ALADDIN SCIENTIFIC
1 μm MPSE-SAX Solid Phase Magnetic Beads (C008B-267094)
1 μm MPSE-SAX Solid Phase Extraction Magnetic Beads (Strong Anion Exchange) are composed of silica, polystyrene, and iron oxide nanoparticles, enabling rapid separation of proteins and peptides from complex biological samples (e.g.
1 μm MPSE-SAX Solid Phase Extraction Magnetic Beads (Strong Anion Exchange) are composed of silica, polystyrene, and iron oxide nanoparticles, enabling rapid separation of proteins and peptides from complex biological samples (e.g., serum, plasma, urine). This product can bind weakly cationic species in samples that typically cannot be captured by weak anion exchange magnetic beads. Solid phase extraction magnetic beads combine solid phase extraction technology with magnetic separation technology and are widely used in sample pretreatment, with applications in environmental monitoring for pollutant detection, metabolite extraction in pharmaceutical analysis, food safety testing, and extraction of toxins or pesticide residues, among others. The bead surface is functionalized with specific functional groups, allowing selective adsorption of targets through hydrophobic, electrostatic, or specific interactions. Sample preparation is rapid and straightforward, and the beads can be conveniently and quickly separated using an external magnetic field, thereby improving the efficiency and effectiveness of sample pretreatment.Cat. No.M1520788Product Name1 μm MPSE-SAX Solid Phase Extraction Magnetic BeadsConcentration10 mg/mLParticle SizeApprox. 1 μmSurface PotentialApprox. -20 mVMagnetic ContentApprox. 35% – 45%Dispersion SolventPure WaterInstructions for UseNote: Technically, it is challenging to design a universal protocol for protein purification using 1 μm MPSE-SAX (Strong Anion Exchange) Solid Phase Extraction Magnetic Beads. The following protocol is an example of using 1 μm MPSE-SAX (Strong Anion Exchange) Solid Phase Extraction Magnetic Beads for the fractionation and purification of protein and/or peptide mixtures. For optimal results, users may adapt alternative binding, washing, and elution buffers based on this protocol, while determining the optimal bead quantity and elution volume for each application through titration experiments.1. Selecting the Appropriate Ion Exchange Magnetic BeadsCharged proteins or peptides bind to matrices of the opposite charge. If the isoelectric point (pI) of the target protein or peptide is higher than the pH of the buffer solution, the protein or peptide surface carries a positive charge. In this case, anion exchange magnetic beads, MPSE-WAX (Weak Anion Exchange) or MPSE-SAX (Strong Anion Exchange), should be selected for purification. If the isoelectric point of the target protein or peptide is lower than the pH of the buffer solution, the protein or peptide surface carries a negative charge, and cation exchange magnetic beads, such as 1 μm MPSE-WCX (Weak Cation Exchange) or MPSE-SCX (Strong Cation Exchange), should be selected for purification.2. Selecting the Appropriate Buffer SolutionsBinding/Washing Buffer: The pH of the binding/washing buffer should differ from the isoelectric point of the protein or peptide by at least one pH unit.Elution Buffer: To elute the target protein or peptide from the beads, users should gradually optimize the elution conditions for their specific application. Elution can be performed using solutions with increasing salt concentrations (0.1–1.0 M NaCl), using 0.5% trifluoroacetic acid (TFA), or by changing the pH of the elution buffer (e.g., 20 mM Tris pH 7.0, followed by 20 mM MES pH 6.0, followed by 20 mM MES pH 5.0, 50 mM citrate buffer pH 4.0) for stepwise elution.Reference Experimental ProcedurePre-treatment Buffer: 50 mM PB solution containing 1 M NaCl, pH 8.0.Binding/Washing Buffer: 50 mM PB solution containing 20 mM NaCl, pH 8.0.A. Bead PreparationThoroughly disperse the bead solution. Transfer 100 μL of magnetic beads (10 mg/mL) into a centrifuge tube. Place the tube on a magnetic separator for 1–3 minutes to allow complete magnetic separation, then remove the supernatant.Add 200 μL of pre-treatment buffer to fully resuspend the beads. Allow the tube to equilibrate at room temperature for 2–3 minutes. Place the tube on the magnetic separator for 1–3 minutes for complete magnetic separation, then remove the supernatant.Repeat step 2 once.Remove the tube from the magnetic separator. Resuspend the beads thoroughly in 200 μL of binding/washing buffer. Place the tube on the magnetic separator for 1–3 minutes for complete