High Affinity Ni-Charged Resin

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GenScript High Affinity Ni-Charged Resin is an 4% 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 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 the excellent choice for high performance purification of polyhistidine-tagged proteins.

产品编号	L00223
规格	大单询价

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产品概述产品属性

产品概述

Product description

GenScript High Affinity Ni-Charged Resin is an 4% 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 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 the excellent choice for high performance purification of polyhistidine-tagged proteins.

Key Features

● low Ni²⁺ leakage
● high protein-binding capacity and stability
● compatible with a wide range of additives used in protein purification

产品属性

Formulation

50% slurry in 1 × PBS containing 20% ethanol

Matrix

4% cross-linked agarose

Average Particle Size

90 μm (45-165 μm)

Ligand

Nickel

Binding Capacity

≥20 mg of 6xHis-tagged protein (27 kDa) /ml settled resin

Reagents Compatibility

Denaturants	Detergents	Reducing Agents	Salts	Others
6 M Gu·HCl	2% Triton X-100	20 mM β-ME	4 M MgCl₂	50% glycerol
8 M Urea	2% Tween 20	1 mM DTT	5 mM CaCl₂	20% ethanol
——	1% CHAPS	——	2 M NaCl	1 mM EDTA

Application

1. Purification of polyhistidine-tagged proteins under native conditions.
2. Purification of polyhistidine-tagged proteins from E. coli under denaturing conditions.

Storage

2-8 °C; DO NOT FREEZE

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

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2. Binita Shah; Moritz Hunkeler; Ariana Bratt; Hong Yue; Isabella Jaen Maisonet; Eric S. Fischer; Sara J. Buhrlage, et al. Structural basis of VCP-VCPIP1-p47 ternary complex in Golgi maintenance. Nature Communications. (2021-02)
3. Binita Shah; Moritz Hunkeler; Ariana Bratt; Hong Yue; Isabella Jaen Maisonet; Eric S. Fischer; Sara J. Buhrlage, et al. Structural basis of VCP-VCPIP1-p47 ternary complex in Golgi maintenance. Nature Communications. (2021-02)
4. Binita Shah; Moritz Hunkeler; Ariana Bratt; Hong Yue; Isabella Jaen Maisonet; Eric S. Fischer; Sara J. Buhrlage, et al. Structural basis of VCP-VCPIP1-p47 ternary complex in Golgi maintenance. Nature Communications. (2021-02)
5. Binita Shah; Moritz Hunkeler; Ariana Bratt; Hong Yue; Isabella Jaen Maisonet; Eric S. Fischer; Sara J. Buhrlage, et al. Structural basis of VCP-VCPIP1-p47 ternary complex in Golgi maintenance. Nature Communications. (2021-02)
6. View Runting Li, et al. Characterization of Isoforms of the Ovine Granulocyte Colony Stimulating Factor. biorxiv. (2019)
7. HsuKuan-Wei, et al. The synergy between RSC， Nap1 and adjacent nucleosome in nucleosome remodeling. Biochim Biophys Acta Gene Regul Mech. (2019)
8. Xu X, et al. Obtaining a mutant of Bacillus amyloliquefaciens xylanase A with improved catalytic activity by directed evolution. Enzyme Microb Technol. (2016-05)