± SEM from five separate experiments, each performed in quadruplicate. **p
    Snap Tag Alexafluor 647, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/snap tag alexafluor 647/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    snap tag alexafluor 647 - by Bioz Stars, 2021-09
    95/100 stars
      Buy from Supplier

    95
    New England Biolabs snap surface alexa fluor 647
    Fluorescent in-gel detection of <t>SNAP-TTC</t> labeled with different dyes. a SDS-PAGE of SNAP-TTC fusion protein labeled with SNAP-Surface® <t>Alexa</t> Fluor® 488 (2) or BG-647 (3), respectively. Fluorescence signals were visualized using the Maestro CRi in vivo imaging system with the appropriate filter set. b Coomassie-stained SDS gel from ( a ). The stained protein bands correspond to the measured fluorescence signals from ( a ). (1) prestained protein marker, broad range (NEB), (2) SNAP-TTC-SNAP-Surface® Alexa Fluor® 488, (3) SNAP-TTC-BG647, (4) uncoupled SNAP-TTC protein
    Snap Surface Alexa Fluor 647, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/snap surface alexa fluor 647/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    snap surface alexa fluor 647 - by Bioz Stars, 2021-09
    95/100 stars
      Buy from Supplier

    Image Search Results


    Effect of Agonist Stimulation on Receptor Oligomerization (A) Schematic of experimental setup to investigate the effect of isoprenaline or VEGF 165 a on receptor oligomerization measured using NanoBRET. (B) Visualization of VEGFR2/β 2 -adrenoceptor oligomers by NanoBRET using a luminescence LV200 Olympus microscope. HEK293 cells were transiently co-transfected to express NLuc-tagged-VEGFR2 and SNAP-tagged β 2 -adrenoceptors. Sequential images were captured from unlabeled (top panels) or SNAP-surface AF647-labeled co-transfected cells (bottom panels). Sequential images were acquired by capturing DAPI channel, displayed in the left panels (donor detection; using a 438/24 nm emission filter, 5 s exposure time), followed by CY5 channel, displayed in the right panels (BRET-excited acceptor, using a 647 long-pass filter, 30 s exposure time). Scale bar represents 20 μm. (C and D) HEK293 cells were transiently transfected with 0.05 μg/well NLuc-VEGFR2 and 0.10 μg/well SNAP-β 2 -AR and treated for 1 h at 37°C with increasing concentrations of (C) VEGF 165 a or (D) isoprenaline. Bar C corresponds to untreated (control) condition. Data are means ± SEM from five separate experiments, each performed in quadruplicate. **p

    Journal: Cell Chemical Biology

    Article Title: Complex Formation between VEGFR2 and the β2-Adrenoceptor

    doi: 10.1016/j.chembiol.2019.02.014

    Figure Lengend Snippet: Effect of Agonist Stimulation on Receptor Oligomerization (A) Schematic of experimental setup to investigate the effect of isoprenaline or VEGF 165 a on receptor oligomerization measured using NanoBRET. (B) Visualization of VEGFR2/β 2 -adrenoceptor oligomers by NanoBRET using a luminescence LV200 Olympus microscope. HEK293 cells were transiently co-transfected to express NLuc-tagged-VEGFR2 and SNAP-tagged β 2 -adrenoceptors. Sequential images were captured from unlabeled (top panels) or SNAP-surface AF647-labeled co-transfected cells (bottom panels). Sequential images were acquired by capturing DAPI channel, displayed in the left panels (donor detection; using a 438/24 nm emission filter, 5 s exposure time), followed by CY5 channel, displayed in the right panels (BRET-excited acceptor, using a 647 long-pass filter, 30 s exposure time). Scale bar represents 20 μm. (C and D) HEK293 cells were transiently transfected with 0.05 μg/well NLuc-VEGFR2 and 0.10 μg/well SNAP-β 2 -AR and treated for 1 h at 37°C with increasing concentrations of (C) VEGF 165 a or (D) isoprenaline. Bar C corresponds to untreated (control) condition. Data are means ± SEM from five separate experiments, each performed in quadruplicate. **p

    Article Snippet: SNAP-Tag® AlexaFluor 647 (AF647) and AlexaFluor 488 (AF488) were purchased from New England BioLabs (Massachusetts, USA).

