streptavidin coupled agarose beads  (Thermo Fisher)


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    Structured Review

    Thermo Fisher streptavidin coupled agarose beads
    Notch1 S2 cleavage occurs at the cell surface. A, upper panel, Myc immunoblot of surface-biotinylated and <t>streptavidin-precipitated</t> U2OS cells transfected with the active LNR CC → SS 6Myc. Left upper panel shows input, and right panel streptavidin

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    Images

    1) Product Images from "Metalloprotease ADAM10 Is Required for Notch1 Site 2 Cleavage *"

    Article Title: Metalloprotease ADAM10 Is Required for Notch1 Site 2 Cleavage *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M109.006775

    Notch1 S2 cleavage occurs at the cell surface. A, upper panel, Myc immunoblot of surface-biotinylated and streptavidin-precipitated U2OS cells transfected with the active LNR CC → SS 6Myc. Left upper panel shows input, and right panel streptavidin
    Figure Legend Snippet: Notch1 S2 cleavage occurs at the cell surface. A, upper panel, Myc immunoblot of surface-biotinylated and streptavidin-precipitated U2OS cells transfected with the active LNR CC → SS 6Myc. Left upper panel shows input, and right panel streptavidin

    Techniques Used: Transfection

    2) Product Images from "β-Catenin Regulates Acetylcholine Receptor Clustering in Muscle Cells through Interaction with Rapsyn"

    Article Title: β-Catenin Regulates Acetylcholine Receptor Clustering in Muscle Cells through Interaction with Rapsyn

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.4691-06.2007

    β-Catenin associates with the AChR complex through rapsyn. A , Direct interaction of β-catenin with rapsyn. [ 35 S]-labeled β-catenin proteins were incubated with GST alone or GST–rapsyn immobilized on beads. Bound [ 35 S]-β-catenin proteins were visualized by autoradiogram. Molecular weight markers are in kilodaltons. B , Schematic diagram of β-catenin constructs and binding activity to rapsyn. C , Association of β-catenin with surface AChR in muscle cells. Live myotubes, treated with agrin for indicated times, were incubated with biotin-αBTX to label surface AChR. Lysates were incubated with streptavidin-coupled agarose beads, and bead-associated proteins were subjected to immunoblotting with antibodies against AChRα, β-catenin, and rapsyn. Lysates (5% of input) were blotted to indicate equal amounts of inputs. D , β-Catenin association with AChR requires rapsyn. Control or rapsyn mutant (R−/−) myotubes were stimulated without or with agrin for 12 h. Proteins associated with surface AChRs were isolated as in C and probed with indicated antibodies. Lysates (5% of input) were blotted to indicate equal amounts of inputs. PD, Pull down; IB, immunoblotting; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.
    Figure Legend Snippet: β-Catenin associates with the AChR complex through rapsyn. A , Direct interaction of β-catenin with rapsyn. [ 35 S]-labeled β-catenin proteins were incubated with GST alone or GST–rapsyn immobilized on beads. Bound [ 35 S]-β-catenin proteins were visualized by autoradiogram. Molecular weight markers are in kilodaltons. B , Schematic diagram of β-catenin constructs and binding activity to rapsyn. C , Association of β-catenin with surface AChR in muscle cells. Live myotubes, treated with agrin for indicated times, were incubated with biotin-αBTX to label surface AChR. Lysates were incubated with streptavidin-coupled agarose beads, and bead-associated proteins were subjected to immunoblotting with antibodies against AChRα, β-catenin, and rapsyn. Lysates (5% of input) were blotted to indicate equal amounts of inputs. D , β-Catenin association with AChR requires rapsyn. Control or rapsyn mutant (R−/−) myotubes were stimulated without or with agrin for 12 h. Proteins associated with surface AChRs were isolated as in C and probed with indicated antibodies. Lysates (5% of input) were blotted to indicate equal amounts of inputs. PD, Pull down; IB, immunoblotting; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.

