

Magnetic Bead Protein Purification Instrument
磁珠法蛋白纯化仪
- SKU PRP-0003
- Protein Purification
- CE (to be confirmed)
- ISO 9001 manufacturing (to be confirmed)
- IEC 61010-1 safety (to be confirmed)
Price on request — FOB / CIF quoted per order
Prices depend on configuration, quantity and destination port.
Key specifications
| Samples per run | 8–96 |
|---|---|
| Sample volume | 100–1,000 µL |
| Elution volume | 20–200 µL |
| Binding capacity | 0.5–5 mg target per mL bead suspension |
| Bead diameter | approx. 1–3 µm |
| Bead recovery | over 95% (typical) |
By Lab Manufacturers China Technical TeamLast reviewed Standards: USP <1057>, Ph. Eur. 2.2.29, Ph. Eur. 2.2.30
What is the Magnetic Bead Protein Purification Instrument?
A magnetic bead protein purification instrument captures tagged proteins on functionalised magnetic particles and collects them with a magnetic rod, allowing 8 to 96 small-scale purifications in parallel for expression screening and yield optimisation.
What is the Magnetic Bead Protein Purification Instrument?
A magnetic bead protein purification instrument captures tagged proteins on functionalised magnetic particles and collects them with a magnetic rod, allowing 8 to 96 small-scale purifications in parallel for expression screening and yield optimisation.
Overview
Functionalised beads carrying nickel, glutathione, streptavidin or antibody ligands bind the target from clarified lysate in a tube or deep-well plate. The instrument moves a magnetic rod into each well to collect the beads, removes the supernatant, washes and then elutes into a small volume. Because each well is independent, dozens of expression conditions, constructs or buffer compositions can be compared in one run, and the eluate can be analysed directly by SDS-PAGE or activity assay. Binding capacities are lower than for packed columns, typically 0.5–5 mg target per millilitre of bead suspension depending on ligand density, but the format is fast and needs little sample. Protocols take 30–90 minutes for a plate, and bead recovery above 95% is typical.
How does it work?
Chromatographic purification separates proteins by differences in a specific property. In affinity chromatography, a ligand such as immobilised nickel for histidine tags, glutathione for GST tags or protein A for antibodies retains the target while other proteins wash through, and a competing agent or a pH shift elutes it. Ion exchange uses charged resins so that proteins bind according to net charge at a chosen pH and elute under a salt gradient. Hydrophobic interaction chromatography binds proteins in high-salt buffers and elutes them as salt decreases. Size exclusion separates by hydrodynamic radius, with large molecules eluting first, which makes it useful for aggregate removal and buffer exchange. Magnetic bead methods bind the target on functionalised particles and collect them with a magnet, allowing parallel small-scale purification. Throughout, detectors measure absorbance at 280 nm and conductivity, and fractions are collected by peak.
What are the key features?
- Magnetic rod head for 8, 24, 48 or 96 parallel samples
- Bead chemistries for histidine, GST, biotin and antibody capture
- Programmable mixing, washing and elution steps
- Elution volumes as low as 20–50 µL for concentrated product
- Suitable for clarified lysate, supernatant and plasma samples
- Bead recovery above 95% with low carry-over between wells
What are the technical specifications?
A typical magnetic bead protein purification instrument configuration offers samples per run of 8–96, sample volume of 100–1,000 µL, elution volume of 20–200 µL, binding capacity of 0.5–5 mg target per mL bead suspension, bead diameter of approx. 1–3 µm and bead recovery of over 95% (typical). Values are indicative of the product class; the exact figures for each configuration are confirmed on the quotation and the calibration documents supplied with the instrument.
Which applications is it used for?
The Magnetic Bead Protein Purification Instrument is used in expression screening of many constructs, small-scale tagged protein purification, immunoprecipitation and pull-down assays and yield optimisation across buffer conditions. Across the wider Protein Purification class, laboratories also deploy it for recombinant protein purification for analysis, antibody purification from culture supernatant and aggregate and fragment removal before testing.
Which standards and certifications apply?
Relevant standards and methods include USP <1057>, Ph. Eur. 2.2.29, Ph. Eur. 2.2.30, IEC 61010-1, ISO 17025 and 21 CFR Part 11. Certification candidates for this model are CE, ISO 9001 manufacturing and IEC 61010-1 safety; each is to be confirmed for the specific configuration before shipment, and certificates are supplied only where they have been issued.