    Techniques: Microscopy, Transfection, Labeling, Bioluminescence Resonance Energy Transfer

    Influence of Agonists on the Cellular Location of Receptors and on Complex Formation between β 2 -Adrenoceptors and β-Arrestin2 (A) Confocal imaging (Zeiss LSM 710) of HEK293 cells transiently co-transfected with 0.25 μg/well HaloTag- VEGFR2 and 0.25 μg/well SNAP-β 2 -AR cDNAs, under unstimulated conditions (vehicle) or after treatment with 10 μM isoprenaline or 10 nM VEGF 165 a ligands (30 min at 37°C). Data are representative of three individual experiments. Scale bar represents 20 μm. (B) Immunolabeling of early endosomes (anti-Rab 5 antibody labeling). HEK293 cells transiently co-transfected with 0.5 μg/well HaloTag-VEGFR2 (green) and 0.5 μg/well SNAP-β 2 -AR (red) cDNAs, under unstimulated conditions (vehicle) or after treatment with 10 μM isoprenaline or 10 nM VEGF 165 a (30 min at 37°C). Cells were fixed using 3% paraformaldehyde/PBS, permeabilized using Triton X-100 (0.025% in PBS) and Rab 5 endosomal compartments labeled (cyan). Cells were imaged using a LSM880 confocal microscope (Zeiss). Data are representative of three individual experiments. Scale bar represents 10 μm. (C) Structured illumination microscopy (SIM) super-resolution images of HEK293 cells transiently co-transfected with HaloTag-VEGFR2 (green) and SNAP-β 2 -AR (red; 3 μg total cDNA). Cells were incubated with vehicle, 10 μM isoprenaline or 10 nM VEGF 165 a (30 min at 37°C) before fixation and mounting onto microscope slides. Coverslips were imaged using a Zeiss ELYRA PS.1 microscope. Areas of co-localized HaloTag-VEGFR2 and SNAP-β 2 -AR-labeled receptors are shown in yellow. Scale bar represents 10 μm. (D and E) Summary of Pearson's correlation coefficients (D) obtained following co-localization analysis of SIM images of circular regions of interest (ROI) in HEK293 cells co-expressing HaloTag-VEGFR2 and SNAP-β 2 -AR. ROI were placed on areas of fluorescence either at the plasma membrane or intracellular regions of SIM images of HEK293 cells co-expressing HaloTag-VEGFR2 (green; HaloTag AF488 membrane impermeant label) and SNAP-β 2 -AR (red; SNAP AF647 membrane impermeant label). TetraSpeck microspheres (0.1-μm spectral beads stained with four fluorophores: 365/430 nm [blue], 505/515 nm [green], 560/580 nm [orange], and 660/680 nm [red]) were included in each experiment to allow X/Y/Z channel alignment correction in image processing. The Fiji (ImageJ) analysis program CoLoc2 was applied to these ROI (six ROIs for spectral bead images and 12–15 ROIs for all other conditions) and Pearson's correlation coefficients obtained. Values were averaged across all ROI and are expressed as means ± SEM. A Pearson correlation coefficient value of +1 implies a perfect co-occurrence of both green (HaloTag-VEGFR2) and red (SNAP-β 2 -AR) fluorophores. *p