    Techniques Used: Labeling, Incubation, Molecular Weight, Construct, Binding Assay, Activity Assay, Mutagenesis, Isolation

    3) Product Images from "The Neural Cell Adhesion Molecule Regulates Cell-Surface Delivery of G-Protein-Activated Inwardly Rectifying Potassium Channels Via Lipid Rafts"

    Article Title: The Neural Cell Adhesion Molecule Regulates Cell-Surface Delivery of G-Protein-Activated Inwardly Rectifying Potassium Channels Via Lipid Rafts

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.22-16-07154.2002

    NCAM140 reduces cell-surface localization of Kir3.1/3.2 in CHO cells but does not alter internalization rates of Kir3.1/3.2. A , Immunoblot analysis of Kir3.1/3.2 cell-surface expression in CHO cells. CHO cells were cotransfected with Kir3.1/3.2 and either NCAM120 ( lanes 3, 6, 9 , and 12 ), NCAM140 ( lanes 2, 5, 8 , and 11 ), or NCAM140Δ ( lanes 1, 4, 7 , and 10 ). Cell lysates ( lanes 4–6 and 10–12 ) and proteins bound to streptavidin-agarose ( lanes 1–3 and 7–9 ) were separated by SDS-PAGE, and the amount of Kir3.1/3.2 or NCAM was quantified by immunoblot analysis using polyclonal Kir3.1 antibodies. NCAM140 reduces surface localization of Kir3.1/3.2 compared with NCAM120 and NCAM140Δ ( lane 8 vs lanes 7 and 9 ), whereas the overall intensity of Kir3.1/3.2-immunoreactive bands in the cell lysate is not altered by NCAM140 ( lane 11 vs lanes 10 and 12 ). Incubation with lovastatin does not influence Kir3.1/3.2 expression ( lanes 4–6 vs 10–12 ) but enhances surface localization of Kir3.1/3.2 ( lane 2 vs lanes 1 and 3 ). B , Normalized surface localization of Kir3.1/3.2 in the presence of NCAM140 (0.48 ± 0.03) and NCAM140Δ (0.84 ± 0.09) in comparison with NCAM120. Kir3.1-immunoreactive bands of streptavidin-agarose-precipitated proteins were quantified by densitometric analysis and expressed relative to NCAM120 (100%). ∗Values significantly different from that of NCAM120 (Student's t test; p
    Figure Legend Snippet: NCAM140 reduces cell-surface localization of Kir3.1/3.2 in CHO cells but does not alter internalization rates of Kir3.1/3.2. A , Immunoblot analysis of Kir3.1/3.2 cell-surface expression in CHO cells. CHO cells were cotransfected with Kir3.1/3.2 and either NCAM120 ( lanes 3, 6, 9 , and 12 ), NCAM140 ( lanes 2, 5, 8 , and 11 ), or NCAM140Δ ( lanes 1, 4, 7 , and 10 ). Cell lysates ( lanes 4–6 and 10–12 ) and proteins bound to streptavidin-agarose ( lanes 1–3 and 7–9 ) were separated by SDS-PAGE, and the amount of Kir3.1/3.2 or NCAM was quantified by immunoblot analysis using polyclonal Kir3.1 antibodies. NCAM140 reduces surface localization of Kir3.1/3.2 compared with NCAM120 and NCAM140Δ ( lane 8 vs lanes 7 and 9 ), whereas the overall intensity of Kir3.1/3.2-immunoreactive bands in the cell lysate is not altered by NCAM140 ( lane 11 vs lanes 10 and 12 ). Incubation with lovastatin does not influence Kir3.1/3.2 expression ( lanes 4–6 vs 10–12 ) but enhances surface localization of Kir3.1/3.2 ( lane 2 vs lanes 1 and 3 ). B , Normalized surface localization of Kir3.1/3.2 in the presence of NCAM140 (0.48 ± 0.03) and NCAM140Δ (0.84 ± 0.09) in comparison with NCAM120. Kir3.1-immunoreactive bands of streptavidin-agarose-precipitated proteins were quantified by densitometric analysis and expressed relative to NCAM120 (100%). ∗Values significantly different from that of NCAM120 (Student's t test; p