magnetic separation, then remove the supernatant.Repeat step 4 once.Resuspend the beads thoroughly in binding/washing buffer.B. Protein BindingAdd the sample containing 60 μg of protein or peptide (Note: For optimal results, the sample should be suspended in binding/washing buffer) to the centrifuge tube containing the washed beads from Step A-6. If necessary, adjust the total volume to 200 μL with binding/washing buffer. Mix the beads thoroughly by pipetting and incubate at room temperature for 2–3 minutes.Place the centrifuge tube on the magnetic separator for 1–3 minutes for complete magnetic separation, then aspirate and discard the supernatant.Remove the tube from the magnetic separator. Wash the beads with 200 μL of binding/washing buffer. Place the tube on the magnetic separator for 1–3 minutes for complete magnetic separation, then remove the supernatant.Repeat step 3 three times.C. ElutionRemove the tube from the magnetic separator. Resuspend the beads in 200 μL of binding/washing buffer and incubate at room temperature for 3 minutes.Place the centrifuge tube on the magnetic separator for 1–3 minutes for complete magnetic separation. Transfer the supernatant containing the eluted protein to a new centrifuge tube for downstream analysis.Frequently Asked Questions and TroubleshootingProblemPossible CauseSuggestionLow YieldInsufficient ionic interaction; pH of binding/washing buffer is higher than the isoelectric point of the target protein or peptideOptimize the sodium chloride concentration in the binding/washing buffer; Optimize the pH of the binding bufferPoor ElutionIonic interaction is too strongOptimize the sodium chloride concentration; Optimize the pH of the elution buffer; Use weak anion exchange magnetic beadsPoor Purification EfficiencyInsufficient washingIncrease the number of wash steps before each elution stepPoor Purification EfficiencyPresence of proteins or peptides with isoelectric points similar to the target protein or peptideOptimize the sodium chloride concentration or pH of the elution bufferPrecautionsEnsure the magnetic beads are thoroughly mixed before use to prevent changes in concentration during pipetting. Avoid prolonged ultrasonication, which may damage the bead surface.
Specifications & Purity: 1 μm MPSE-SAX Solid Phase Extraction Magnetic Beads (Strong Anion Exchange) are composed of silica, polystyrene, and iron oxide nanoparticles, enabling rapid separation of proteins and peptides from complex biological samples (e.g., serum, plasma, urine). This product can bind weakly cationic species in samples that typically cannot be captured by weak anion exchange magnetic beads. Solid phase extraction magnetic beads combine solid phase extraction technology with magnetic separation technology and are widely used in sample pretreatment, with applications in environmental monitoring for pollutant detection, metabolite extraction in pharmaceutical analysis, food safety testing, and extraction of toxins or pesticide residues, among others. The bead surface is functionalized with specific functional groups, allowing selective adsorption of targets through hydrophobic, electrostatic, or specific interactions. Sample preparation is rapid and straightforward, and the beads can be conveniently and quickly separated using an external magnetic field, thereby improving the efficiency and effectiveness of sample pretreatment.Cat. No.M1520788Product Name1 μm MPSE-SAX Solid Phase Extraction Magnetic BeadsConcentration10 mg/mLParticle SizeApprox. 1 μmSurface PotentialApprox. -20 mVMagnetic ContentApprox. 35% – 45%Dispersion SolventPure WaterInstructions for UseNote: Technically, it is challenging to design a universal protocol for protein purification using 1 μm MPSE-SAX (Strong Anion Exchange) Solid Phase Extraction Magnetic Beads. The following protocol is an example of using 1 μm MPSE-SAX (Strong Anion Exchange) Solid Phase Extraction Magnetic Beads for the fractionation and purification of protein and/or peptide mixtures. For optimal results, users may adapt alternative binding, washing, and elution buffers based on this protocol, while determining the optimal bead quantity and elution volume for each application through titration experiments.1. Selecting the Appropriate Ion Exchange Magnetic BeadsCharged proteins or peptides bind to matrices of the opposite charge. If the isoelectric point (pI) of the target protein or peptide is higher than the pH of the buffer solution, the protein or peptide surface carries a positive charge. In this case, anion exchange magnetic