Co-IDA Agarose 500 mL - S5370.0500

Package Size: 500 mL Genaxxon Co-IDA-Agarose consists of crosslinked agarose, to which iminodiacetic acid (IDA) charged with Co2+ ions is covalently bound. In processing recombinant fusion proteins from eukaryotes or in the case of special protein complexes, Genaxxon Co-IDA Agarose should always be used offering the possibility of higher protein purity levels. Both metal ions feature differing spatial properties and electronic binding potentials. While Co2+ binds only domains adjacent to residual histidine and is thus highly selective for 6×histidine-tagged fusion proteins, Ni2+ ions are less specific and can bind residual histidine outside the polyhistidine tag, which may result in higher contamination with foreign proteins. Genaxxon Co-IDA Agarose fulfils the most rigorous quality standards, featuring high pH and chemical stability and enabling purification directly from raw lysates. Genaxxon Co-IDA Agarose can be regenerated several times with cobalt chloride solution for re-use. Co-IDA-Agarose (Low Pressure) - the most effective method for the separation of 6-His tagged fusion proteins. Highlights: ideal for grafity-flow and batch procedures - no expensive purification system necessary - consistent performance - for native and denaturing conditions - cheap! The Genaxxon Co-IDA Agarose consists of 4% cross-linked Agarose, covalently bound to Iminodiacetic acid loaded with Co2+-ions. Binding capacity: up to 10mg 6xHis tagged fusion protein per mL Agarose. Application: Affinity chromatography of 6-His tagged fusion proteins in batch or grafity flow procedure. Co-IDA Agarose is supplied as buffered suspension in 20% Ethanol.

Co-IDA Agarose Manual / Protocol (pdf)

Technical Data: 4% cross-linked Agarose, grain size: 45 – 165µm; MW: 7×10E4 – 2×10E7; max. pressure: 0.18 bar (2.6 psi); 20 – 40 µmol Me2+ / mL resin; pH-stability: 2–14 (short term), 3–13 (long term storage); regenerable.

Shipping / Storing Information: shipped at RT, store at +2°C to +8°C

Productnumber: S5370.0500

changedate: 11.6.2011

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