    Techniques Used: Expressing, SDS Page, Incubation

    4) Product Images from "Cellular Form of Prion Protein Inhibits Reelin-Mediated Shedding of Caspr from the Neuronal Cell Surface to Potentiate Caspr-Mediated Inhibition of Neurite Outgrowth"

    Article Title: Cellular Form of Prion Protein Inhibits Reelin-Mediated Shedding of Caspr from the Neuronal Cell Surface to Potentiate Caspr-Mediated Inhibition of Neurite Outgrowth

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.5657-09.2010

    PrP increases cell surface expression of Caspr. A , Caspr +/+ and Caspr −/− brain homogenates were probed by Western blot with polyclonal antibodies (N15) against a peptide at the N terminus of Caspr extracellular domain. Note that the full-length 180 kDa product and the 50 kDa degradation product of Caspr are recognized in Caspr +/+ but not in Caspr −/− brain homogenates. B , Culture medium from Caspr +/+ and Caspr −/− (top) or PrP +/+ and PrP −/− (bottom) cerebellar neurons was analyzed by Western blot with polyclonal antibodies against Caspr extracellular domain. Note that these antibodies recognize the 50 kDa degradation product of Caspr in the culture medium from Caspr +/+ but not Caspr −/− neurons. The level of this band is increased in the culture medium from PrP −/− versus PrP +/+ neurons. Labeling for close homolog of L1 (CHL1), which is also released into the culture medium, served as a loading control. C , Cultured PrP +/+ and PrP −/− cerebellar neurons were labeled live with polyclonal antibodies against Caspr extracellular domain. Note reduced levels of Caspr at the cell surface of PrP −/− versus PrP +/+ neurites. Scale bar, 10 μm. D , CHO cells were transfected with Caspr alone or cotransfected with Caspr and PrP or contactin (cont.). Cell surface proteins were then biotinylated on live cells and separated via streptavidin-coated beads from the total protein pool following cell lysis. Samples containing cell surface proteins (biot.) and total cell lysates (lysate) were then probed by Western blot with polyclonal antibodies against Caspr intracellular domain, PrP, and contactin. Labeling for the FGF receptor (Flg) served as a loading control. Higher levels of cell surface-biotinylated Caspr are observed in the samples of cells cotransfected with Caspr and PrP when compared with Caspr-only transfected cells. Cell surface Caspr levels are also higher in contactin and Caspr cotransfected versus Caspr-only transfected cells, although this effect is less prominent than in Caspr and PrP cotransfected cells. Graph shows quantitation of the blots (mean ± SEM, n = 3) with the signal from Caspr-only transfected cells set to 100%. * p
    Figure Legend Snippet: PrP increases cell surface expression of Caspr. A , Caspr +/+ and Caspr −/− brain homogenates were probed by Western blot with polyclonal antibodies (N15) against a peptide at the N terminus of Caspr extracellular domain. Note that the full-length 180 kDa product and the 50 kDa degradation product of Caspr are recognized in Caspr +/+ but not in Caspr −/− brain homogenates. B , Culture medium from Caspr +/+ and Caspr −/− (top) or PrP +/+ and PrP −/− (bottom) cerebellar neurons was analyzed by Western blot with polyclonal antibodies against Caspr extracellular domain. Note that these antibodies recognize the 50 kDa degradation product of Caspr in the culture medium from Caspr +/+ but not Caspr −/− neurons. The level of this band is increased in the culture medium from PrP −/− versus PrP +/+ neurons. Labeling for close homolog of L1 (CHL1), which is also released into the culture medium, served as a loading control. C , Cultured PrP +/+ and PrP −/− cerebellar neurons were labeled live with polyclonal antibodies against Caspr extracellular domain. Note reduced levels of Caspr at the cell surface of PrP −/− versus PrP +/+ neurites. Scale bar, 10 μm. D , CHO cells were transfected with Caspr alone or cotransfected with Caspr and PrP or contactin (cont.). Cell surface proteins were then biotinylated on live cells and separated via streptavidin-coated beads from the total protein pool following cell lysis. Samples containing cell surface proteins (biot.) and total cell lysates (lysate) were then probed by Western blot with polyclonal antibodies against Caspr intracellular domain, PrP, and contactin. Labeling for the FGF receptor (Flg) served as a loading control. Higher levels of cell surface-biotinylated Caspr are observed in the samples of cells cotransfected with Caspr and PrP when compared with Caspr-only transfected cells. Cell surface Caspr levels are also higher in contactin and Caspr cotransfected versus Caspr-only transfected cells, although this effect is less prominent than in Caspr and PrP cotransfected cells. Graph shows quantitation of the blots (mean ± SEM, n = 3) with the signal from Caspr-only transfected cells set to 100%. * p