    Journal: Cell Chemical Biology

    Article Title: Complex Formation between VEGFR2 and the β2-Adrenoceptor

    doi: 10.1016/j.chembiol.2019.02.014

    Figure Lengend Snippet: Influence of Agonists on the Cellular Location of Receptors and on Complex Formation between β 2 -Adrenoceptors and β-Arrestin2 (A) Confocal imaging (Zeiss LSM 710) of HEK293 cells transiently co-transfected with 0.25 μg/well HaloTag- VEGFR2 and 0.25 μg/well SNAP-β 2 -AR cDNAs, under unstimulated conditions (vehicle) or after treatment with 10 μM isoprenaline or 10 nM VEGF 165 a ligands (30 min at 37°C). Data are representative of three individual experiments. Scale bar represents 20 μm. (B) Immunolabeling of early endosomes (anti-Rab 5 antibody labeling). HEK293 cells transiently co-transfected with 0.5 μg/well HaloTag-VEGFR2 (green) and 0.5 μg/well SNAP-β 2 -AR (red) cDNAs, under unstimulated conditions (vehicle) or after treatment with 10 μM isoprenaline or 10 nM VEGF 165 a (30 min at 37°C). Cells were fixed using 3% paraformaldehyde/PBS, permeabilized using Triton X-100 (0.025% in PBS) and Rab 5 endosomal compartments labeled (cyan). Cells were imaged using a LSM880 confocal microscope (Zeiss). Data are representative of three individual experiments. Scale bar represents 10 μm. (C) Structured illumination microscopy (SIM) super-resolution images of HEK293 cells transiently co-transfected with HaloTag-VEGFR2 (green) and SNAP-β 2 -AR (red; 3 μg total cDNA). Cells were incubated with vehicle, 10 μM isoprenaline or 10 nM VEGF 165 a (30 min at 37°C) before fixation and mounting onto microscope slides. Coverslips were imaged using a Zeiss ELYRA PS.1 microscope. Areas of co-localized HaloTag-VEGFR2 and SNAP-β 2 -AR-labeled receptors are shown in yellow. Scale bar represents 10 μm. (D and E) Summary of Pearson's correlation coefficients (D) obtained following co-localization analysis of SIM images of circular regions of interest (ROI) in HEK293 cells co-expressing HaloTag-VEGFR2 and SNAP-β 2 -AR. ROI were placed on areas of fluorescence either at the plasma membrane or intracellular regions of SIM images of HEK293 cells co-expressing HaloTag-VEGFR2 (green; HaloTag AF488 membrane impermeant label) and SNAP-β 2 -AR (red; SNAP AF647 membrane impermeant label). TetraSpeck microspheres (0.1-μm spectral beads stained with four fluorophores: 365/430 nm [blue], 505/515 nm [green], 560/580 nm [orange], and 660/680 nm [red]) were included in each experiment to allow X/Y/Z channel alignment correction in image processing. The Fiji (ImageJ) analysis program CoLoc2 was applied to these ROI (six ROIs for spectral bead images and 12–15 ROIs for all other conditions) and Pearson's correlation coefficients obtained. Values were averaged across all ROI and are expressed as means ± SEM. A Pearson correlation coefficient value of +1 implies a perfect co-occurrence of both green (HaloTag-VEGFR2) and red (SNAP-β 2 -AR) fluorophores. *p

    Article Snippet: SNAP-Tag® AlexaFluor 647 (AF647) and AlexaFluor 488 (AF488) were purchased from New England BioLabs (Massachusetts, USA).

    Techniques: Imaging, Transfection, Immunolabeling, Antibody Labeling, Labeling, Microscopy, Incubation, Expressing, Fluorescence, Staining

    Live-cell imaging and post-embedding fluorescence at different UA levels. (a, b) Live-cell imaging of L-cells stably expressing SNAPf-NCadherin labeled with Alexa Fluor 647. The cell–cell junctions are visualized in the red channel. The auto-fluorescence

    Journal: Journal of structural biology

    Article Title: Correlative Light- and Electron Microscopy with chemical tags

    doi: 10.1016/j.jsb.2014.03.018

    Figure Lengend Snippet: Live-cell imaging and post-embedding fluorescence at different UA levels. (a, b) Live-cell imaging of L-cells stably expressing SNAPf-NCadherin labeled with Alexa Fluor 647. The cell–cell junctions are visualized in the red channel. The auto-fluorescence

    Article Snippet: For staining of HeLa cells, 3 μM SNAP-Cell TMR Star, 2 μM SNAP-Surface Alexa Fluor 647 (New England BioLabs), 3 μM SiR-SNAP ( ) and 50 μM HaloTag TMR Ligand (Promega) diluted in OptiMEM (Life Technologies) with 10% FBS were used.

    Techniques: Live Cell Imaging, Fluorescence, Stable Transfection, Expressing, Labeling

    ia-SEM CLEM of NCadherin in L-cells. (a) Fluorescence image of L-cells stably expressing SNAPf-NCadherin labeled with Alexa Fluor 647 after high-pressure freezing and freeze substitution with 2% UA. The box outlines the 32 μm × 17 μm

    Journal: Journal of structural biology

    Article Title: Correlative Light- and Electron Microscopy with chemical tags

    doi: 10.1016/j.jsb.2014.03.018

    Figure Lengend Snippet: ia-SEM CLEM of NCadherin in L-cells. (a) Fluorescence image of L-cells stably expressing SNAPf-NCadherin labeled with Alexa Fluor 647 after high-pressure freezing and freeze substitution with 2% UA. The box outlines the 32 μm × 17 μm

    Article Snippet: For staining of HeLa cells, 3 μM SNAP-Cell TMR Star, 2 μM SNAP-Surface Alexa Fluor 647 (New England BioLabs), 3 μM SiR-SNAP ( ) and 50 μM HaloTag TMR Ligand (Promega) diluted in OptiMEM (Life Technologies) with 10% FBS were used.

