alexa fluor 488  (New England Biolabs)


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    Name:
    SNAP Surface Alexa Fluor 488
    Description:
    SNAP Surface Alexa Fluor 488 50 nmol
    Catalog Number:
    s9129s
    Price:
    380
    Size:
    50 nmol
    Category:
    Fluorochromes
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    Structured Review

    New England Biolabs alexa fluor 488
    SNAP Surface Alexa Fluor 488
    SNAP Surface Alexa Fluor 488 50 nmol
    https://www.bioz.com/result/alexa fluor 488/product/New England Biolabs
    Average 98 stars, based on 66 article reviews
    Price from $9.99 to $1999.99
    alexa fluor 488 - by Bioz Stars, 2020-10
    98/100 stars

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    Images

    1) Product Images from "Emerin induces nuclear breakage in Xenopus extract and early embryos"

    Article Title: Emerin induces nuclear breakage in Xenopus extract and early embryos

    Journal: Molecular Biology of the Cell

    doi: 10.1091/mbc.E18-05-0277

    TRC40 rescues emerin’s nuclear localization. (A) Experiments were performed as in Figure 1 , except that the extract was supplemented with 1 µM DiI and 0.4 µM SNAP-emerin conjugated to Alexa Fluor 488. Representative images of small and large emerin puncta are shown. (B) Nuclei assembled in X. laevis egg extract as shown in Figure 1 were supplemented with 8 nM TRC40-EMD or an equivalent volume of dialysis buffer. After a 30-min incubation, nuclei were fixed, spun down onto coverslips, and stained with an anti-emerin antibody and Hoechst. Emerin images were acquired with the same exposure time. Representative images are shown.
    Figure Legend Snippet: TRC40 rescues emerin’s nuclear localization. (A) Experiments were performed as in Figure 1 , except that the extract was supplemented with 1 µM DiI and 0.4 µM SNAP-emerin conjugated to Alexa Fluor 488. Representative images of small and large emerin puncta are shown. (B) Nuclei assembled in X. laevis egg extract as shown in Figure 1 were supplemented with 8 nM TRC40-EMD or an equivalent volume of dialysis buffer. After a 30-min incubation, nuclei were fixed, spun down onto coverslips, and stained with an anti-emerin antibody and Hoechst. Emerin images were acquired with the same exposure time. Representative images are shown.

    Techniques Used: Incubation, Staining

    2) Product Images from "Stoichiometric Analyses of Soluble CD4 to Native-like HIV-1 Envelope by Single-Molecule Fluorescence Spectroscopy"

    Article Title: Stoichiometric Analyses of Soluble CD4 to Native-like HIV-1 Envelope by Single-Molecule Fluorescence Spectroscopy

    Journal: Cell reports

    doi: 10.1016/j.celrep.2019.08.074

    Functional Characterization of the hu-sCD4-SNAP-tag Fusion Protein (A) Western blot showing the expression of SNAP-tagged sCD4 (sCD4-SNAP) in the supernatant from the 293FS-transfected cells. Bands corresponding to sCD4-SNAP fusion protein and untagged sCD4 were detected using anti-huCD4 antibody. L, molecular weight ladder; W, wash; E, elute; FT, flow through; H, harvest; sCD4, positive control at 75 and 150 ng concentration. (B) SDS-PAGE with Coomassie staining showing successful purification of sCD4-SNAP from transfected 293FS cells using CNBr-activated Sepharose conjugated with an anti-CD4 antibody. Samples are as described in (A). (C) FCS autocorrelation plots for sCD4-SNAP-A488 alone and in complex with monomeric gp120, SOSIP.664 (BG505), and SOSIP.664.D7 (BG505.D7) trimers are shown. (D) FCS binding of Alexa 647 labeled mAbs b12 and 17b to HIV-1 BaL virions with or without 100 μg/mL sCD4-SNAP. Data are presented as the mean of three experiments ± SEM. ***Average percentage binding is significantly (p
    Figure Legend Snippet: Functional Characterization of the hu-sCD4-SNAP-tag Fusion Protein (A) Western blot showing the expression of SNAP-tagged sCD4 (sCD4-SNAP) in the supernatant from the 293FS-transfected cells. Bands corresponding to sCD4-SNAP fusion protein and untagged sCD4 were detected using anti-huCD4 antibody. L, molecular weight ladder; W, wash; E, elute; FT, flow through; H, harvest; sCD4, positive control at 75 and 150 ng concentration. (B) SDS-PAGE with Coomassie staining showing successful purification of sCD4-SNAP from transfected 293FS cells using CNBr-activated Sepharose conjugated with an anti-CD4 antibody. Samples are as described in (A). (C) FCS autocorrelation plots for sCD4-SNAP-A488 alone and in complex with monomeric gp120, SOSIP.664 (BG505), and SOSIP.664.D7 (BG505.D7) trimers are shown. (D) FCS binding of Alexa 647 labeled mAbs b12 and 17b to HIV-1 BaL virions with or without 100 μg/mL sCD4-SNAP. Data are presented as the mean of three experiments ± SEM. ***Average percentage binding is significantly (p

