The rise of therapeutic monoclonal antibodies (mAbs) offers immense potential for precision medicine but also brings unique purification hurdles. Conventional chromatography methods can struggle with altered Fc regions, complex aggregates and diverse isoforms, affecting yield, purity and scalability.
This infographic explores innovative solutions to streamline mAb purification. Learn how innovative affinity ligands and resins address these challenges, enabling high-specificity, stable purification platforms for scalable production.
Download this infographic to discover:
- How to purify complex mAb isoforms with precision and stability
- Strategies for overcoming the limitations of traditional chromatography methods
- Key solutions for achieving high yield and scalability in mAb production
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CaptureSelect
agarose affinity
resin technology
harnesses features
of single-domain camelid
antibodies. They are small
and robust, enabling them to
reach obscured target regions
and withstand a wide range
of bind/elute conditions.1
POROS beads support all our mAb polishing
resins. Their structural properties contribute to
stable, high-throughput mAb purification.
Resolving 5 challenges
of novel mAb purification
The diversity of new therapeutic monoclonal antibody (mAb) modalities brings potential
to transform medicine with highly specific and efficient antigen targeting. However, added
structural complexity can present purification challenges that conventional chromatography
strategies can’t address. Thermo Scientific™ CaptureSelect™ affinity chromatography
ligands and Thermo Scientific™ POROS™ chromatography resins are designed to
overcome these challenges to enable ample yield, high purity, and scalable mAb production.
IgG Antibody drug
conjugates
Fc-fusion
proteins
Bi-specific
antibodies
Fab fragments
For research use or further manufacturing. © 2024 Thermo Fisher Scientific Inc. All rights reserved. All trademarks are the property of Thermo Fisher Scientific
and its subsidiaries unless otherwise specified. INFG-9407412
Explore workflow solutions thermofisher.com/antibody-therapeutics
Reference
1. Harmsen MM, De Haard HJ (2007). Properties, production, and applications of camelid single-domain antibody fragments. Appl Microbiol Biotechnol 77(1):13-22.
Therapeutic mAb modalities
Top 5 purification challenges
CaptureSelect affinity ligands go where
Protein A cannot
Antibody purification
Modified mAb conformations may result in a wide range of product related impurities
and physiochemical properties that may limit the efficacy of Protein A.
Target mAb
has absent
or altered
Fc region
Target
mAb is
pH-sensitive
Culture medium
contains mAb
dimers and aggregates
Culture medium
contains elevated
levels of mixed molecular
weight species
Culture medium
contains overexpressed light chains
and light chain dimers
Impact on purification
mAb affinity binding
is impaired
mAb interaction with
polishing matrices
is impaired
Competes with
target mAb for
matrix interaction
Aggregation or
degradation of
target mAb
Elevated sensitivity
to binding and
elution conditions
Introduces workflow
issues
Master challenges with adaptable solutions and start-to-finish support
• Purify complex mAb isoforms at high specificity and stability
• Establish your mAb purification platform early for streamlined scale-up
• Work with us to develop solutions tailored for your specific mAb purification needs
What to do when Protein A doesn’t work?
Polishing for
purity, yield,
and scalability
POROS hydrophobic interaction (HIC), cation and anion
exchange (IEX), and multi-mode resins remove:
• Host cell proteins (HCPs)
• Leached ligands
• mAb aggregates and fragments
• DNA
• Virus particles
• Product-related impurities
CaptureSelect CH1-XL
• Will not bind free
light chains
Fab
Fab
Fc -fusion IgG
protein
F(ab)2
Bi-specific IgG
containing kappa or
lambda light chain
Chemically robust
backbone – linearity
and stringent
cleaning maximize
efficiency and
scalability
50-micron beads – tight peaks and small elution
volumes maximize resolution and purity
Large pores – high capacity
and resolution independent of
flow rate maximize yield, purity,
and scalability
CaptureSelect KappaXP
CaptureSelect LambdaXP
• Bind only the indicated light chains
• High dynamic binding capacity
• Enables mild elution
CaptureSelect FcXP
• Binds at a specific, conserved epitope
that remains accessible when other
parts of Fc are obstructed
• Enables mild elution
MabCaptureC (ProA)