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Product Information
Phase Detail
Biozen MagBeads
Biozen Magbeads is a streptavidin coated paramagnetic affinity bead that can be used to isolate proteins and peptides

Biozen MagBeads

Immunocapture of mAbs Using Magnetic Beads

Biozen MagBeads are used for the purification, clean up, and isolation of proteins and peptide molecules using a paramagnetic affinity bead with a streptavidin coated surface. Magnetic beads offer a rapid solution compared to traditional sample preparation options by maximizing binding capacity with a uniform particle for accurate and reliable results, in less time.

Brand
bioZen
Recommended Use
Consistent purification, clean-up, and isolation of proteins and peptide molecules using a paramagnetic particle

Blocked with hydrophilic copolymer and coupled with biotinylated BSA which:

  • Properly orients capture antibody
  • Prevents surface crowding and ligand inactivation through non-specific binding
  • Enhances dispersion of particles
  • Improves binding efficiency

MagBead Protocol

MagBead Activation

 

Immunocapture


Rituximab Signature Peptide - ASGYTFTSYNMHWVK

Comparison of Dynabeads M-280 vs. Biozen MagBeads

Column:
Biozen 3 µm Peptide PS-C18
Dimension:
50 x 2.1 mm
Part No.:
Mobile Phase:
A: 0.1 % Formic acid in Water
B: 0.1 % Formic acid in Acetonitrile
Gradient:
3-50 % B in 4.5 minutes
Flow Rate:
0.3 mL/min
Temperature:
40 °C
Detection:
SCIEX X500B Q-TOF
Sample:
Rituximab 1.5 µg/mL (ASGYTFTSYNMHWVK)

Biozen MagBeads Binding Activity Leads to
Accurate and Sensitive Results 

Rituximab

  • Reduction in non-specific binding
  • Excellent reproducibility lot-to-lot

 

Immunocapture Bead Correlation Coefficient
Thermo® Dynabeads M-280 0.9176
 Biozen MagBeads, Lot 1 0.9914
 Biozen MagBeads, Lot 2 0.9941

Comparative separations may not be representative of all applications.

Troponin

  • Increased assay precision
  • Improvements in response

 

Concentration
(ng/mL)
MyOne™ Streptavidin T1 % CV Cal Dose Biozen MagBeads
% CV Cal Dose
0.3 1 1.8
1.2 1.8 0.7
5 3.6 0.4
25 3.2 1
50 4.6 1.7

Non-saturated, accurate binding surface orientation