    Techniques Used: Expressing, Western Blot, Labeling, Cell Culture, Transfection, Lysis, Quantitation Assay

    5) Product Images from "Intersectin‐s interaction with DENND2B facilitates recycling of epidermal growth factor receptor"

    Article Title: Intersectin‐s interaction with DENND2B facilitates recycling of epidermal growth factor receptor

    Journal: EMBO Reports

    doi: 10.15252/embr.201744034

    DENND2B promotes EGFR recycling A, B HeLa cells expressing the indicated constructs. Boxed regions are magnified on the bottom. Scale bars: 5 μm in the top panel and 1 μm in the bottom panel. White arrows and arrowheads point to co‐localization on vesicles and plasma membrane, respectively. C Transduced MCF10A cells were quantified by real‐time PCR. Mean ± SD, ANOVA with Dunnett's post hoc test *** P = 0.000 for both comparisons, n = 3 from three independent experiments. D Transduced HEK‐293T cells expressing Flag‐DENND2B were analysed by Western blot. E Transduced MCF10A cells were biotinylated and cell lysates were incubated with streptavidin beads. Bound proteins were detected by Western blot. F Quantification of (E) where surface EGFR is normalized to total EGFR. Mean ± SD, ANOVA with Dunnett's post hoc test * P = 0.013 and *** P = 0.000. n = 6 for all treatment groups from four independent experiments. G Quantification of (E) where total EGFR is normalized to Hsc70. Mean ± SD, n = 3 for all treatment groups from three independent experiments. H Schematic of trafficking assay. Surface EGFR is labelled and internalized at 16°C or recycled at 37°C. Acid washing removes labelled surface pools and allows analysis of the internal pool of EGFR originating from the surface. I MCF10A cells expressing GFP‐DENND2B were labelled for surface EGFR on ice, incubated at 16°C to allow internalization, acid washed to remove remaining labelled‐EGFR and processed for immunofluorescence to visualize the internal pool of EGFR (post‐endocytosis, top panel) or incubated at 37°C to allow recycling, acid washed again and processed for immunofluorescence to visualize the remaining internal pool of EGFR (post‐recycling, bottom panel). Scale bars: 5 μm. J Quantification of experiment in (I), top panel, internal EGFR post‐endocytosis. Mean fluorescence per cell ± SD, n = 13 for GFP‐DENND2B and n = 21 for control cells pooled from two independent experiments. K Quantification of experiment in (I), bottom panel, internal EGFR post‐recycling. Mean fluorescence per cell ± SD, n = 10 for GFP‐DENND2B and n = 26 for control cells pooled from 2 independent experiments. Source data are available online for this figure.
    Figure Legend Snippet: DENND2B promotes EGFR recycling A, B HeLa cells expressing the indicated constructs. Boxed regions are magnified on the bottom. Scale bars: 5 μm in the top panel and 1 μm in the bottom panel. White arrows and arrowheads point to co‐localization on vesicles and plasma membrane, respectively. C Transduced MCF10A cells were quantified by real‐time PCR. Mean ± SD, ANOVA with Dunnett's post hoc test *** P = 0.000 for both comparisons, n = 3 from three independent experiments. D Transduced HEK‐293T cells expressing Flag‐DENND2B were analysed by Western blot. E Transduced MCF10A cells were biotinylated and cell lysates were incubated with streptavidin beads. Bound proteins were detected by Western blot. F Quantification of (E) where surface EGFR is normalized to total EGFR. Mean ± SD, ANOVA with Dunnett's post hoc test * P = 0.013 and *** P = 0.000. n = 6 for all treatment groups from four independent experiments. G Quantification of (E) where total EGFR is normalized to Hsc70. Mean ± SD, n = 3 for all treatment groups from three independent experiments. H Schematic of trafficking assay. Surface EGFR is labelled and internalized at 16°C or recycled at 37°C. Acid washing removes labelled surface pools and allows analysis of the internal pool of EGFR originating from the surface. I MCF10A cells expressing GFP‐DENND2B were labelled for surface EGFR on ice, incubated at 16°C to allow internalization, acid washed to remove remaining labelled‐EGFR and processed for immunofluorescence to visualize the internal pool of EGFR (post‐endocytosis, top panel) or incubated at 37°C to allow recycling, acid washed again and processed for immunofluorescence to visualize the remaining internal pool of EGFR (post‐recycling, bottom panel). Scale bars: 5 μm. J Quantification of experiment in (I), top panel, internal EGFR post‐endocytosis. Mean fluorescence per cell ± SD, n = 13 for GFP‐DENND2B and n = 21 for control cells pooled from two independent experiments. K Quantification of experiment in (I), bottom panel, internal EGFR post‐recycling. Mean fluorescence per cell ± SD, n = 10 for GFP‐DENND2B and n = 26 for control cells pooled from 2 independent experiments. Source data are available online for this figure.