beads, MPSE-WAX (Weak Anion Exchange) or MPSE-SAX (Strong Anion Exchange), should be selected for purification. If the isoelectric point of the target protein or peptide is lower than the pH of the buffer solution, the protein or peptide surface carries a negative charge, and cation exchange magnetic beads, such as 1 μm MPSE-WCX (Weak Cation Exchange) or MPSE-SCX (Strong Cation Exchange), should be selected for purification.2. Selecting the Appropriate Buffer SolutionsBinding/Washing Buffer: The pH of the binding/washing buffer should differ from the isoelectric point of the protein or peptide by at least one pH unit.Elution Buffer: To elute the target protein or peptide from the beads, users should gradually optimize the elution conditions for their specific application. Elution can be performed using solutions with increasing salt concentrations (0.1–1.0 M NaCl), using 0.5% trifluoroacetic acid (TFA), or by changing the pH of the elution buffer (e.g., 20 mM Tris pH 7.0, followed by 20 mM MES pH 6.0, followed by 20 mM MES pH 5.0, 50 mM citrate buffer pH 4.0) for stepwise elution.Reference Experimental ProcedurePre-treatment Buffer: 50 mM PB solution containing 1 M NaCl, pH 8.0.Binding/Washing Buffer: 50 mM PB solution containing 20 mM NaCl, pH 8.0.A. Bead PreparationThoroughly disperse the bead solution. Transfer 100 μL of magnetic beads (10 mg/mL) into a centrifuge tube. Place the tube on a magnetic separator for 1–3 minutes to allow complete magnetic separation, then remove the supernatant.Add 200 μL of pre-treatment buffer to fully resuspend the beads. Allow the tube to equilibrate at room temperature for 2–3 minutes. Place the tube on the magnetic separator for 1–3 minutes for complete magnetic separation, then remove the supernatant.Repeat step 2 once.Remove the tube from the magnetic separator. Resuspend the beads thoroughly in 200 μL of binding/washing buffer. Place the tube on the magnetic separator for 1–3 minutes for complete magnetic separation, then remove the supernatant.Repeat step 4 once.Resuspend the beads thoroughly in binding/washing buffer.B. Protein BindingAdd the sample containing 60 μg of protein or peptide (Note: For optimal results, the sample should be suspended in binding/washing buffer) to the centrifuge tube containing the washed beads from Step A-6. If necessary, adjust the total volume to 200 μL with binding/washing buffer. Mix the beads thoroughly by pipetting and incubate at room temperature for 2–3 minutes.Place the centrifuge tube on the magnetic separator for 1–3 minutes for complete magnetic separation, then aspirate and discard the supernatant.Remove the tube from the magnetic separator. Wash the beads with 200 μL of binding/washing buffer. Place the tube on the magnetic separator for 1–3 minutes for complete magnetic separation, then remove the supernatant.Repeat step 3 three times.C. ElutionRemove the tube from the magnetic separator. Resuspend the beads in 200 μL of binding/washing buffer and incubate at room temperature for 3 minutes.Place the centrifuge tube on the magnetic separator for 1–3 minutes for complete magnetic separation. Transfer the supernatant containing the eluted protein to a new centrifuge tube for downstream analysis.Frequently Asked Questions and TroubleshootingProblemPossible CauseSuggestionLow YieldInsufficient ionic interaction; pH of binding/washing buffer is higher than the isoelectric point of the target protein or peptideOptimize the sodium chloride concentration in the binding/washing buffer; Optimize the pH of the binding bufferPoor ElutionIonic interaction is too strongOptimize the sodium chloride concentration; Optimize the pH of the elution buffer; Use weak anion exchange magnetic beadsPoor Purification EfficiencyInsufficient washingIncrease the number of wash steps before each elution stepPoor Purification EfficiencyPresence of proteins or peptides with isoelectric points similar to the target protein or peptideOptimize the sodium chloride concentration or pH of the elution bufferPrecautionsEnsure the magnetic beads are thoroughly mixed before use to prevent changes in concentration during pipetting. Avoid prolonged ultrasonication, which may damage the bead surface.
Grade: BioReagent
Storage Temperature: Store at 2-8°C;Desiccated;Do not freeze
Shipped in: Wet ice;Do not freeze
- UPC:
- 51473028
- Weight:
- 11.30 Ounces
- HazmatClass:
- No
- Quantity:
- 1
- Unit of Measurement:
- EA
- WeightUOM:
- LB
- MPN:
- M1520788-100ml
- Country of Origin:
- China
- Product Size:
- 100ml
- Harmonized Tariff Code:
- 2931.90.90



