streptavidin mag sepharose  (Millipore)


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    Name:
    Streptavidin Mag Sepharose
    Description:
    Streptavidin Mag Sepharose R is a magnetic bead for simple and efficient enrichment of target proteins by immunoprecipitation and purification of biotinylated biomolecules Streptavidin Mag Sepharose R utilizes the strong interaction between biotin and streptavidin ligand which is immobilized on magnetic beads Magnetic beads simplify sample handling in small scale purifications
    Catalog Number:
    ge28-9857-38
    Price:
    None
    Applications:
    Streptavidin Mag Sepharose(R) is a magnetic bead for simple and efficient enrichment of target Proteins by immunoprecipitation and purification of biotinylated biomolecules. Streptavidin Mag Sepharose(R) utilizes the strong interaction between biotin and streptavidin ligand, which is immobilized on magnetic beads. Magnetic beads simplify sample handling in small-scale purifications.The beads are available in two pack sizes: 2 x 1 mL 10% medium slurry and 5 x 1 mL 10% medium slurry. A milliliter of 10% medium slurry is the same as 100 muL sedimented medium and it is sufficient for 20 purification runs according to the recommended immunoprecipitation protocol.
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    Structured Review

    Millipore streptavidin mag sepharose
    Streptavidin Mag Sepharose
    Streptavidin Mag Sepharose R is a magnetic bead for simple and efficient enrichment of target proteins by immunoprecipitation and purification of biotinylated biomolecules Streptavidin Mag Sepharose R utilizes the strong interaction between biotin and streptavidin ligand which is immobilized on magnetic beads Magnetic beads simplify sample handling in small scale purifications
    https://www.bioz.com/result/streptavidin mag sepharose/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    streptavidin mag sepharose - by Bioz Stars, 2020-04
    99/100 stars

    Images

    1) Product Images from "Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein"

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein

    Journal: Journal of Virology

    doi: 10.1128/JVI.00184-17

    Western blot analysis of a biotin internalization assay of RSV F proteins. RSV-infected and noninfected HEp-2 cells were biotin labeled using a membrane-impermeable biotinylation reagent. The cells were shifted with or without antibodies to 37°C for 90 min to allow endocytosis. Noninternalized biotinylated surface proteins were removed by cleavage with glutathione, while internalized proteins were protected from biotin removal. After cell lysis, biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose, separated by SDS-PAGE under nonreducing conditions, and detected with RSV F-specific antibodies. (A) Sample of noninfected cells. (B) Internalized RSV F proteins after incubation at 37°C. (C) Internalized RSV F proteins after incubation with RSV F-specific antibodies. (D) Amount of biotinylated surface RSV F proteins after cleavage with glutathione. (E) Total amount of biotinylated surface RSV F proteins before 37°C incubation step. A representative blot of a duplicate experiment is shown.
    Figure Legend Snippet: Western blot analysis of a biotin internalization assay of RSV F proteins. RSV-infected and noninfected HEp-2 cells were biotin labeled using a membrane-impermeable biotinylation reagent. The cells were shifted with or without antibodies to 37°C for 90 min to allow endocytosis. Noninternalized biotinylated surface proteins were removed by cleavage with glutathione, while internalized proteins were protected from biotin removal. After cell lysis, biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose, separated by SDS-PAGE under nonreducing conditions, and detected with RSV F-specific antibodies. (A) Sample of noninfected cells. (B) Internalized RSV F proteins after incubation at 37°C. (C) Internalized RSV F proteins after incubation with RSV F-specific antibodies. (D) Amount of biotinylated surface RSV F proteins after cleavage with glutathione. (E) Total amount of biotinylated surface RSV F proteins before 37°C incubation step. A representative blot of a duplicate experiment is shown.

    Techniques Used: Western Blot, Infection, Labeling, Lysis, Immunoprecipitation, SDS Page, Incubation

    Related Articles

    Amplification:

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ). .. The identity of the biotinylated pmKan plasmid was confirmed by PCR amplification of a 496 bp-region of the kan gene which contained the site of the original point mutation using primer 1 and primer 2.

    Synthesized:

    Article Title: Specificity of ? and Non-? Isoforms of Arabidopsis 14-3-3 Proteins Towards the H+-ATPase and Other Targets
    Article Snippet: The bL15Vp peptide biotinyl-LKGLDIDTIQQNYTpV (Tp, phosphothreonine) was synthesized by Neosystem (Strasbourg, France). .. Streptavidin-agarose magnetic beads, glutathione-sepharose resin, the catalytic subunit of protein kinase A and thrombin were obtained from Sigma (St. Louis, MO, USA).

    Incubation:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: One sample was neither incubated nor reduced with cleavage buffer to determine the total amount of biotinylated proteins. .. After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions.

