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IDA Magnetic Beads

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1 μm BcMag™ IDA Magnetic Beads
Cat. No.  FF105

Unit Size  150 mg
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1 μm BcMag™ IDA Magnetic Beads
Cat. No.  FF106

Unit Size  300 mg
Order
5 μm BcMag™ IDA Magnetic Beads
Cat. No.  FF109

Unit Size  150 mg
Order
5 μm BcMag™ IDA Magnetic Beads
Cat. No.  FF110

Unit Size  300 mg
Order
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Cat. No.

Product Name

Unit Size

Order

FF105

1 μm BcMag™ IDA Magnetic Beads

150 mg

FF106

1 μm BcMag™ IDA Magnetic Beads

300 mg

FF109

5 μm BcMag™ IDA Magnetic Beads

150 mg

FF110

5 μm BcMag™ IDA Magnetic Beads

300 mg

Specification

Composition

Magnetic beads imobilized with IDA group on the surface

Number of Beads

~ 1.68 x 109 beads/mg (1μm beads)

~ 5 x 107 beads /mg (5μm beads)

Stability

Short Term (<1 hour): pH 3-11; Long-Term: pH 4-10

Temperature: 4°C -140°C; Most organic solvents

Magnetization

~40-45 EMU/g

Type of Magnetization

Superparamagnetic

Functional Group Density

1μm Magnetic Beads

~40 μMol NiSO4 / Gram of Beads

5μm Magnetic Beads

~32 μMol NiSO4 / Gram of Beads

Storage

Store at 4°C upon receipt. Do not freeze.

Description

BcMag™ IDA Magnetic Beads are 1μm and 5μm in diameter and highly uniform magnetic microspheres covalently immobilized with a high density of IDA (Iminodiacetic Acid) ligand designed for capture and purification of proteins from various sample types. The microspheres combine all the advantages of Immobilized metal ion affinity chromatography (IMAC) protein purification such phosphoproteins, phosphopeptides or his-tagged protein (low costs, simplicity, high specificity, and capacity) and magnetic properties to perform efficient manual or automatic quick high-throughput purification.

Workflow

BcMag™ IDA Magnetic Beads work perfectly as solid resin for various affinity purifications to refine molecules, cells, and parts of cells into purified fractions. Add the beads to a solution containing the target molecules, then mix, incubate, wash, and elute the target molecules

Workflow of magnetic beads for affinity purification

Features and Advantages

Easy to use

More efficient and low nonspecific binding

Stable covalent bond with minimal ligand leakage

Produces reusable matrices

Low nonspecific binding

Applications

To purify phosphoproteins and phosphopeptides, you can easily replace your current Al3+, Ga3+, or Fe3+ chelated resin or cartridge without needing to change your protocol or optimize the process. This method works for purification under both native and denaturing conditions and is effective for proteins of various sizes and with low expression rates.
Phosphopeptides are often found in complex proteolytic digest mixtures containing both phosphorylated and nonphosphorylated components, and immobilized Al3+, Ga3+, and Fe3+ ions are commonly used to selectively enrich them. NTA and IDA are popular ligands used in this process, and different ligand-metal ion combinations can yield varying purification results depending on the protein’s identity, impurity profile, and purification conditions.

How to choose different ligands in IMAC?

When selecting ligands for IMAC, NTA and IDA are the two most used options. NTA has a coordination number of 4 and is a tetravalent ligand, resulting in strong coordination of metal ions. In contrast, IDA has a coordination number of 3 and is a trivalent ligand. NTA typically provides higher binding specificity and lower metal ion leaching, while IDA has more non-specific binding and greater metal ion leaching. IDA can handle higher metal ion loading density and often requires a lower imidazole concentration in the eluent.

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