    Techniques Used: Expressing, Construct, Real-time Polymerase Chain Reaction, Western Blot, Incubation, Immunofluorescence, Fluorescence

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    Centrifugation:

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    Article Snippet: .. After centrifugation at 270,000 × g at 4 °C for 15 h, 2-ml aliquots of the gradients were collected from the top and submitted to precipitation with neutravidin-agarose beads (Pierce) at 4 °C overnight. .. Neutravidin-bound proteins from each sucrose gradient fraction were separated by SDS-PAGE and transferred to nitrocellulose membranes.

    Immunoprecipitation:

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    Purification:

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    Article Snippet: RT-L4 Binding Site Screening Assay Mapping the potential binding region of RT-L4 was carried out using purified Vps26A, Vps351-390 , Vps26-Vps351-390 subcomplex and the associated mutants. .. First, 10 μM of purified proteins were incubated with fresh streptavidin agarose containing either 100 μM of RT-L4 or equivalent percentage (v/v) of DMSO. .. The mixture was incubated in binding buffer containing 50 mM HEPES pH 7.5, 200 mM NaCl, 5% glycerol, 0.5 mM TCEP for 30 min at 4°C.

    Incubation:

    Article Title: De novo macrocyclic peptides for inhibiting, stabilising and probing the function of the Retromer endosomal trafficking complex
    Article Snippet: RT-L4 Binding Site Screening Assay Mapping the potential binding region of RT-L4 was carried out using purified Vps26A, Vps351-390 , Vps26-Vps351-390 subcomplex and the associated mutants. .. First, 10 μM of purified proteins were incubated with fresh streptavidin agarose containing either 100 μM of RT-L4 or equivalent percentage (v/v) of DMSO. .. The mixture was incubated in binding buffer containing 50 mM HEPES pH 7.5, 200 mM NaCl, 5% glycerol, 0.5 mM TCEP for 30 min at 4°C.

    Article Title: Metalloprotease ADAM10 Is Required for Notch1 Site 2 Cleavage *
    Article Snippet: .. After input, samples were taken, and streptavidin-coupled agarose beads (Pierce) were added to the supernatant and incubated for 90 min. .. Samples were washed three times in RIPA and three times in PBS, boiled in Laemmli buffer, and analyzed by PAGE.