    Techniques Used: Functional Assay, Western Blot, Expressing, Transfection, Molecular Weight, Flow Cytometry, Positive Control, Concentration Assay, SDS Page, Staining, Purification, Binding Assay, Labeling

    3) Product Images from "Emerin induces nuclear breakage in Xenopus extract and early embryos"

    Article Title: Emerin induces nuclear breakage in Xenopus extract and early embryos

    Journal: Molecular Biology of the Cell

    doi: 10.1091/mbc.E18-05-0277

    TRC40 rescues emerin’s nuclear localization. (A) Experiments were performed as in Figure 1 , except that the extract was supplemented with 1 µM DiI and 0.4 µM SNAP-emerin conjugated to Alexa Fluor 488. Representative images of small and large emerin puncta are shown. (B) Nuclei assembled in X. laevis egg extract as shown in Figure 1 were supplemented with 8 nM TRC40-EMD or an equivalent volume of dialysis buffer. After a 30-min incubation, nuclei were fixed, spun down onto coverslips, and stained with an anti-emerin antibody and Hoechst. Emerin images were acquired with the same exposure time. Representative images are shown.
    Figure Legend Snippet: TRC40 rescues emerin’s nuclear localization. (A) Experiments were performed as in Figure 1 , except that the extract was supplemented with 1 µM DiI and 0.4 µM SNAP-emerin conjugated to Alexa Fluor 488. Representative images of small and large emerin puncta are shown. (B) Nuclei assembled in X. laevis egg extract as shown in Figure 1 were supplemented with 8 nM TRC40-EMD or an equivalent volume of dialysis buffer. After a 30-min incubation, nuclei were fixed, spun down onto coverslips, and stained with an anti-emerin antibody and Hoechst. Emerin images were acquired with the same exposure time. Representative images are shown.

    Techniques Used: Incubation, Staining

    4) Product Images from "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"

    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

    Journal: BMC Biotechnology

    doi: 10.1186/s12896-016-0249-x

    Binding analysis of recombinant TTC and TTC-FITC on isolated PBMCs. Surface staining of CD27 + memory B cells ( a ) and intracellular staining of CD27 ++ CD38 ++ plasma cells ( c ) using recombinant TTC (10 nM) and anti-His5 Alexa Fluor 488 antibody (1:100). Surface staining of CD27 + memory B cells ( b ) and intracellular staining of CD27 ++ CD38 ++ plasma cells ( d ) using a FITC-coupled TTC peptide (1:25)
    Figure Legend Snippet: Binding analysis of recombinant TTC and TTC-FITC on isolated PBMCs. Surface staining of CD27 + memory B cells ( a ) and intracellular staining of CD27 ++ CD38 ++ plasma cells ( c ) using recombinant TTC (10 nM) and anti-His5 Alexa Fluor 488 antibody (1:100). Surface staining of CD27 + memory B cells ( b ) and intracellular staining of CD27 ++ CD38 ++ plasma cells ( d ) using a FITC-coupled TTC peptide (1:25)

    Techniques Used: Binding Assay, Recombinant, Isolation, Staining

    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
    Figure Legend 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