Maintain the system at a stable temperature, either at ambient with buffer equilibration or in a cold cabinet for labile proteins. Filter and degas all buffers to prevent pump damage and baseline noise, and choose buffers compatible with the resin and the downstream assay. Sanitise or clean-in-place the flow path between different proteins to avoid cross-contamination, and store columns in the recommended preservative. Monitor pressure throughout the run, because resin compression or a blocked line shows up first as rising pressure and then as distorted peaks. Keep tubing volumes small to limit peak broadening. Validate linearity, precision and carry-over before use in quality control, and retain chromatograms, gradients and fraction records so that a purification can be reproduced or investigated later.
How do I select the right Magnetic Bead Protein Purification Instrument?
Select a magnetic bead instrument when many small samples must be purified in parallel for screening, or when sample volume is limited. Specify sample capacity, bead chemistry, elution volume range, binding capacity and mixing control, and confirm that the elution buffer suits your downstream assay.
How does it compare with other Protein Purification variants?
Match the purification mode to the property you will exploit: a tag or known binding partner points to affinity chromatography, charge differences to ion exchange, salt-dependent hydrophobicity to hydrophobic interaction, and size differences to size exclusion. Then decide on scale and automation. Magnetic bead instruments suit parallel screening of 8–96 small samples where yield optimisation matters. Fast protein liquid chromatography systems with gradient pumps and fraction collectors handle method development and preparative work up to tens of milligrams per run. For screening many conditions quickly, perfusion chromatography allows short cycles at high flow rates. Check pressure rating, flow rate range, column and resin compatibility, gradient accuracy, fraction collector capacity and whether the software records methods and runs for traceability.
Full specifications
| Samples per run | 8–96 |
|---|---|
| Sample volume | 100–1,000 µL |
| Elution volume | 20–200 µL |
| Binding capacity | 0.5–5 mg target per mL bead suspension |
| Bead diameter | approx. 1–3 µm |
| Bead recovery | over 95% (typical) |
| Mixing modes | Vertical oscillation, programmable speed |
| Protocol time | approx. 30–90 min per plate |
| Plate formats | 96-deep-well plate or strip tubes |
| Dimensions (W x D x H) | approx. 350 x 450 x 400 mm |
Indicative values for this product class. Final specifications are confirmed on the quotation and in the calibration documents supplied with the instrument.
Applications
- Expression screening of many constructs
- Small-scale tagged protein purification
- Immunoprecipitation and pull-down assays
- Yield optimisation across buffer conditions
Key features
- Magnetic rod head for 8, 24, 48 or 96 parallel samples
- Bead chemistries for histidine, GST, biotin and antibody capture
- Programmable mixing, washing and elution steps
- Elution volumes as low as 20–50 µL for concentrated product
- Suitable for clarified lysate, supernatant and plasma samples
- Bead recovery above 95% with low carry-over between wells
Frequently asked questions about Magnetic Bead Protein Purification Instrument
Bead capacity is usually lower, around 0.5–5 mg of target per millilitre of bead suspension, because the particles have a smaller surface area per unit settled volume. Beads compensate with speed, low elution volume and parallel processing.
A small elution volume, such as 20–50 µL, concentrates the product so it can be loaded directly onto a gel or used in an assay without a concentration step. Very small volumes can reduce recovery if the beads are not fully resuspended.
Yes for manual workflows, where a magnetic rack or centrifugation pellets the beads so supernatant can be removed. The instrument automates the same steps and improves consistency when many samples are handled at once.
If the target carries a tag, start with affinity chromatography because it usually gives the highest purity in one step. If no tag is available, use ion exchange or hydrophobic interaction based on the protein's charge and hydrophobicity, followed by size exclusion for polishing.
A UV detector at 280 nm measures protein concentration in the eluate, and a conductivity monitor tracks the salt gradient. Together they show when the target elutes and allow fractions to be pooled, which is then confirmed by electrophoresis or activity assay.
Affinity purification removes most impurities but leaves aggregates, fragments and buffer components. Size exclusion separates molecules by hydrodynamic radius, so it removes aggregates and simultaneously exchanges the sample into the final formulation buffer.
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