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Ech sepharose 4b beads

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ECH Sepharose 4B beads are a chromatography medium used for protein purification. They consist of cross-linked agarose beads with epichlorohydrin (ECH) groups, which can be used to couple various ligands for affinity chromatography. The beads have a bead size range of 45-165 μm and a medium porosity.

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Sepharose 4B (96 citations) Sepharose 4B beads (52 citations) Sepharose beads (43 citations) ECH Sepharose 4B (6 citations)

2 protocols using ech sepharose 4b beads

1

Affinity Purification of Histone Binders

Cited 1 time
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An amino propyl linker was added for coupling UNC063826 (link) to ECH sepharose 4B beads (General Electric cat# 17-0571-01). UNC0638 immobilized on sepharose beads were washed in Buffer D with 0.1% Triton-X100 twice before added into the nuclear extract. After incubation overnight, the beads was washed with 250mM KCl buffer (20mM HEPES pH7.9, 0.2mM EDTA, 250mM KCl, 20% Glycerol, 1mM PMSF, 1mM DTT and protease inhibitor cocktail) for five times. The pull-down products were eluted by boiling the beads in 2×SDS-PAGE loading buffer for 10 minutes. For histone peptide pull-down experiments, histone H3 N-tail peptides was synthesized with a biotin tag, then the peptide was conjugated to streptavidin beads and the pull-down experiment was carried out in a similar way as UNC0638 pull-down except for that the washing buffer was substituted by a low-stringent buffer containing 100mM KCl. The pull-down products were resolved by SDS-PAGE, either for immunoblotting or followed by in-gel tryptic digestion prior to MS analysis.
Liu C., Yu Y., Liu F., Wei X., Wrobel J.A., Gunawardena H.P., Zhou L., Jin J, & Chen X. (2014). A chromatin activity based chemoproteomic approach reveals a transcriptional repressome for gene-specific silencing. Nature communications, 5, 5733.
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2

Affinity Purification of Histone Binders

Cited 1 time
Check if the same lab product or an alternative is used in the 5 most similar protocols
An amino propyl linker was added for coupling UNC063826 (link) to ECH sepharose 4B beads (General Electric cat# 17-0571-01). UNC0638 immobilized on sepharose beads were washed in Buffer D with 0.1% Triton-X100 twice before added into the nuclear extract. After incubation overnight, the beads was washed with 250mM KCl buffer (20mM HEPES pH7.9, 0.2mM EDTA, 250mM KCl, 20% Glycerol, 1mM PMSF, 1mM DTT and protease inhibitor cocktail) for five times. The pull-down products were eluted by boiling the beads in 2×SDS-PAGE loading buffer for 10 minutes. For histone peptide pull-down experiments, histone H3 N-tail peptides was synthesized with a biotin tag, then the peptide was conjugated to streptavidin beads and the pull-down experiment was carried out in a similar way as UNC0638 pull-down except for that the washing buffer was substituted by a low-stringent buffer containing 100mM KCl. The pull-down products were resolved by SDS-PAGE, either for immunoblotting or followed by in-gel tryptic digestion prior to MS analysis.
Liu C., Yu Y., Liu F., Wei X., Wrobel J.A., Gunawardena H.P., Zhou L., Jin J, & Chen X. (2014). A chromatin activity based chemoproteomic approach reveals a transcriptional repressome for gene-specific silencing. Nature communications, 5, 5733.
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