    Article Title: Cystine 186-cystine 209 disulfide bond is not essential for the procoagulant activity of tissue factor or for its de-encryption
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    Molecular Weight:

    Article Title: Variant surface glycoproteins from Venezuelan trypanosome isolates are recognized by sera from animals infected with either Trypanosoma evansi or Trypanosoma vivax
    Article Snippet: In this study, we investigated the potential use of VSG variants as diagnostic reagents for the detection of trypanosomosis caused by T. vivax and T. evansi , and examined whether the soluble form of these VSG antigens contained common epitopes recognized by sera from animals infected with either of these species of trypanosomes. .. 2.1 Materials Reagents were purchased from the following sources: middle range molecular weight protein markers, anti-mouse IgG horseradish peroxidase conjugate, 5-bromo-4-chloro-3 indolyl phosphate (BCIP), nitro blue tetrazolium (NBT), Promega ; anti-rabbit IgG alkaline phosphatase conjugate, anti-bovine IgG horseradish peroxidase conjugate, anti-bovine IgG alkaline phosphatase conjugate, anti-equine IgG alkaline phosphatase conjugate, anti-mouse IgG alkaline phosphatase conjugate, diaminobenzidine (DAB), horseradish peroxidase type VI-A, fibrous DEAE-cellulose, benzamidine, iodoacetamide, phenyl methyl sulfonyl fluoride (PMSF), N-N′-1,2 phenylenedimaleimide (o-PDM), N-N′-1,4 phenyllenedimaleimide (p-PDM), gel filtration molecular weight protein marker kit, Staphylococcus aureus V8 protease, concanavalin A (Con A), 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), methyl-α-d -mannopyranoside, methyl-α-d -glucopyranoside, Sigma ; Q-Sepharose, S-Sepharose, Sefacryl S-300, Pharmacia ; pre-stained high molecular weight protein markers, Gibco BRL ; sulfosuccinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate (sulfo-SMCC), nitrocellulose (0.45 μm pore size), Pierce; broad range isoelectric focusing calibration kit (3–10), Immobilin dry strips (pH 5–8), ampholites (pH 3–10), BioRad . ..

    Filtration:

    Article Title: Variant surface glycoproteins from Venezuelan trypanosome isolates are recognized by sera from animals infected with either Trypanosoma evansi or Trypanosoma vivax
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    Marker:

    Article Title: Variant surface glycoproteins from Venezuelan trypanosome isolates are recognized by sera from animals infected with either Trypanosoma evansi or Trypanosoma vivax
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    Thermo Fisher streptavidin coupled agarose beads
    Notch1 S2 cleavage occurs at the cell surface. A, upper panel, Myc immunoblot of surface-biotinylated and <t>streptavidin-precipitated</t> U2OS cells transfected with the active LNR CC → SS 6Myc. Left upper panel shows input, and right panel streptavidin
    Streptavidin Coupled Agarose Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin coupled agarose beads/product/Thermo Fisher
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    streptavidin coupled agarose beads - by Bioz Stars, 2021-06
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    99
    Thermo Fisher streptavidin coupled magnetic beads
    Overview of the antibody selection process. A) PBMC from a Mamu-A1*001 positive macaque was used to alloimmunize a Mamu-A1*001 negative macaque to induce Mamu-A1*001-binding antibodies. B) Timeline for the immunizations and blood draws for the alloimmunized animal. C) The panning process to isolate the Mamu-A1*001-binding antibody was initiated by amplifying immunoglobulin genes from the alloimmunized macaque and inserting into the phagemid pCOMB3X. The resulting phage library was screened with biotinylated MHC molecules bound to <t>streptavidin-coated</t> magnetic beads and applied to a magnet to wash away unbound phage. Bound phage was eluted and amplified in E . coli for new rounds of selection.
    Streptavidin Coupled Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin coupled magnetic beads/product/Thermo Fisher
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    streptavidin coupled magnetic beads - by Bioz Stars, 2021-06
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    Notch1 S2 cleavage occurs at the cell surface. A, upper panel, Myc immunoblot of surface-biotinylated and streptavidin-precipitated U2OS cells transfected with the active LNR CC → SS 6Myc. Left upper panel shows input, and right panel streptavidin