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

    Dose-dependent binding analysis of the recombinant fusion protein TTC-ETA’ on hybridoma cells. Various concentrations (1–400 nM) of TTC-ETA’ were used to determine a dose-dependent binding activity on TTC-reactive hybridoma cell line 5E4 ( a ) and to exclude specific binding to the control hybridoma cell line 8.18-C5 ( b ). The detection of bound protein was carried out by flow cytometry using a Penta-His Alexa Fluor 488 Conjugate antibody. Measurements were performed in triplicates (n = 3); error bars indicate SD. The recombinant TTC-ETA’ exhibits a dosedependent binding on the target hybridoma cell line 5E4, whereas no binding could be determined on the control hybridoma cell line 8.18-C5
    Figure Legend Snippet: Dose-dependent binding analysis of the recombinant fusion protein TTC-ETA’ on hybridoma cells. Various concentrations (1–400 nM) of TTC-ETA’ were used to determine a dose-dependent binding activity on TTC-reactive hybridoma cell line 5E4 ( a ) and to exclude specific binding to the control hybridoma cell line 8.18-C5 ( b ). The detection of bound protein was carried out by flow cytometry using a Penta-His Alexa Fluor 488 Conjugate antibody. Measurements were performed in triplicates (n = 3); error bars indicate SD. The recombinant TTC-ETA’ exhibits a dosedependent binding on the target hybridoma cell line 5E4, whereas no binding could be determined on the control hybridoma cell line 8.18-C5

    Techniques Used: Binding Assay, Recombinant, Activity Assay, Flow Cytometry, Cytometry

    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 )
    Figure Legend 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 )

    Techniques Used: Binding Assay, Recombinant, Staining, Fluorescence

    5) Product Images from "Myosin Va’s adaptor protein melanophilin enforces track selection on the microtubule and actin networks in vitro"

    Article Title: Myosin Va’s adaptor protein melanophilin enforces track selection on the microtubule and actin networks in vitro

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.1619473114

    Mlph’s phosphorylation state does not interfere substantially with actin binding. ( A ) Actin decoration experiments were performed with surface-immobilized and Atto488-labeled actin filaments (red). Filaments were incubated with the complex formed between Mlph and Alexa Fluor 647-labeled Rab27a (green). Dephosphorylated (Dephos; Left ) and the phosphorylated (Phos; Right ) Mlph decorated actin filaments similarly well. Removal of the C-terminal ABD of Mlph (Rab27a/Mlph ΔABD) abolished this interaction regardless of Mlph’s phosphorylation state. ( B ) The dephosphorylated, Alexa Fluor 488-labeled Rab27a/Mlph complex was mixed in equal amounts with the phosphorylated, Alexa Fluor 647-labeled Rab27a/Mlph complex and was incubated with surface-attached, Atto565-labeled actin filaments. The quantification of the actin-associated fluorescence signals from the respective PKA- and phosphatase-treated Rab27a/Mlph complexes showed that the phosphorylation state of Mlph did not substantially interfere with actin binding. Error bars represent SD. (Scale bars: 3 µm.)
    Figure Legend Snippet: Mlph’s phosphorylation state does not interfere substantially with actin binding. ( A ) Actin decoration experiments were performed with surface-immobilized and Atto488-labeled actin filaments (red). Filaments were incubated with the complex formed between Mlph and Alexa Fluor 647-labeled Rab27a (green). Dephosphorylated (Dephos; Left ) and the phosphorylated (Phos; Right ) Mlph decorated actin filaments similarly well. Removal of the C-terminal ABD of Mlph (Rab27a/Mlph ΔABD) abolished this interaction regardless of Mlph’s phosphorylation state. ( B ) The dephosphorylated, Alexa Fluor 488-labeled Rab27a/Mlph complex was mixed in equal amounts with the phosphorylated, Alexa Fluor 647-labeled Rab27a/Mlph complex and was incubated with surface-attached, Atto565-labeled actin filaments. The quantification of the actin-associated fluorescence signals from the respective PKA- and phosphatase-treated Rab27a/Mlph complexes showed that the phosphorylation state of Mlph did not substantially interfere with actin binding. Error bars represent SD. (Scale bars: 3 µm.)

