Mal-PEG4-Lys(TFA)-NH-m-PEG24
Cat No.: BP-502093
4.5 
Mal-PEG4-Lys(TFA)-NH-m-PEG24 is a heterobifunctional PEG-based linker featuring a maleimide group for chemoselective conjugation to thiols and a lysine-derived amide handle that connects to a long, flexible monodisperse PEG segment. The structure combines a short PEG spacer with a terminal maleimide electrophile, enabling efficient formation of stable thioether bonds under mild aqueous conditions, while the extended PEG chain provides pronounced hydrophilicity, steric shielding, and improved solubility that can reduce nonspecific interactions in complex biological media. In PROTAC and targeted degradation constructs, this linker serves as a modular “distance and attachment” element: it positions the two functional partners to support productive ternary complex formation and can tune the effective linker length and conformational freedom between the recruiting ligand and the E3 ligase-binding moiety. Researchers use such PEG–maleimide lysine linkers to systematically optimize conjugation efficiency and degradation performance while maintaining experimental robustness across different protein-binding chemistries.
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* For research and manufacturing use only. Not for human or clinical use.
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This Mal-PEG4-Lys(TFA)-NH-m-PEG24 linker is designed to connect a maleimide-bearing PEG segment to a lysine-derived amide handle, enabling versatile conjugation strategies commonly used in PROTAC assembly. Its PEG-rich architecture supports solubility, flexible linker behavior, and efficient presentation of reactive groups for targeted protein degradation workflows. The detailed Structure and Reactivity parameters below describe the chemical features and practical considerations for constructing PROTACs using this linker.
Structure: The linker contains a maleimide electrophile for selective thiol coupling, a lysine-derived amide linkage, and extended PEG segments that confer high hydrophilicity and conformational flexibility. It features amide and ether linkages typical of PEG-based bioconjugation scaffolds, with a TFA-associated counterion improving handling and salt formation.
Reactivity: Maleimide groups react with cysteine thiols via a Michael-type addition under mildly basic to neutral aqueous conditions, commonly in the presence of reducing agents that maintain free thiols. Typical PROTAC construction uses thiol-functional ligands or engineered cysteine-containing binding moieties, followed by purification to remove unreacted maleimide. Care is taken to minimize competing thiol side reactions and to control pH and buffer composition for reproducible coupling efficiency.
* 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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