High Affinity Ni-Charged Resin FF

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.

价格	￥403 在线订购包邮(港澳台除外)
产品编号	L00666-5
规格	5 ml Resin (Total 10 ml) 25 ml Resin (Total 50 ml) 100 ml Resin (Total 200 ml) 大单询价
数量
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Description

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.

图例

Figure 1. Schematic diagram of the chemical structure of Ni IDA Resin, Ni IDA Resin FF, Hi affinity Ni-Charged Resin and Hi affinity Ni-Charged Resin FF »

For research and manufacturing use. Direct human use, including taking orally and injection are forbidden.

相关文献

1. Wenhua Kuang, et al. Structure and function of the nairovirus cap-snatching endonuclease. Nucleic Acids Research. (2026-01)
2. Yingjie Lei, et al. Discovery of a Serine-Directed Chemical Reaction for Site-Specific Protein Modification via Phage Display Screening. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION. (2025-10)
3. Yin Li, et al. β-propeller protein-associated neurodegeneration protein WDR45 regulates stress granule disassembly via phase separation with Caprin-1. Nature Communications. (2025-06)
4. Ruofan Hu, et al. Dual-Targeted Protein MRI Contrast Agent for Early. Aggregate. (2024-12)
5. Deyu Zhang , et al. Identification of FBLL1 as a neuron-specific RNA 2'-O-methyltransferase mediating neuronal differentiation. Proc Natl Acad Sci U S A. (2024-11)