    Techniques Used: Binding Assay, Labeling, Incubation, Fluorescence

    6) Product Images from "NEDD4 and NEDD4L regulate Wnt signalling and intestinal stem cell priming by degrading LGR5 receptor"

    Article Title: NEDD4 and NEDD4L regulate Wnt signalling and intestinal stem cell priming by degrading LGR5 receptor

    Journal: The EMBO Journal

    doi: 10.15252/embj.2019102771

    NEDD4 and NEDD4L selectively degrade Lgr4 and Lgr5 but not FZD receptors of Wnt signalling pathway HEK293T cells were transfected with empty vector (EV), LGR4‐Flag, MYC‐NEDD4 WT or C854S (CS) mutant, MYC‐NEDD4L wild‐type (WT) or C962A (CA) mutant, followed by Western blot analysis of the indicated antibodies. HEK293T cells were transfected with V5‐FZD4 (B) or V5‐FZD5 (C) with or without MYC‐NEDD4 or MYC‐NEDD4L or empty vector (EV) as control. Lysates were subjected to Western blotting using the indicated antibodies. Subcellular localisation of SNAP‐FZD5 in HEK293T cells co‐expressed with the indicated plasmids. Surface SNAP‐FZD5 was labelled with SNAP Alexa‐488 for 10 min. Scale bars, 10 µm. Quantitation of fluorescent intensity in total and surface LGR5 and FZD5 with the indicated transfections of NEDD4 and NEDD4L. Data are presented as percentage of fluorescence intensity compared to the EV control in triplicate for LGR5 and duplicate for FZD5. Error bars represent ± SEM. P ‐values were determined using the unpaired two‐sided t ‐test (* P
    Figure Legend Snippet: NEDD4 and NEDD4L selectively degrade Lgr4 and Lgr5 but not FZD receptors of Wnt signalling pathway HEK293T cells were transfected with empty vector (EV), LGR4‐Flag, MYC‐NEDD4 WT or C854S (CS) mutant, MYC‐NEDD4L wild‐type (WT) or C962A (CA) mutant, followed by Western blot analysis of the indicated antibodies. HEK293T cells were transfected with V5‐FZD4 (B) or V5‐FZD5 (C) with or without MYC‐NEDD4 or MYC‐NEDD4L or empty vector (EV) as control. Lysates were subjected to Western blotting using the indicated antibodies. Subcellular localisation of SNAP‐FZD5 in HEK293T cells co‐expressed with the indicated plasmids. Surface SNAP‐FZD5 was labelled with SNAP Alexa‐488 for 10 min. Scale bars, 10 µm. Quantitation of fluorescent intensity in total and surface LGR5 and FZD5 with the indicated transfections of NEDD4 and NEDD4L. Data are presented as percentage of fluorescence intensity compared to the EV control in triplicate for LGR5 and duplicate for FZD5. Error bars represent ± SEM. P ‐values were determined using the unpaired two‐sided t ‐test (* P

    Techniques Used: Transfection, Plasmid Preparation, Mutagenesis, Western Blot, Quantitation Assay, Fluorescence