    Techniques: IA, Fluorescence, Stable Transfection, Expressing, Labeling

    Analysis of mGluR4 stoichiometry by single-molecule microscopy. ( A ) Schematic view of the mGluR4 construct carrying an N-terminal SNAP-tag (SNAP-mGluR4), which was used for the analysis. The construct was transiently expressed in CHO cells at low densities, corresponding to 0.45 ± 0.08 (SD) fluorescently labeled mGluR4s/μm 2 , and labeled at 1:1 stoichiometry with a saturating concentration of an Alexa Fluor 647 benzylguanine derivative, which binds covalently and irreversibly to the SNAP-tag. Cells were sequentially fixed and imaged by TIRF microscopy. ( B ) Representative TIRF image of a fixed CHO cell expressing the SNAP-mGluR4 construct. Dots represent individual receptor particles, which were identified with an automated single-particle detection algorithm. ( C ) Representative distribution of the intensity of mGluR4 particles in a cell expressing the SNAP-mGluR4 construct. Data were fitted with a mixed Gaussian model. The result of a mixed Gaussian fitting after partial photobleaching (dotted black line) was used to precisely estimate the intensity of single fluorophores in each image sequence. a.u., arbitrary units. ( D ) Relative abundance of monomers, dimers, and higher-order oligomers or nanoclusters detected by the analysis. Data are means ± SEM of 11 cells from three independent experiments (12,012 particles). ( E ) Estimation of the number of primary antibodies binding to one mGluR4. CHO cells transiently transfected to express wild-type mGluR4 at low densities—0.55 ± 0.07 (SD) fluorescently labeled mGluR4s/μm 2 —were incubated with either a limiting dilution (1:10 6 ) or a saturating concentration (1:100) of the primary antibody against mGluR4 and labeled with an Alexa Fluor 647–conjugated secondary antibody. Cells were then imaged and analyzed as in (B) and (C). Representative images and results of 20 (17,257) and 22 (13,553) cells from three independent experiments, respectively (number of particles in brackets), are shown.

    Journal: Science Advances

    Article Title: Super-resolution imaging reveals the nanoscale organization of metabotropic glutamate receptors at presynaptic active zones

    doi: 10.1126/sciadv.aay7193

    Figure Lengend Snippet: Analysis of mGluR4 stoichiometry by single-molecule microscopy. ( A ) Schematic view of the mGluR4 construct carrying an N-terminal SNAP-tag (SNAP-mGluR4), which was used for the analysis. The construct was transiently expressed in CHO cells at low densities, corresponding to 0.45 ± 0.08 (SD) fluorescently labeled mGluR4s/μm 2 , and labeled at 1:1 stoichiometry with a saturating concentration of an Alexa Fluor 647 benzylguanine derivative, which binds covalently and irreversibly to the SNAP-tag. Cells were sequentially fixed and imaged by TIRF microscopy. ( B ) Representative TIRF image of a fixed CHO cell expressing the SNAP-mGluR4 construct. Dots represent individual receptor particles, which were identified with an automated single-particle detection algorithm. ( C ) Representative distribution of the intensity of mGluR4 particles in a cell expressing the SNAP-mGluR4 construct. Data were fitted with a mixed Gaussian model. The result of a mixed Gaussian fitting after partial photobleaching (dotted black line) was used to precisely estimate the intensity of single fluorophores in each image sequence. a.u., arbitrary units. ( D ) Relative abundance of monomers, dimers, and higher-order oligomers or nanoclusters detected by the analysis. Data are means ± SEM of 11 cells from three independent experiments (12,012 particles). ( E ) Estimation of the number of primary antibodies binding to one mGluR4. CHO cells transiently transfected to express wild-type mGluR4 at low densities—0.55 ± 0.07 (SD) fluorescently labeled mGluR4s/μm 2 —were incubated with either a limiting dilution (1:10 6 ) or a saturating concentration (1:100) of the primary antibody against mGluR4 and labeled with an Alexa Fluor 647–conjugated secondary antibody. Cells were then imaged and analyzed as in (B) and (C). Representative images and results of 20 (17,257) and 22 (13,553) cells from three independent experiments, respectively (number of particles in brackets), are shown.

    Article Snippet: SNAP-Surface Alexa Fluor 647 was from New England Biolabs (Ipswich, MA, USA).

