Ni-IDA Agarose 10 mL - S5353.0010

Package Size: 10 mL Nickel-loaded agaroses are the most frequently used products for the efficient purification of 6×histidine-tagged recombinant fusion proteins. Because Ni2+ ions show high affinity for 6×histidine-tagged fusion proteins, extremely high yields result from purification of these fusion proteins from the lysates. However, if purification takes place from lysates containing foreign protein chains with repeated histidine elements, selectivity with respect to 6×histidine-tagged fusion protein decreases as non-tagged histidine-containing proteins increasingly also bind to the Ni-IDA agarose. In this case the use of Genaxxon Co-IDA Agarose is recommend (cat#: S535k), which features far higher selectivity with respect to 6×histidine-tagged fusion protein. Genaxxon Ni-IDA Agarose has high chemically and pH stability and enables purification directly from raw lysates. Genaxxon Ni-IDA Agarose can be regenerated several times with nickel sulfate solution for re-use. Ni-IDA-Agarose (Low Pressure) - a highly efficient and favorable way 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 Ni-IDA Agarose consists of 4% cross-linked Agarose, covalently bound to Iminodiacetic acid loaded with Ni2+-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. Ni-IDA Agarose is supplied as buffered suspension in 20% Ethanol.

Ni-IDA Agarose Manual / Protocol (pdf)

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

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

Productnumber: S5353.0010

changedate: 11.6.2011

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