    NEDD4 and NEDD4L target LGR5 receptor for lysosomal and proteasomal degradation HEK293T cells were transfected with empty vector (EV), LGR5‐Flag, MYC‐NEDD4 WT or C854S (CS) mutant, MYC‐NEDD4L wild‐type (WT) or C962A (CA) mutant, followed by Western blot analysis of the indicated antibodies. Black triangle indicates the mature glycosylated form of LGR5, while white triangle indicates the immature unprocessed form of LGR5. Subcellular localisation of SNAP‐Lgr5 in the absence or presence of Myc‐NEDD4‐WT, catalytically inactive HA‐NEDD4‐CS, Myc‐NEDD4L‐WT or catalytically inactive HA‐NEDD4L‐CA. Surface SNAP‐Lgr5 was labelled with SNAP Alexa‐488 for 10 min. Scale bar, 10 µm. HEK293T cells were transfected with constructs expressing LGR5‐Flag, HA‐Ubiquitin, EV, or the indicated NEDD4 (C) or NEDD4L (D) plasmids. Cells were treated with MG132 followed by anti‐Flag IP under denaturing conditions and Western blot analysis using the indicated antibodies. HEK293T control, NEDD4 or NEDD4L CRISPR‐mediated mutant cells were transfected with LGR5‐Flag and HA‐Ubiquitin. Cells were pre‐treated with MG132 followed by anti‐Flag IP and Western blot analysis using the indicated antibodies. Relative TOPFlash reporter activities of HEK293T cells and NEDD4 and NEDD4L CRISPR cell lines with the indicated siRNA constructs. Cells were treated with Wnt3a supplemented with RSPO‐conditioned media. Data represent mean ± standard error of at least three independent experiments. P ‐values were determined using the unpaired two‐sided t ‐test (* P
    Figure Legend Snippet: NEDD4 and NEDD4L target LGR5 receptor for lysosomal and proteasomal degradation HEK293T cells were transfected with empty vector (EV), LGR5‐Flag, MYC‐NEDD4 WT or C854S (CS) mutant, MYC‐NEDD4L wild‐type (WT) or C962A (CA) mutant, followed by Western blot analysis of the indicated antibodies. Black triangle indicates the mature glycosylated form of LGR5, while white triangle indicates the immature unprocessed form of LGR5. Subcellular localisation of SNAP‐Lgr5 in the absence or presence of Myc‐NEDD4‐WT, catalytically inactive HA‐NEDD4‐CS, Myc‐NEDD4L‐WT or catalytically inactive HA‐NEDD4L‐CA. Surface SNAP‐Lgr5 was labelled with SNAP Alexa‐488 for 10 min. Scale bar, 10 µm. HEK293T cells were transfected with constructs expressing LGR5‐Flag, HA‐Ubiquitin, EV, or the indicated NEDD4 (C) or NEDD4L (D) plasmids. Cells were treated with MG132 followed by anti‐Flag IP under denaturing conditions and Western blot analysis using the indicated antibodies. HEK293T control, NEDD4 or NEDD4L CRISPR‐mediated mutant cells were transfected with LGR5‐Flag and HA‐Ubiquitin. Cells were pre‐treated with MG132 followed by anti‐Flag IP and Western blot analysis using the indicated antibodies. Relative TOPFlash reporter activities of HEK293T cells and NEDD4 and NEDD4L CRISPR cell lines with the indicated siRNA constructs. Cells were treated with Wnt3a supplemented with RSPO‐conditioned media. Data represent mean ± standard error of at least three independent experiments. P ‐values were determined using the unpaired two‐sided t ‐test (* P

    Techniques Used: Transfection, Plasmid Preparation, Mutagenesis, Western Blot, Construct, Expressing, CRISPR

    Related Articles

    Transfection:

    Article Title: NEDD4 and NEDD4L regulate Wnt signalling and intestinal stem cell priming by degrading LGR5 receptor
    Article Snippet: .. After 24 h of transfection, cells were labelled with 1 μM SNAP‐Surface Alexa 488 (NEB) for 15 min at 4°C to block endocytosis. ..

    Incubation:

    Article Title: Super-assembly of ER-phagy receptor Atg40 induces local ER remodeling at contacts with forming autophagosomal membranes
    Article Snippet: .. Briefly, 200 μM proteins were incubated with 20 μM SNAP-Surface Alexa Fluor 488, 1 mM DTT, 20 mM HEPES pH 6.8, and 150 mM NaCl for 10 min in a light-blocked box at room temperature. ..

    Blocking Assay:

    Article Title: NEDD4 and NEDD4L regulate Wnt signalling and intestinal stem cell priming by degrading LGR5 receptor
    Article Snippet: .. After 24 h of transfection, cells were labelled with 1 μM SNAP‐Surface Alexa 488 (NEB) for 15 min at 4°C to block endocytosis. ..

    Purification:

    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
    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 [ ]. .. Briefly, 1 μg SNAP-TTC protein was mixed with 2 nmol BG-647 or BG-488 solution prepared from a 50 nmol stock and incubated for 1 h at room temperature.

    Generated:

    Article Title: Emerin induces nuclear breakage in Xenopus extract and early embryos
    Article Snippet: .. SNAP-emerin generated from pDL97 was labeled with Janelia Fluor 549 ( ) or Alexa Fluor 488 according to the manufacturer’s protocol (S9129, NEB). .. The TRC40-EMD complex was purified as previously described ( ).

    Labeling:

    Article Title: A direct role for SNX9 in the biogenesis of filopodia
    Article Snippet: .. Chemical labeling of proteins with fluorescent dyes SNAP-tagged TOCA-1 and SNX9 were labeled using SNAP-Surface Alexa Fluor 488 or Alexa Fluor 647 (New England Biolabs, S9129S, S9136S). .. 5–10 µM final concentration of protein was mixed with 10 µM SNAP-dye in a buffer containing 150 mM NaCl, 20 mM Na-Hepes, pH 7.4, 1 mM DTT, and 1% (vol/vol) TWEEN 20 and incubated under gentle rotation at 4°C overnight.

