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agarose streptavidin  (Vector Laboratories)


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    Vector Laboratories agarose streptavidin
    Mass spectrometry identifies nuclear paraspeckles as interacting partners of unphosphorylated miR-34 probes. ( A ) Workflow of sample isolation for mass spectrometry. <t>Streptavidin</t> sepharose beads were incubated with biotinylated miRNA mimics and mixed with sonicated whole-cell lysates. Samples were eluted by RNAse A treatment. The figure was created with Biorender. ( B ) Curation of mass spectrometry hits. Candidate proteins were identified by significance, uniqueness to the 5′OH miR-34a probe, and presence of known RNA-binding activity. ( C ) Characterization of isolated proteins. The total number of proteins isolated binding to the indicated probe is shown in parentheses, with the number of proteins unique to that sample or overlapping with other samples shown in the Venn diagram. ( D ) Gene ontology (GO) curation for cellular compartments performed on proteins identified in the 5′OH miR-34a eluates before and after curation (which was the removal of hits with a score below 20, p value > 0.05, non-unique proteins across three replicates, and non-RNA-binding proteins).
    Agarose Streptavidin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/SA-5010-2/pmc13119040-108-9-11?v=Vector+Laboratories
    Average 93 stars, based on 25 article reviews
    agarose streptavidin - by Bioz Stars, 2026-08
    93/100 stars

    Images

    1) Product Images from "Paraspeckles Are Associated with the Activation and Nuclear Localization of Unphosphorylated miR-34a"

    Article Title: Paraspeckles Are Associated with the Activation and Nuclear Localization of Unphosphorylated miR-34a

    Journal: Non-Coding RNA

    doi: 10.3390/ncrna12020012

    Mass spectrometry identifies nuclear paraspeckles as interacting partners of unphosphorylated miR-34 probes. ( A ) Workflow of sample isolation for mass spectrometry. Streptavidin sepharose beads were incubated with biotinylated miRNA mimics and mixed with sonicated whole-cell lysates. Samples were eluted by RNAse A treatment. The figure was created with Biorender. ( B ) Curation of mass spectrometry hits. Candidate proteins were identified by significance, uniqueness to the 5′OH miR-34a probe, and presence of known RNA-binding activity. ( C ) Characterization of isolated proteins. The total number of proteins isolated binding to the indicated probe is shown in parentheses, with the number of proteins unique to that sample or overlapping with other samples shown in the Venn diagram. ( D ) Gene ontology (GO) curation for cellular compartments performed on proteins identified in the 5′OH miR-34a eluates before and after curation (which was the removal of hits with a score below 20, p value > 0.05, non-unique proteins across three replicates, and non-RNA-binding proteins).
    Figure Legend Snippet: Mass spectrometry identifies nuclear paraspeckles as interacting partners of unphosphorylated miR-34 probes. ( A ) Workflow of sample isolation for mass spectrometry. Streptavidin sepharose beads were incubated with biotinylated miRNA mimics and mixed with sonicated whole-cell lysates. Samples were eluted by RNAse A treatment. The figure was created with Biorender. ( B ) Curation of mass spectrometry hits. Candidate proteins were identified by significance, uniqueness to the 5′OH miR-34a probe, and presence of known RNA-binding activity. ( C ) Characterization of isolated proteins. The total number of proteins isolated binding to the indicated probe is shown in parentheses, with the number of proteins unique to that sample or overlapping with other samples shown in the Venn diagram. ( D ) Gene ontology (GO) curation for cellular compartments performed on proteins identified in the 5′OH miR-34a eluates before and after curation (which was the removal of hits with a score below 20, p value > 0.05, non-unique proteins across three replicates, and non-RNA-binding proteins).

    Techniques Used: Mass Spectrometry, Isolation, Incubation, Sonication, RNA Binding Assay, Activity Assay, Binding Assay



