Mal-PEG11-Mal
Cat No.: BP-502072
Purity: ≥95%
4.5 
Mal-PEG11-Mal is a homobifunctional polyethylene glycol linker featuring two maleimide termini separated by an extended PEG chain, enabling efficient conjugation to thiol-containing partners. The maleimide groups undergo rapid, chemoselective Michael addition with accessible cysteine or other sulfhydryl groups under mild aqueous conditions, forming stable thioether linkages that preserve the integrity of sensitive PROTAC-relevant moieties. In PROTAC design and targeted protein degradation workflows, this linker can be used to connect an E3 ligase ligand and a target-binding ligand (or other functional modules) while providing conformational flexibility and improved solubility, which can help mitigate steric constraints and support productive ternary complex formation. Its long, hydrophilic PEG scaffold is particularly valuable for tuning linker length and reducing nonspecific aggregation, thereby facilitating systematic structure–activity studies and optimization of degrader performance in vitro.
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* For research and manufacturing use only. Not for human or clinical use.
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Mal-PEG11-Mal is a heterobifunctional, PEG-based bifunctional linker designed for constructing PROTACs through efficient conjugation to protein-binding ligands. Its flexible poly(ethylene glycol) scaffold can enhance solubility and provide spatial separation between the warhead and the E3 ligase-binding moiety, which is often beneficial for productive ternary complex formation. The two maleimide termini enable selective thio-Michael addition under mild conditions. Detailed structural and reactivity considerations are provided below.
Structure: The linker comprises a long PEG chain terminated by two maleimide groups, connected through stable carbon–carbon and ether linkages along the polymer backbone. Maleimides contain activated alkene moieties that undergo conjugate addition, while the PEG segment imparts hydrophilicity and conformational flexibility.
Reactivity: Mal-PEG11-Mal is typically used for thio-Michael coupling with sulfhydryl-containing ligands or reduced cysteine residues on targeting moieties. Reactions are commonly performed in aqueous buffer systems at mildly basic to neutral pH, where maleimide electrophilicity supports conjugate addition. No special catalysts are required; solvent choice should maintain maleimide stability and ligand solubility. Care is taken to minimize competing hydrolysis of maleimides.
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
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