    Article Title: Emerin induces nuclear breakage in Xenopus extract and early embryos
    Article Snippet: .. SNAP-emerin generated from pDL97 was labeled with Janelia Fluor 549 ( ) or Alexa Fluor 488 according to the manufacturer’s protocol (S9129, NEB). .. The TRC40-EMD complex was purified as previously described ( ).

    Article Title: Stoichiometric Analyses of Soluble CD4 to Native-like HIV-1 Envelope by Single-Molecule Fluorescence Spectroscopy
    Article Snippet: .. 100 μM of sCD4-SNAP was then fluorescently labeled with a SNAP surface Alexa Fluor 488 labeling kit (NEB) and dialyzed against PBS as necessary. .. Microscope setup A customized confocal microscope (based on ISS Q2 laser scanning nanoscope) with single-molecule detection sensitivity was used for all recording and analyses.

    Staining:

    Article Title: Snorkel: An Epitope Tagging System for Measuring the Surface Expression of Membrane Proteins
    Article Snippet: .. For SNAP tag staining we used SNAP surface Alexa fluor 488 (NEB). .. All staining was in a final volume of 50 µl of 10% normal goat serum (heat inactivated, 30 minutes at 56o C) in PBS with 0.025% sodium azide and was performed at 2-8o C. After 30 minutes with gentle shaking cells were washed three times with cold 1% bovine serum albumin (BSA) in PBS with 0.025% sodium azide and analyzed.

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    • alexa fluor 488  (New England Biolabs)
    98
    New England Biolabs alexa fluor 488
    TRC40 rescues emerin’s nuclear localization. (A) Experiments were performed as in Figure 1 , except that the extract was supplemented with 1 µM DiI and 0.4 µM SNAP-emerin conjugated to <t>Alexa</t> Fluor 488. Representative images of small and large emerin puncta are shown. (B) Nuclei assembled in X. laevis egg extract as shown in Figure 1 were supplemented with 8 nM TRC40-EMD or an equivalent volume of dialysis buffer. After a 30-min incubation, nuclei were fixed, spun down onto coverslips, and stained with an anti-emerin antibody and Hoechst. Emerin images were acquired with the same exposure time. Representative images are shown.
    Alexa Fluor 488, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 98/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alexa fluor 488/product/New England Biolabs
    Average 98 stars, based on 23 article reviews
    Price from $9.99 to $1999.99
    alexa fluor 488 - by Bioz Stars, 2020-10
    98/100 stars
    		  Buy from Supplier

    Image Search Results


    TRC40 rescues emerin’s nuclear localization. (A) Experiments were performed as in Figure 1 , except that the extract was supplemented with 1 µM DiI and 0.4 µM SNAP-emerin conjugated to Alexa Fluor 488. Representative images of small and large emerin puncta are shown. (B) Nuclei assembled in X. laevis egg extract as shown in Figure 1 were supplemented with 8 nM TRC40-EMD or an equivalent volume of dialysis buffer. After a 30-min incubation, nuclei were fixed, spun down onto coverslips, and stained with an anti-emerin antibody and Hoechst. Emerin images were acquired with the same exposure time. Representative images are shown.

    Journal: Molecular Biology of the Cell

    Article Title: Emerin induces nuclear breakage in Xenopus extract and early embryos

    doi: 10.1091/mbc.E18-05-0277

    Figure Lengend Snippet: TRC40 rescues emerin’s nuclear localization. (A) Experiments were performed as in Figure 1 , except that the extract was supplemented with 1 µM DiI and 0.4 µM SNAP-emerin conjugated to Alexa Fluor 488. Representative images of small and large emerin puncta are shown. (B) Nuclei assembled in X. laevis egg extract as shown in Figure 1 were supplemented with 8 nM TRC40-EMD or an equivalent volume of dialysis buffer. After a 30-min incubation, nuclei were fixed, spun down onto coverslips, and stained with an anti-emerin antibody and Hoechst. Emerin images were acquired with the same exposure time. Representative images are shown.

