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News release

News release

Merck Millipore and celares GmbH
announce collaboration

New: Discrete 4-arm-PEG Maleimide

New: Discrete 4-arm-PEG Maleimide

The multimerisation with discrete 4-arm PEG facilitates defined linker lenght according to binding requirments

Hydrophilic linkers for ADCs

Hydrophilic linkers for ADCs

celares PEG based linker increase solubility of hydrophobic cytotoxic drugs

Tetramerisation

In the past 10-15 years biologically active agents with antigen binding activity like antibodies, antibody fragments, antibody like molecules, and scaffold proteins have gained significant relevance.

However,

The Affilin® tetramer 8A7 clearly binds to human TNFα with an apparent KD value of 100 nM. In comparison to the monomer the affinity was increased by the factor of 30. This is in contrast to traditional PEGylation which typically leads to a decrease in in-vitro activity. The Affilin® tetramer 8A7 clearly binds to human TNFα with an apparent KD value of 100 nM. In comparison to the monomer the affinity was increased by the factor of 30. This is in contrast to traditional PEGylation which typically leads to a decrease in in-vitro activity.
 
Our multimeric binding agent has been co-developed with Scil Proteins GmbH and is covered by patent WO2008096012. Our multimeric binding agent has been co-developed with Scil Proteins GmbH and is covered by patent WO2008096012.

their therapeutic use has yet been limited because of rapid renal excretion, or poor solubility, or immunogenicity, or reduced binding affinity and/or avidity as compared with native human antibodies. For this reason, many attempts have been made to improve the pharmacological properties of such antigen binding proteins routinely having molecular weights far below 50,000 Dalton. Reviews have been published in Nature Biotechnology Volume 21, Number 4, 2006: 1126-36 or Nature Reviews Immunology, Vol 6, 2006: 343 -357.

celares GmbH and Scil Proteins GmbH have co-developed a multimeric binding agent for the multimerization of antigen binding proteins. This reagent is characterized by a defined structure and adjustable linker length. In this way, it is possible to prepare conjugates with decelerated renal clearance showing a higher avidity compared to the avidity of the monomeric binding molecule.

An example is a TNF-α binding Affilin® molecules. By tetramerization with our agent it has been able to increase its affinity in an in-vitro assay 30-fold.

Affilin® is a registered mark designation owned by Scil Proteins GmbH.