    Article Title: Conserved Intergenic Elements and DNA Methylation Cooperate to Regulate Transcription at the il17 Locus *
    Article Snippet: Oligonucleotide probes used for EMSA analysis were 5′ end-labeled with biotin and incubated (0.5 μ m ) with total cell lysate (400 μg) prepared from stimulated Th17 cells under the same ionic conditions used in EMSA reactions. .. Magnetic streptavidin-conjugated agarose beads (MagSelect, Sigma-Aldrich) were used to collect protein complexes bound to the DNA probes.

    Activity Assay:

    Article Title: DNA binding induces dissociation of the multimeric form of HIV-1 integrase: A time-resolved fluorescence anisotropy study
    Article Snippet: Paragraph title: IN and Activity Assay. ... After removal of thrombin by streptavidin-agarose magnetic beads (Novagen), a final dialysis was performed against buffer A containing 20% (vol/vol) glycerol.

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: The helicases containing fractions, identified by both DNA-dependent ATP hydrolysis and helicase activity assays, were pooled. .. Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI).

    Expressing:

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: The expression of the protein was induced by adding isopropylthio-β- d -galactoside to 0.5 mM at low-log phase (OD600 = 0.6). .. Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI).

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: Verification of biotinylated-SSO incorporation λ-Red expression was induced in cultures of DY380/pmKan cells (in 50 ml LB medium in 250 ml Erlenmeyer flasks, grown to OD600 0.3) by shifting them from incubation at 32°C to a shaking water bath at 42°C for 15 min, before chilling them in iced-water. .. After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ).

    Transferring:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions. .. The presence of RSV F proteins was detected by transferring the gel to a polyvinylidene difluoride (PVDF) membrane and subsequent incubation with RSV F-specific MAb.

    Infection:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: Surface proteins of the infected cells were biotinylated using EZ-link Sulfo-NHS-SS-biotin (Thermo Fisher Scientific) at 4°C. .. After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions.

    Endocytosis Assay:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: Paragraph title: Spontaneous endocytosis assay. ... After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions.

    DNA Sequencing:

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI). .. The mutation was created using the QuikChange kit for Site-Directed Mutagenesis from Stratagene and confirmed by DNA sequencing (MWG Biotech).

    Polymerase Chain Reaction:

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ). .. The identity of the biotinylated pmKan plasmid was confirmed by PCR amplification of a 496 bp-region of the kan gene which contained the site of the original point mutation using primer 1 and primer 2.

    Binding Assay:

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: The lysate was centrifuged and applied to the column charged with histidine binding resin (Novagen). .. Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI).

    Magnetic Beads:

    Article Title: Specificity of ? and Non-? Isoforms of Arabidopsis 14-3-3 Proteins Towards the H+-ATPase and Other Targets
    Article Snippet: .. Streptavidin-agarose magnetic beads, glutathione-sepharose resin, the catalytic subunit of protein kinase A and thrombin were obtained from Sigma (St. Louis, MO, USA). .. Restriction enzymes were obtained from Roche Diagnostics (Mannheim, Germany).

    Article Title: DNA binding induces dissociation of the multimeric form of HIV-1 integrase: A time-resolved fluorescence anisotropy study
    Article Snippet: .. After removal of thrombin by streptavidin-agarose magnetic beads (Novagen), a final dialysis was performed against buffer A containing 20% (vol/vol) glycerol. .. TFA parameters were obtained from the two polarized fluorescence decays Ivv(t) and Ivh(t) by using a time-correlated, single-photon counting technique.

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: .. Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI). .. RecQ helicase was further purified by FPLC size-exclusion chromatography using a Superdex 200 column (Pharmacia).

    Mutagenesis:

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI). .. The mutation was created using the QuikChange kit for Site-Directed Mutagenesis from Stratagene and confirmed by DNA sequencing (MWG Biotech).

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ). .. The identity of the biotinylated pmKan plasmid was confirmed by PCR amplification of a 496 bp-region of the kan gene which contained the site of the original point mutation using primer 1 and primer 2.

    Isolation:

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: .. After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ). .. The identity of the biotinylated pmKan plasmid was confirmed by PCR amplification of a 496 bp-region of the kan gene which contained the site of the original point mutation using primer 1 and primer 2.

    Size-exclusion Chromatography:

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI). .. RecQ helicase was further purified by FPLC size-exclusion chromatography using a Superdex 200 column (Pharmacia).

    Purification:

    Article Title: DNA binding induces dissociation of the multimeric form of HIV-1 integrase: A time-resolved fluorescence anisotropy study
    Article Snippet: The purification was based on a batch procedure by using Ni-NTA agarose beads (Amersham Pharmacia). .. After removal of thrombin by streptavidin-agarose magnetic beads (Novagen), a final dialysis was performed against buffer A containing 20% (vol/vol) glycerol.