    Article Snippet: SNAP-emerin generated from pDL97 was labeled with Janelia Fluor 549 ( ) or Alexa Fluor 488 according to the manufacturer’s protocol (S9129, NEB).

    Techniques: Incubation, Staining

    Functional Characterization of the hu-sCD4-SNAP-tag Fusion Protein (A) Western blot showing the expression of SNAP-tagged sCD4 (sCD4-SNAP) in the supernatant from the 293FS-transfected cells. Bands corresponding to sCD4-SNAP fusion protein and untagged sCD4 were detected using anti-huCD4 antibody. L, molecular weight ladder; W, wash; E, elute; FT, flow through; H, harvest; sCD4, positive control at 75 and 150 ng concentration. (B) SDS-PAGE with Coomassie staining showing successful purification of sCD4-SNAP from transfected 293FS cells using CNBr-activated Sepharose conjugated with an anti-CD4 antibody. Samples are as described in (A). (C) FCS autocorrelation plots for sCD4-SNAP-A488 alone and in complex with monomeric gp120, SOSIP.664 (BG505), and SOSIP.664.D7 (BG505.D7) trimers are shown. (D) FCS binding of Alexa 647 labeled mAbs b12 and 17b to HIV-1 BaL virions with or without 100 μg/mL sCD4-SNAP. Data are presented as the mean of three experiments ± SEM. ***Average percentage binding is significantly (p

    Journal: Cell reports

    Article Title: Stoichiometric Analyses of Soluble CD4 to Native-like HIV-1 Envelope by Single-Molecule Fluorescence Spectroscopy

    doi: 10.1016/j.celrep.2019.08.074

    Figure Lengend Snippet: Functional Characterization of the hu-sCD4-SNAP-tag Fusion Protein (A) Western blot showing the expression of SNAP-tagged sCD4 (sCD4-SNAP) in the supernatant from the 293FS-transfected cells. Bands corresponding to sCD4-SNAP fusion protein and untagged sCD4 were detected using anti-huCD4 antibody. L, molecular weight ladder; W, wash; E, elute; FT, flow through; H, harvest; sCD4, positive control at 75 and 150 ng concentration. (B) SDS-PAGE with Coomassie staining showing successful purification of sCD4-SNAP from transfected 293FS cells using CNBr-activated Sepharose conjugated with an anti-CD4 antibody. Samples are as described in (A). (C) FCS autocorrelation plots for sCD4-SNAP-A488 alone and in complex with monomeric gp120, SOSIP.664 (BG505), and SOSIP.664.D7 (BG505.D7) trimers are shown. (D) FCS binding of Alexa 647 labeled mAbs b12 and 17b to HIV-1 BaL virions with or without 100 μg/mL sCD4-SNAP. Data are presented as the mean of three experiments ± SEM. ***Average percentage binding is significantly (p

    Article Snippet: 100 μM of sCD4-SNAP was then fluorescently labeled with a SNAP surface Alexa Fluor 488 labeling kit (NEB) and dialyzed against PBS as necessary.

    Techniques: Functional Assay, Western Blot, Expressing, Transfection, Molecular Weight, Flow Cytometry, Positive Control, Concentration Assay, SDS Page, Staining, Purification, Binding Assay, Labeling

    Binding analysis of recombinant TTC and TTC-FITC on isolated PBMCs. Surface staining of CD27 + memory B cells ( a ) and intracellular staining of CD27 ++ CD38 ++ plasma cells ( c ) using recombinant TTC (10 nM) and anti-His5 Alexa Fluor 488 antibody (1:100). Surface staining of CD27 + memory B cells ( b ) and intracellular staining of CD27 ++ CD38 ++ plasma cells ( d ) using a FITC-coupled TTC peptide (1:25)

    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 and TTC-FITC on isolated PBMCs. Surface staining of CD27 + memory B cells ( a ) and intracellular staining of CD27 ++ CD38 ++ plasma cells ( c ) using recombinant TTC (10 nM) and anti-His5 Alexa Fluor 488 antibody (1:100). Surface staining of CD27 + memory B cells ( b ) and intracellular staining of CD27 ++ CD38 ++ plasma cells ( d ) using a FITC-coupled TTC peptide (1:25)