    Journal: The Journal of Biological Chemistry

    Article Title: Metalloprotease ADAM10 Is Required for Notch1 Site 2 Cleavage *

    doi: 10.1074/jbc.M109.006775

    Figure Lengend Snippet: Notch1 S2 cleavage occurs at the cell surface. A, upper panel, Myc immunoblot of surface-biotinylated and streptavidin-precipitated U2OS cells transfected with the active LNR CC → SS 6Myc. Left upper panel shows input, and right panel streptavidin

    Article Snippet: After input, samples were taken, and streptavidin-coupled agarose beads (Pierce) were added to the supernatant and incubated for 90 min.

    Techniques: Transfection

    β-Catenin associates with the AChR complex through rapsyn. A , Direct interaction of β-catenin with rapsyn. [ 35 S]-labeled β-catenin proteins were incubated with GST alone or GST–rapsyn immobilized on beads. Bound [ 35 S]-β-catenin proteins were visualized by autoradiogram. Molecular weight markers are in kilodaltons. B , Schematic diagram of β-catenin constructs and binding activity to rapsyn. C , Association of β-catenin with surface AChR in muscle cells. Live myotubes, treated with agrin for indicated times, were incubated with biotin-αBTX to label surface AChR. Lysates were incubated with streptavidin-coupled agarose beads, and bead-associated proteins were subjected to immunoblotting with antibodies against AChRα, β-catenin, and rapsyn. Lysates (5% of input) were blotted to indicate equal amounts of inputs. D , β-Catenin association with AChR requires rapsyn. Control or rapsyn mutant (R−/−) myotubes were stimulated without or with agrin for 12 h. Proteins associated with surface AChRs were isolated as in C and probed with indicated antibodies. Lysates (5% of input) were blotted to indicate equal amounts of inputs. PD, Pull down; IB, immunoblotting; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.

    Journal: The Journal of Neuroscience

    Article Title: β-Catenin Regulates Acetylcholine Receptor Clustering in Muscle Cells through Interaction with Rapsyn

    doi: 10.1523/JNEUROSCI.4691-06.2007

    Figure Lengend Snippet: β-Catenin associates with the AChR complex through rapsyn. A , Direct interaction of β-catenin with rapsyn. [ 35 S]-labeled β-catenin proteins were incubated with GST alone or GST–rapsyn immobilized on beads. Bound [ 35 S]-β-catenin proteins were visualized by autoradiogram. Molecular weight markers are in kilodaltons. B , Schematic diagram of β-catenin constructs and binding activity to rapsyn. C , Association of β-catenin with surface AChR in muscle cells. Live myotubes, treated with agrin for indicated times, were incubated with biotin-αBTX to label surface AChR. Lysates were incubated with streptavidin-coupled agarose beads, and bead-associated proteins were subjected to immunoblotting with antibodies against AChRα, β-catenin, and rapsyn. Lysates (5% of input) were blotted to indicate equal amounts of inputs. D , β-Catenin association with AChR requires rapsyn. Control or rapsyn mutant (R−/−) myotubes were stimulated without or with agrin for 12 h. Proteins associated with surface AChRs were isolated as in C and probed with indicated antibodies. Lysates (5% of input) were blotted to indicate equal amounts of inputs. PD, Pull down; IB, immunoblotting; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.

    Article Snippet: Lysates were incubated with streptavidin-coupled agarose beads (Invitrogen) for 6 h at 4°C and washed extensively with the extraction buffer, except Lubrol-PX was 0.1%.

    Techniques: Labeling, Incubation, Molecular Weight, Construct, Binding Assay, Activity Assay, Mutagenesis, Isolation

    Overview of the antibody selection process. A) PBMC from a Mamu-A1*001 positive macaque was used to alloimmunize a Mamu-A1*001 negative macaque to induce Mamu-A1*001-binding antibodies. B) Timeline for the immunizations and blood draws for the alloimmunized animal. C) The panning process to isolate the Mamu-A1*001-binding antibody was initiated by amplifying immunoglobulin genes from the alloimmunized macaque and inserting into the phagemid pCOMB3X. The resulting phage library was screened with biotinylated MHC molecules bound to streptavidin-coated magnetic beads and applied to a magnet to wash away unbound phage. Bound phage was eluted and amplified in E . coli for new rounds of selection.