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI). .. RecQ helicase was further purified by FPLC size-exclusion chromatography using a Superdex 200 column (Pharmacia).

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: .. After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ). .. The identity of the biotinylated pmKan plasmid was confirmed by PCR amplification of a 496 bp-region of the kan gene which contained the site of the original point mutation using primer 1 and primer 2.

    Fast Protein Liquid Chromatography:

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI). .. RecQ helicase was further purified by FPLC size-exclusion chromatography using a Superdex 200 column (Pharmacia).

    SDS Page:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: .. After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions. .. The presence of RSV F proteins was detected by transferring the gel to a polyvinylidene difluoride (PVDF) membrane and subsequent incubation with RSV F-specific MAb.

    Plasmid Preparation:

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: .. After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ). .. The identity of the biotinylated pmKan plasmid was confirmed by PCR amplification of a 496 bp-region of the kan gene which contained the site of the original point mutation using primer 1 and primer 2.

    Radio Immunoprecipitation:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: .. After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions. .. The presence of RSV F proteins was detected by transferring the gel to a polyvinylidene difluoride (PVDF) membrane and subsequent incubation with RSV F-specific MAb.

    Immunoprecipitation:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: .. After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions. .. The presence of RSV F proteins was detected by transferring the gel to a polyvinylidene difluoride (PVDF) membrane and subsequent incubation with RSV F-specific MAb.

    Lysis:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: .. After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions. .. The presence of RSV F proteins was detected by transferring the gel to a polyvinylidene difluoride (PVDF) membrane and subsequent incubation with RSV F-specific MAb.

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  • 97
    Millipore streptavidin agarose beads
    Proline-rich reading array screen and peptide pulldown. (A) Use of biotinylated eVP40 WT (MRRVILPTAPPEYMEAI[Lys-biotin]) peptide (50 μg) to screen a proline-rich reading array. The GST-WW domain fusion proteins are arrayed in duplicate and at different angles, as indicated in enlarged box C. Box C shows duplicate samples of all four WW domains from WWP1, WWP2, and ITCH as indicated. Additional positive interactions are indicated in the highlighted red boxes and ovals (A to H). The eVP40 mutant peptide (MRRVILPTAAAEAMEAI[Lys-biotin]) did not interact with any GST-WW domain fusion protein (data not shown). (B) Exogenously expressed FLAG-tagged WWP1-WT was pulled down with <t>streptavidin</t> beads bound to either eVP40 WT (WT) or PPXY mutant (mut) peptides and detected by Western blotting using anti-Flag antiserum (top). Expression controls for WWP1 and actin are shown (bottom).
    Streptavidin Agarose Beads, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 293 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin agarose beads/product/Millipore
    Average 97 stars, based on 293 article reviews
    Price from $9.99 to $1999.99
    streptavidin agarose beads - by Bioz Stars, 2020-04
    97/100 stars
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    Proline-rich reading array screen and peptide pulldown. (A) Use of biotinylated eVP40 WT (MRRVILPTAPPEYMEAI[Lys-biotin]) peptide (50 μg) to screen a proline-rich reading array. The GST-WW domain fusion proteins are arrayed in duplicate and at different angles, as indicated in enlarged box C. Box C shows duplicate samples of all four WW domains from WWP1, WWP2, and ITCH as indicated. Additional positive interactions are indicated in the highlighted red boxes and ovals (A to H). The eVP40 mutant peptide (MRRVILPTAAAEAMEAI[Lys-biotin]) did not interact with any GST-WW domain fusion protein (data not shown). (B) Exogenously expressed FLAG-tagged WWP1-WT was pulled down with streptavidin beads bound to either eVP40 WT (WT) or PPXY mutant (mut) peptides and detected by Western blotting using anti-Flag antiserum (top). Expression controls for WWP1 and actin are shown (bottom).

    Journal: Journal of Virology

    Article Title: Ubiquitin Ligase WWP1 Interacts with Ebola Virus VP40 To Regulate Egress

    doi: 10.1128/JVI.00812-17

    Figure Lengend Snippet: Proline-rich reading array screen and peptide pulldown. (A) Use of biotinylated eVP40 WT (MRRVILPTAPPEYMEAI[Lys-biotin]) peptide (50 μg) to screen a proline-rich reading array. The GST-WW domain fusion proteins are arrayed in duplicate and at different angles, as indicated in enlarged box C. Box C shows duplicate samples of all four WW domains from WWP1, WWP2, and ITCH as indicated. Additional positive interactions are indicated in the highlighted red boxes and ovals (A to H). The eVP40 mutant peptide (MRRVILPTAAAEAMEAI[Lys-biotin]) did not interact with any GST-WW domain fusion protein (data not shown). (B) Exogenously expressed FLAG-tagged WWP1-WT was pulled down with streptavidin beads bound to either eVP40 WT (WT) or PPXY mutant (mut) peptides and detected by Western blotting using anti-Flag antiserum (top). Expression controls for WWP1 and actin are shown (bottom).