    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, Isolation, Staining

    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

    Dose-dependent binding analysis of the recombinant fusion protein TTC-ETA’ on hybridoma cells. Various concentrations (1–400 nM) of TTC-ETA’ were used to determine a dose-dependent binding activity on TTC-reactive hybridoma cell line 5E4 ( a ) and to exclude specific binding to the control hybridoma cell line 8.18-C5 ( b ). The detection of bound protein was carried out by flow cytometry using a Penta-His Alexa Fluor 488 Conjugate antibody. Measurements were performed in triplicates (n = 3); error bars indicate SD. The recombinant TTC-ETA’ exhibits a dosedependent binding on the target hybridoma cell line 5E4, whereas no binding could be determined on the control hybridoma cell line 8.18-C5

    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: Dose-dependent binding analysis of the recombinant fusion protein TTC-ETA’ on hybridoma cells. Various concentrations (1–400 nM) of TTC-ETA’ were used to determine a dose-dependent binding activity on TTC-reactive hybridoma cell line 5E4 ( a ) and to exclude specific binding to the control hybridoma cell line 8.18-C5 ( b ). The detection of bound protein was carried out by flow cytometry using a Penta-His Alexa Fluor 488 Conjugate antibody. Measurements were performed in triplicates (n = 3); error bars indicate SD. The recombinant TTC-ETA’ exhibits a dosedependent binding on the target hybridoma cell line 5E4, whereas no binding could be determined on the control hybridoma cell line 8.18-C5

    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, Activity Assay, Flow Cytometry, Cytometry

    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

    Mlph’s phosphorylation state does not interfere substantially with actin binding. ( A ) Actin decoration experiments were performed with surface-immobilized and Atto488-labeled actin filaments (red). Filaments were incubated with the complex formed between Mlph and Alexa Fluor 647-labeled Rab27a (green). Dephosphorylated (Dephos; Left ) and the phosphorylated (Phos; Right ) Mlph decorated actin filaments similarly well. Removal of the C-terminal ABD of Mlph (Rab27a/Mlph ΔABD) abolished this interaction regardless of Mlph’s phosphorylation state. ( B ) The dephosphorylated, Alexa Fluor 488-labeled Rab27a/Mlph complex was mixed in equal amounts with the phosphorylated, Alexa Fluor 647-labeled Rab27a/Mlph complex and was incubated with surface-attached, Atto565-labeled actin filaments. The quantification of the actin-associated fluorescence signals from the respective PKA- and phosphatase-treated Rab27a/Mlph complexes showed that the phosphorylation state of Mlph did not substantially interfere with actin binding. Error bars represent SD. (Scale bars: 3 µm.)

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Myosin Va’s adaptor protein melanophilin enforces track selection on the microtubule and actin networks in vitro

    doi: 10.1073/pnas.1619473114

    Figure Lengend Snippet: Mlph’s phosphorylation state does not interfere substantially with actin binding. ( A ) Actin decoration experiments were performed with surface-immobilized and Atto488-labeled actin filaments (red). Filaments were incubated with the complex formed between Mlph and Alexa Fluor 647-labeled Rab27a (green). Dephosphorylated (Dephos; Left ) and the phosphorylated (Phos; Right ) Mlph decorated actin filaments similarly well. Removal of the C-terminal ABD of Mlph (Rab27a/Mlph ΔABD) abolished this interaction regardless of Mlph’s phosphorylation state. ( B ) The dephosphorylated, Alexa Fluor 488-labeled Rab27a/Mlph complex was mixed in equal amounts with the phosphorylated, Alexa Fluor 647-labeled Rab27a/Mlph complex and was incubated with surface-attached, Atto565-labeled actin filaments. The quantification of the actin-associated fluorescence signals from the respective PKA- and phosphatase-treated Rab27a/Mlph complexes showed that the phosphorylation state of Mlph did not substantially interfere with actin binding. Error bars represent SD. (Scale bars: 3 µm.)

    Article Snippet: Before the elution of the protein from the Ni-NTA beads, the wash buffer was supplemented with 20 µM SNAP-tag substrate SNAP-Surface Alexa Fluor 647 or SNAP-Surface Alexa Fluor 488 (New England Biolabs) and was added to the Ni-NTA beads.

    Techniques: Binding Assay, Labeling, Incubation, Fluorescence