Ni Sepharose 6 Fast Flow His

Ni Sepharose 6 Fast Flow is an effective chromatography resin designed specifically for the purification of his-tagged proteins. Its high binding capacity makes it suitable for use in both process scale and research scale applications.
At process scale, this resin is capable of purifying large quantities of histidine-tagged and untagged recombinant proteins. It provides robust performance and can be used in batch mode, with gravity flow, or when scalability is a priority.
For research scale applications, Ni Sepharose 6 Fast Flow offers a binding capacity of 40 mg his-tag protein/mL resin. It can be used in batch mode, with gravity flow, or with a chromatography system, depending on the specific requirements of the experiment.
In addition to its exceptional performance, this resin meets the demands of the industry by providing security of supply and regulatory support. It is available as both bulk resin and prepacked columns, enabling flexibility in purification methods.
The excellent flow properties of Ni Sepharose 6 Fast Flow allow for high flow rates without compromising performance. This resin combines high binding capacity with efficient chromatography, ensuring optimal purification results for his-tagged proteins.
Ni Sepharose 6 Fast Flow consists of cross-linked agarose beads modified with a chelating ligand immobilized to the base matrix. These beads are precharged with nickel ions, facilitating the selective binding of his-tagged proteins.
Overall, Ni Sepharose 6 Fast Flow is a reliable and versatile chromatography resin that offers excellent performance, high binding capacity, and scalability for the purification of his-tagged proteins.Could you please provide me with information on the particle size and the resin used for the purification of the Tidine-tagged protein?The chromatography medium in question boasts a matrix of 6% cross-linked agarose with a particle size of around 90 µm. The D50V particle size range is between 45 µm to 165 µm, making it an efficient filtration medium. Additionally, its binding capacity per mL is noteworthy, allowing for reliable and effective separations.The metal ion capacity of the histidine-tagged protein is around 15 µmol Ni2+/mL, and it contains approximately 40 mg of the protein. These details are important to remember when working with this particular protein. By being aware of its specific properties, researchers can more effectively use this protein in experiments or other applications.Important Note: When using resins, it is crucial to operate them within a specific pH range to avoid any significant changes in their functionality. Note :Ni² plus stripping medium 2-14 Pressure/Flow Specification 250-400 cm/h, 100 kPa, XK 50/60 column, bed height 25 cm Storage Note :Ni² + stripping medium Stable in commonly used aqueous buffers - 0.1m HCl, 0.1m NaOH, 8 M Ureaabsin For Cytiva packaging (formerly GE Healthcare) packaging

Approximately 0.1~0.4 mg/ml of each protein in the buffer (20 mM Tris-phosphate, pH 7.5 at 25°C), 2 % SDS, 0.2 mM Dithiothreitol, 3.6 M Urea, and 15 % (v/v) Glycerol).

1. Please stand at room temperature to melt before use;
2. Mix gently and thoroughly. Take 5μL of the product and conduct SDS-PAGE simultaneously with the experimental sample.
3. The unused rainbow predyeing marker shall be preserved according to the storage conditions.

1. This product can be used directly without heating.
2. Change the electrophoresis buffer and use the newly prepared gel in time to avoid affecting the electrophoresis results.
3. This product can be stably stored at 4°C for 3 months. If you need to store it longer, please store it at -20°C.
4. In order to avoid pollution, after opening, can be divided into small tubes according to need, it is suggested that each tube is packed into 10μl, -20° C storage, take one tube at a time, to avoid repeated freezing and thawing.

Under suggested conditions, Prestained Protein Ladder resolves 12 major bands in 15% SDS-PAGE (Trisglycine buffer) and after Western blotting to nitrocellulose membrane.