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    Mass spectrometry identifies nuclear paraspeckles as interacting partners of unphosphorylated miR-34 probes. ( A ) Workflow of sample isolation for mass spectrometry. <t>Streptavidin</t> sepharose beads were incubated with biotinylated miRNA mimics and mixed with sonicated whole-cell lysates. Samples were eluted by RNAse A treatment. The figure was created with Biorender. ( B ) Curation of mass spectrometry hits. Candidate proteins were identified by significance, uniqueness to the 5′OH miR-34a probe, and presence of known RNA-binding activity. ( C ) Characterization of isolated proteins. The total number of proteins isolated binding to the indicated probe is shown in parentheses, with the number of proteins unique to that sample or overlapping with other samples shown in the Venn diagram. ( D ) Gene ontology (GO) curation for cellular compartments performed on proteins identified in the 5′OH miR-34a eluates before and after curation (which was the removal of hits with a score below 20, p value > 0.05, non-unique proteins across three replicates, and non-RNA-binding proteins).
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    Mass spectrometry identifies nuclear paraspeckles as interacting partners of unphosphorylated miR-34 probes. ( A ) Workflow of sample isolation for mass spectrometry. <t>Streptavidin</t> sepharose beads were incubated with biotinylated miRNA mimics and mixed with sonicated whole-cell lysates. Samples were eluted by RNAse A treatment. The figure was created with Biorender. ( B ) Curation of mass spectrometry hits. Candidate proteins were identified by significance, uniqueness to the 5′OH miR-34a probe, and presence of known RNA-binding activity. ( C ) Characterization of isolated proteins. The total number of proteins isolated binding to the indicated probe is shown in parentheses, with the number of proteins unique to that sample or overlapping with other samples shown in the Venn diagram. ( D ) Gene ontology (GO) curation for cellular compartments performed on proteins identified in the 5′OH miR-34a eluates before and after curation (which was the removal of hits with a score below 20, p value > 0.05, non-unique proteins across three replicates, and non-RNA-binding proteins).
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    Image Search Results


    Mass spectrometry identifies nuclear paraspeckles as interacting partners of unphosphorylated miR-34 probes. ( A ) Workflow of sample isolation for mass spectrometry. Streptavidin sepharose beads were incubated with biotinylated miRNA mimics and mixed with sonicated whole-cell lysates. Samples were eluted by RNAse A treatment. The figure was created with Biorender. ( B ) Curation of mass spectrometry hits. Candidate proteins were identified by significance, uniqueness to the 5′OH miR-34a probe, and presence of known RNA-binding activity. ( C ) Characterization of isolated proteins. The total number of proteins isolated binding to the indicated probe is shown in parentheses, with the number of proteins unique to that sample or overlapping with other samples shown in the Venn diagram. ( D ) Gene ontology (GO) curation for cellular compartments performed on proteins identified in the 5′OH miR-34a eluates before and after curation (which was the removal of hits with a score below 20, p value > 0.05, non-unique proteins across three replicates, and non-RNA-binding proteins).

    Journal: Non-Coding RNA

    Article Title: Paraspeckles Are Associated with the Activation and Nuclear Localization of Unphosphorylated miR-34a

    doi: 10.3390/ncrna12020012

    Figure Lengend Snippet: Mass spectrometry identifies nuclear paraspeckles as interacting partners of unphosphorylated miR-34 probes. ( A ) Workflow of sample isolation for mass spectrometry. Streptavidin sepharose beads were incubated with biotinylated miRNA mimics and mixed with sonicated whole-cell lysates. Samples were eluted by RNAse A treatment. The figure was created with Biorender. ( B ) Curation of mass spectrometry hits. Candidate proteins were identified by significance, uniqueness to the 5′OH miR-34a probe, and presence of known RNA-binding activity. ( C ) Characterization of isolated proteins. The total number of proteins isolated binding to the indicated probe is shown in parentheses, with the number of proteins unique to that sample or overlapping with other samples shown in the Venn diagram. ( D ) Gene ontology (GO) curation for cellular compartments performed on proteins identified in the 5′OH miR-34a eluates before and after curation (which was the removal of hits with a score below 20, p value > 0.05, non-unique proteins across three replicates, and non-RNA-binding proteins).

    Article Snippet: Lysates were cleared by incubating overnight with 100 μL agarose streptavidin (Vector, Malvern, PA, USA SA-5010).

    Techniques: Mass Spectrometry, Isolation, Incubation, Sonication, RNA Binding Assay, Activity Assay, Binding Assay

    KEY RESOURCES TABLE

    Journal: Cancer cell

    Article Title: A systems biology approach identifies FUT8 as a driver of melanoma metastasis

    doi: 10.1016/j.ccell.2017.05.007

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: Agarose Streptavidin , Vector lab , SA-5010.

    Techniques: Plasmid Preparation, Recombinant, Labeling, Membrane, Cell Viability Assay, Luciferase, Immunoprecipitation, Microarray, Mass Spectrometry, shRNA, Over Expression, Software