Description
GoldBio's Nickel NTA Magnetic Agarose Beads are high-capacity magnetic affinity chromatography beads designed for rapid purification of His-tagged recombinant proteins from complex samples.
By combining nitrilotriacetic acid (NTA) nickel chelation chemistry with a magnetic agarose support, the beads enable efficient isolation of His-tagged proteins without the need for centrifugation or gravity-flow columns. Magnetic separation simplifies washing and elution steps, making the beads particularly well suited for small-volume purifications, high-throughput sample processing, and protein screening applications.
The immobilized NTA ligand coordinates nickel ions through four binding sites, providing greater metal ion stability and lower nickel leaching than IDA-based resins while maintaining high specificity for engineered polyhistidine tags.
His-tagged proteins can be purified under either native conditions to preserve biological activity or denaturing conditions for recovery from inclusion bodies and other insoluble protein fractions.
The magnetic format allows rapid buffer exchange with minimal sample handling while maintaining compatibility with bacterial, yeast, insect, and mammalian expression systems.
With a binding capacity greater than 75 mg of His-tagged protein per mL of gel, Nickel NTA Magnetic Agarose Beads are suitable for applications ranging from routine recombinant protein purification to protein interaction studies, structural biology, enzyme characterization, and high-throughput expression screening.
GoldBio's Nickel NTA Magnetic Agarose Beads are supplied as a ready-to-use suspension, providing you with a convenient, reproducible solution for efficient protein purification while supporting a wide range of downstream biochemical and molecular biology applications.
Suspension: Nickel NTA Magnetic Beads are supplied as a 5% suspension of magnetic beads in 20% ethanol (each 1 ml of suspension contains 50 μl of magnetic beads).
Loading Capacity (μmol me2+/ml gel): >20 µmol/ ml gel
Binding Capacity: >75 mg His-tagged protein/ ml gel
Note: GoldBio recommends using Nickel NTA resins in the presence of elevated levels of reducing agents in order to ensure optimal purification of your target protein. Nickel IDA resins may show some discoloration in reaction with low levels of reducing agents but are still functional at low levels of reducing agents (≤5mM DTT).
Common Applications
(Click each for more information)
Rapid Purification of His-Tagged Recombinant Proteins
-
Purpose: To selectively isolate recombinant proteins containing engineered polyhistidine (His) tags from crude lysates and other biological samples.
-
How It Works: Histidine residues within the affinity tag coordinate with nickel ions immobilized on the NTA agarose matrix. Magnetic separation allows the beads to be rapidly isolated during wash and elution steps without centrifugation or chromatography columns.
-
Applications: Recombinant protein purification, enzyme isolation, antibody fragment purification, protein production, and routine laboratory protein purification.
Bornhorst, J. A., & Falke, J. J. (2000). Purification of proteins using polyhistidine affinity tags. Methods in Enzymology, 326, 245–254. https://doi.org/10.1016/S0076-6879(00)26058-8
High-Throughput Purification and Expression Screening
-
Purpose: To rapidly purify multiple recombinant protein samples simultaneously during protein expression optimization and screening experiments.
-
How It Works: The magnetic agarose support enables rapid parallel washing and elution using magnetic racks or automated liquid-handling systems, eliminating column packing and centrifugation steps.
-
Applications: Expression optimization, clone screening, recombinant protein production, automation, and parallel purification experiments.
Arnau, J., Lauritzen, C., Petersen, G. E., & Pedersen, J. (2006). Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expression and Purification, 48(1), 1–13. https://doi.org/10.1016/j.pep.2005.12.002
Purification Under Native or Denaturing Conditions
-
Purpose: To recover soluble recombinant proteins while preserving biological activity or to purify His-tagged proteins from insoluble inclusion bodies.
-
How It Works: The strong interaction between His tags and immobilized nickel remains effective in both native buffers and denaturing solutions containing urea or guanidine hydrochloride, allowing flexible purification strategies depending on protein solubility.
-
Applications: Purification of soluble proteins, inclusion body recovery, protein refolding studies, and recombinant protein production.
Block, H., Maertens, B., Spriestersbach, A., et al. (2009). Immobilized-metal affinity chromatography (IMAC): A review. Methods in Enzymology, 463, 439–473. https://doi.org/10.1016/S0076-6879(09)63027-5
Protein-Protein Interaction Studies
-
Purpose: To isolate His-tagged bait proteins together with associated binding partners for characterization of molecular interactions.
-
How It Works: His-tagged proteins are immobilized on the Nickel NTA beads, allowing associated binding partners to remain bound during washing and to be analyzed following elution.
-
Applications: Pull-down assays, interaction mapping, protein complex isolation, and binding studies.
Porath, J. (1992). Immobilized metal ion affinity chromatography. Protein Expression and Purification, 3(4), 263–281. https://doi.org/10.1016/1046-5928(92)90001-D
Purification of Recombinant Proteins for Structural and Functional Characterization
-
Purpose: To obtain highly purified recombinant proteins suitable for downstream biochemical and structural analyses.
-
How It Works: Selective enrichment of His-tagged proteins reduces contaminating host proteins, producing purified samples appropriate for analytical techniques requiring high protein purity.
-
Applications: Enzyme characterization, protein structural studies, NMR spectroscopy, functional assays, and biophysical studies.
Porath, J. (1992). Immobilized metal ion affinity chromatography. Protein Expression and Purification, 3(4), 263–281. https://doi.org/10.1016/1046-5928(92)90001-D
Key Benefits
· Rapid Magnetic Separation: Eliminates centrifugation and chromatography columns, simplifying binding, washing, and elution steps while reducing sample handling.
· High Binding Capacity: Binds more than 75 mg of His-tagged protein per mL of gel, supporting efficient purification from both analytical and preparative samples.
· High Specificity with Low Metal Ion Leaching: NTA chemistry provides stronger nickel chelation than IDA-based resins, improving metal ion stability and reducing nickel leaching during purification.
· Compatible with Native and Denaturing Purification: Enables purification of soluble recombinant proteins while also supporting recovery of His-tagged proteins from inclusion bodies using denaturing agents.
· Ideal for Parallel Sample Processing: The magnetic format allows multiple samples to be processed simultaneously, making the beads well suited for expression screening, pull-down assays, and high-throughput purification.
Storage/Handling
Store at 4°C. Do not freeze.
Powered by Bioz