    Article Snippet: Streptavidin agarose beads (Millipore) were prewashed once with 1× mild buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 0.1% NP-40, 5 mM EDTA, 5 mM EGTA, 15 mM MgCl2 ), and 15 μg of the WT or PPXY mutant eVP40 peptide was incubated with the prewashed streptavidin beads in 500 μl of 1× mild buffer for 1 h at 4°C with rocking.

    Techniques: Mutagenesis, Western Blot, Expressing

    The rate of cell surface expression/appearance/transport of BRI2 is reduced in the absence of N-glycosylation. Wild-type mycBRI2 or mycBRI2/N170A was expressed in HEK293 cells. The newly synthesized proteins were labeled with 35 S in radiolabeling medium for 2 h (pulse) at 16°C and then were incubated in non-radiolabeling medium for 0′, 20′, 40′ and 60′ (chase). ( A ) Cell surface proteins were labeled with biotin and precipitated with streptavidin beads. Precipitated cell surface proteins were eluted from the beads and immunoprecipitated with 9B11 antibody against the myc epitope before electrophoresis and autoradiography. ( B ) Immunoprecipitation of cell extracts with 9B11, electrophoresis and autoradiography were performed to verify the expression levels of BRI2.

    Journal: Glycobiology

    Article Title: Glycosylation of BRI2 on asparagine 170 is involved in its trafficking to the cell surface but not in its processing by furin or ADAM10

    doi: 10.1093/glycob/cwr097

    Figure Lengend Snippet: The rate of cell surface expression/appearance/transport of BRI2 is reduced in the absence of N-glycosylation. Wild-type mycBRI2 or mycBRI2/N170A was expressed in HEK293 cells. The newly synthesized proteins were labeled with 35 S in radiolabeling medium for 2 h (pulse) at 16°C and then were incubated in non-radiolabeling medium for 0′, 20′, 40′ and 60′ (chase). ( A ) Cell surface proteins were labeled with biotin and precipitated with streptavidin beads. Precipitated cell surface proteins were eluted from the beads and immunoprecipitated with 9B11 antibody against the myc epitope before electrophoresis and autoradiography. ( B ) Immunoprecipitation of cell extracts with 9B11, electrophoresis and autoradiography were performed to verify the expression levels of BRI2.

    Article Snippet: The cell extracts were centrifuged at 15,000 × g for 30 min and supernatants were incubated with 50 μL of streptavidin–agarose beads (Millipore) for 1 h at 4°C.

    Techniques: Expressing, Synthesized, Labeling, Radioactivity, Incubation, Immunoprecipitation, Electrophoresis, Autoradiography

    Inhibition of N-glycosylation of BRI2 inhibits its expression at the cell surface. Wild-type mycBRI2 or mycBRI2/N170A was expressed in HEK293 cells. Cell surface proteins were labeled with biotin (lanes 1 and 2) or were not labeled (lanes 3 and 4), as a control for biotinylation specificity. ( A ) Cell extracts were precipitated with streptavidin beads and analyzed with western blot against myc with 9B11 antibody. ( B ) Cell extracts were directly analyzed with western blot as a control for protein expression. The two immunoreactive bands of BRI2 proteins correspond to the furin-cleaved and the non-cleaved wild-type mycBRI2 or mycBRI2/N170A.

    Journal: Glycobiology

    Article Title: Glycosylation of BRI2 on asparagine 170 is involved in its trafficking to the cell surface but not in its processing by furin or ADAM10

    doi: 10.1093/glycob/cwr097

    Figure Lengend Snippet: Inhibition of N-glycosylation of BRI2 inhibits its expression at the cell surface. Wild-type mycBRI2 or mycBRI2/N170A was expressed in HEK293 cells. Cell surface proteins were labeled with biotin (lanes 1 and 2) or were not labeled (lanes 3 and 4), as a control for biotinylation specificity. ( A ) Cell extracts were precipitated with streptavidin beads and analyzed with western blot against myc with 9B11 antibody. ( B ) Cell extracts were directly analyzed with western blot as a control for protein expression. The two immunoreactive bands of BRI2 proteins correspond to the furin-cleaved and the non-cleaved wild-type mycBRI2 or mycBRI2/N170A.

    Article Snippet: The cell extracts were centrifuged at 15,000 × g for 30 min and supernatants were incubated with 50 μL of streptavidin–agarose beads (Millipore) for 1 h at 4°C.

    Techniques: Inhibition, Expressing, Labeling, Western Blot