    Techniques: Microscopy, Construct, Labeling, Concentration Assay, Expressing, Sequencing, Binding Assay, Transfection, Incubation

    Fluorescent in-gel detection of SNAP-TTC labeled with different dyes. a SDS-PAGE of SNAP-TTC fusion protein labeled with SNAP-Surface® Alexa Fluor® 488 (2) or BG-647 (3), respectively. Fluorescence signals were visualized using the Maestro CRi in vivo imaging system with the appropriate filter set. b Coomassie-stained SDS gel from ( a ). The stained protein bands correspond to the measured fluorescence signals from ( a ). (1) prestained protein marker, broad range (NEB), (2) SNAP-TTC-SNAP-Surface® Alexa Fluor® 488, (3) SNAP-TTC-BG647, (4) uncoupled SNAP-TTC protein

    Journal: BMC Biotechnology

    Article Title: Novel fusion proteins for the antigen-specific staining and elimination of B cell receptor-positive cell populations demonstrated by a tetanus toxoid fragment C (TTC) model antigen

    doi: 10.1186/s12896-016-0249-x

    Figure Lengend Snippet: Fluorescent in-gel detection of SNAP-TTC labeled with different dyes. a SDS-PAGE of SNAP-TTC fusion protein labeled with SNAP-Surface® Alexa Fluor® 488 (2) or BG-647 (3), respectively. Fluorescence signals were visualized using the Maestro CRi in vivo imaging system with the appropriate filter set. b Coomassie-stained SDS gel from ( a ). The stained protein bands correspond to the measured fluorescence signals from ( a ). (1) prestained protein marker, broad range (NEB), (2) SNAP-TTC-SNAP-Surface® Alexa Fluor® 488, (3) SNAP-TTC-BG647, (4) uncoupled SNAP-TTC protein

    Article Snippet: Coupling SNAP-TTC to the fluorescent dye Purified SNAP-TTC was conjugated to the BG-modified fluorescent dyes SNAP-surface® Alexa Fluor® 647 (New England Biolabs, Frankfurt am Main, Germany; Catalogue number: S9136S) and SNAP-surface® Alexa Fluor® 488 (New England Biolabs; Catalogue number: S9129S) as previously described [ ].

    Techniques: Labeling, SDS Page, Fluorescence, In Vivo Imaging, Staining, SDS-Gel, Marker

    Binding analysis of recombinant TTC-based proteins to TTC-reactive hybridoma cells. Equimolar amounts (100 nM) of TTC ( c ) and TTC-ETA’ ( d ) were used for binding analysis to the TTC-reactive hybridoma cell line 5E4 ( a ) compared to the control hybridoma cell line 8.18-C5 ( b ). Detection of bound proteins was carried out using an Alexa Fluor® 488-coupled anti-His5 antibody. Staining with Alexa Fluor 488-coupled anti-His5 antibody ( b ) and unstained cells ( a ) served as controls. Binding analysis of 100 nM SNAP-TTC coupled to the SNAP-Surface® 647 fluorescence dye ( b ) to 5E4 hybridoma cells ( c ) and to the control hybridoma cell line 8.18-C5 ( d ). Unstained cells served as control ( a )

    Journal: BMC Biotechnology

    Article Title: Novel fusion proteins for the antigen-specific staining and elimination of B cell receptor-positive cell populations demonstrated by a tetanus toxoid fragment C (TTC) model antigen

    doi: 10.1186/s12896-016-0249-x

    Figure Lengend Snippet: Binding analysis of recombinant TTC-based proteins to TTC-reactive hybridoma cells. Equimolar amounts (100 nM) of TTC ( c ) and TTC-ETA’ ( d ) were used for binding analysis to the TTC-reactive hybridoma cell line 5E4 ( a ) compared to the control hybridoma cell line 8.18-C5 ( b ). Detection of bound proteins was carried out using an Alexa Fluor® 488-coupled anti-His5 antibody. Staining with Alexa Fluor 488-coupled anti-His5 antibody ( b ) and unstained cells ( a ) served as controls. Binding analysis of 100 nM SNAP-TTC coupled to the SNAP-Surface® 647 fluorescence dye ( b ) to 5E4 hybridoma cells ( c ) and to the control hybridoma cell line 8.18-C5 ( d ). Unstained cells served as control ( a )

    Article Snippet: Coupling SNAP-TTC to the fluorescent dye Purified SNAP-TTC was conjugated to the BG-modified fluorescent dyes SNAP-surface® Alexa Fluor® 647 (New England Biolabs, Frankfurt am Main, Germany; Catalogue number: S9136S) and SNAP-surface® Alexa Fluor® 488 (New England Biolabs; Catalogue number: S9129S) as previously described [ ].

    Techniques: Binding Assay, Recombinant, Staining, Fluorescence