Mal-PEG36-NHS ester
Cat No.: BP-501810
4.5 
Mal-PEG36-NHS ester is a heterobifunctional polyethylene glycol (PEG) linker featuring a terminal maleimide group and an N-hydroxysuccinimide (NHS) ester, connected through a long, flexible PEG chain that provides substantial hydrophilicity and molecular spacing. The maleimide moiety enables selective conjugation to thiol-containing partners (e.g., cysteine residues or thiol-functionalized ligands) via stable thioether bond formation, while the NHS ester reacts with primary amines on peptides, proteins, or amine-bearing small molecules to form an amide linkage. In PROTAC and targeted protein degradation workflows, this linker design supports modular assembly of degraders by temporally and spatially tuning the connection between a ligand-bearing thiol and an amine-functionalized component, often improving solubility and reducing steric constraints that can impair recruitment of the target and E3 ligase. Its long PEG chain and dual-reactivity make it a practical tool for generating well-defined conjugates for mechanistic studies and optimization of degradation efficiency.
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* For research and manufacturing use only. Not for human or clinical use.
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Mal-PEG36-NHS ester is a PEG-based bifunctional linker designed for efficient conjugation in targeted protein degradation workflows. Its maleimide handle enables selective coupling to thiol-containing ligands, while the NHS ester supports rapid amide-bond formation with primary amines. This combination facilitates modular PROTAC assembly, improving synthetic flexibility and enabling stable, well-defined linker architectures. Detailed structural and reactivity considerations are provided below.
Structure: The linker comprises a polyethylene glycol chain terminating in a maleimide group and an N-hydroxysuccinimide ester. It contains an amide-reactive activated ester, a conjugated maleimide double bond, and ether linkages along the PEG backbone, providing water compatibility and conformational mobility.
Reactivity: The NHS ester reacts with primary amines to form stable amide bonds under mildly basic aqueous or mixed solvent conditions, typically using short reaction times to preserve activation. The maleimide undergoes thiol–maleimide Michael addition with cysteine or reduced thiol groups, often in near-neutral buffers that minimize maleimide hydrolysis. No special catalysts are generally required; careful control of pH and thiol availability is key for clean coupling.
* 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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