ROTI®Garose-His/Co Beads, 100 ml

For the isolation of high yields of highly pure His-tagged proteins under non-reducing conditions.

Immobilized metal ion affinity chromatography (IMAC) still is the most widely used method to obtain high yield of very pure proteins with reasonable effort.
ROTI^®Garose His/Co Beads and ready-to-use columns offer the perfect solution for your specific applications in the field of benchtop column chromatography, for protein isolation in batch processes or under medium pressures (MPLC, FPLC). Depending on the product, our beads are optimally suited for low or high flow rates or when small or large sample volumes are to be purified. The ready-to-use columns and cartridges offer you the perfect solution for fast and easy purification of His-tag proteins from total lysate.

The matrix of ROTI^®Garose His/Co products consists of crosslinked and beaded 6 % agarose, IDA-conjugated and charged with divalent Cobalt ions. Cobalt chelates recognize two exposed, vicinal histidines with superior specificity and good affinity, resulting in acceptable to good recovery rates only, but yielding proteins of superior purity. This matrix is, therefore, the perfect choice if extremely pure proteins are required, or if hard-to-separate proteins shall be isolated. ROTI^®Garose His/Co beads result in eluates with considerably low metal contamination.

The tridentate IDA cross-linker provides easy elution with low amounts of imidazole. Additionally, ROTI^®Garose Beads may repeatedly be regenerated, making them very cost-effective.
The Matrix is stable in all commonly used reagents including denaturing reagents (like 8 M urea, 6 M guanidinium hydrochloride, 5 mM DTT).
For insulation under reducing conditions we recommend ROTI^®Garose-His/Ni NTA beads.

Cobalt charged IDA-agarose beads for low pressure affinity chromatography.
50 % bead suspension in 20 % ethanol.

Perfect choice if extremely pure proteins are required, or if hard-to-separate proteins shall be isolated.

May be autoclaved at 121 °C for 30 mins.