GenScript High Affinity Ni-Charged Resin FF is an 6% highly cross-linked agarose medium covalently coupled to a chelating agent that binds Ni²⁺ by four coordination sites for high-affinity purification of polyhistidine-tagged recombinant proteins.
High Affinity Ni-Charged Resin FF has low Ni²⁺ leakage, high protein-binding capacity and stability, and is compatible with a wide range of additives used in protein purification. This makes High Affinity Ni Charged Resin FF the excellent choice for high performance purification of polyhistidine-tagged proteins.

Characteristics of High Affinity Ni-Charged Resin FF

Matrix spherical	6% highly cross-linked agarose
Average particle size	90 µm (45-165 µm)
Dynamic Binding capacity1	≥50 mg of histidine-tagged protein /mL settled resin
Storage solution	20% ethanol
Storage temperature	stored at 2-8 °C; DO NOT FREEZE

¹ Dynamic binding capacity conditions:
Sample: 5 mg/mL (histidine)₆-tagged pure proteins (M_r 43 000) in binding buffer (capacity at 10%  Breakthrough)
Column volume: 1 mL 
Retention time: 3min
Flow rate: 0.333 mL/min
Binding buffer: 20 mM sodium phosphate, 500 mM NaCl, 10 mM imidazole, pH 7.4
Elution buffer: 20 mM sodium phosphate, 500 mM NaCl, 250 mM imidazole, pH 7.4 
Note: Dynamic binding capacity is protein-dependent.

Reagents Compatible with High Affinity Ni-Charged Resin FF

Reducing agents	Denaturants	Detergents	Salts	Others
1 mM DTT	6 M Gua·HCl†	2% Triton X-100	4 M MgCl2	50% glycerol
20 mM β-ME	8 M Urea†	2% Tween 20	5 mM CaCl2	20% ethanol
5mM TCEP-HCl	——	50% glycerin	2 M NaCl	1 mM EDTA‡
10 mM reduced glutathione	——	——	100mM Na2SO4	60 mM citrate†

^† Tested for 1 week at 40°C. 
^‡ The strong chelator EDTA has been used successfully in some cases at 1 mM. Generally, chelating agents should be used with caution (and only in the sample, not in buffers). Any metal ion stripping may be counteracted by addition of a small excess of MgCl2 before centrifugation/filtration of the sample. Note that stripping effects may vary with applied sample volume.