    Journal: PLoS ONE

    Article Title: Isolation of a monoclonal antibody from a phage display library binding the rhesus macaque MHC class I allomorph Mamu-A1*001

    doi: 10.1371/journal.pone.0179039

    Figure Lengend Snippet: Overview of the antibody selection process. A) PBMC from a Mamu-A1*001 positive macaque was used to alloimmunize a Mamu-A1*001 negative macaque to induce Mamu-A1*001-binding antibodies. B) Timeline for the immunizations and blood draws for the alloimmunized animal. C) The panning process to isolate the Mamu-A1*001-binding antibody was initiated by amplifying immunoglobulin genes from the alloimmunized macaque and inserting into the phagemid pCOMB3X. The resulting phage library was screened with biotinylated MHC molecules bound to streptavidin-coated magnetic beads and applied to a magnet to wash away unbound phage. Bound phage was eluted and amplified in E . coli for new rounds of selection.

    Article Snippet: The MHC-binding phages were captured by adding streptavidin-coupled magnetic beads (Invitrogen) suspended in “PBS Tween” containing 4% fetal bovine serum (FBS) and 1% Tween 20 and incubated for 30 minutes at room temperature.

    Techniques: Selection, Binding Assay, Magnetic Beads, Amplification

    TRIB1 and HNF4A form a complex. ( A ), Constructs coding for myc-tagged BirA alone or inserted N terminal of TRIB1 were co-transfected with HNF4A expression plasmids in HEK293T for 24 h. Following an additional 24 h growth in media supplemented with 0.1 mM biotin, cells were harvested and lysed under denaturing conditions. Biotinylated targets were then isolated using streptavidin beads and analyzed by Western blotting using cognate antibodies followed by streptavidin coupled to IRDye800CW. ( B ), Plasmids encoding either HNF4A or HNF1A were transfected alongside FLAG-tagged TRIB1 plasmids in HEK293T cells. Potential complexes were isolated with FLAG-specific immunobeads and analyzed by Western blotting. ( C ), Interaction is independent of DNA binding. Ethidium bromide (0.2 mg/ml) was included during the immunoprecipitation. Samples were analyzed by Western blotting using the indicated antibodies.

    Journal: Scientific Reports

    Article Title: TRIB1 is a positive regulator of hepatocyte nuclear factor 4-alpha

    doi: 10.1038/s41598-017-05768-1

    Figure Lengend Snippet: TRIB1 and HNF4A form a complex. ( A ), Constructs coding for myc-tagged BirA alone or inserted N terminal of TRIB1 were co-transfected with HNF4A expression plasmids in HEK293T for 24 h. Following an additional 24 h growth in media supplemented with 0.1 mM biotin, cells were harvested and lysed under denaturing conditions. Biotinylated targets were then isolated using streptavidin beads and analyzed by Western blotting using cognate antibodies followed by streptavidin coupled to IRDye800CW. ( B ), Plasmids encoding either HNF4A or HNF1A were transfected alongside FLAG-tagged TRIB1 plasmids in HEK293T cells. Potential complexes were isolated with FLAG-specific immunobeads and analyzed by Western blotting. ( C ), Interaction is independent of DNA binding. Ethidium bromide (0.2 mg/ml) was included during the immunoprecipitation. Samples were analyzed by Western blotting using the indicated antibodies.

    Article Snippet: Insoluble material was removed by centrifugation at 15,000 x g for 10 min and the supernatant was incubated with Streptavidin-coupled magnetic beads (Life Technologies) for 1 h. Samples were washed 4 X in dilution buffer and analyzed by Western blot.

    Techniques: Construct, Transfection, Expressing, Isolation, Western Blot, Binding Assay, Immunoprecipitation