N-(m-PEG4)-N'-(PEG3-Mal)-Cy5
Cat No.: BP-502038
Purity: 98%
4.5 
N-(m-PEG4)-N'-(PEG3-Mal)-Cy5 is a heterobifunctional, PEG-based linker conjugated to a Cy5 fluorophore, bearing a thiol-reactive maleimide handle for conjugation to thiol-functionalized partners. Structurally, it contains an m-PEG4 segment and a PEG3 segment that provide hydrophilic, flexible spacing, reducing steric interference and helping preserve productive ternary complex formation in PROTAC workflows. The maleimide moiety enables stable thioether coupling to cysteine- or thiol-functionalized partners, while the mPEG terminus is methoxy-capped and does not provide a separate amine-reactive handle. In targeted protein degradation research, this linker is valuable for building fluorescently traceable PROTACs or related conjugates, allowing researchers to monitor synthesis, quantify conjugation efficiency, and track cellular association or uptake of degradation constructs. The Cy5 label further facilitates fluorescence-based optimization of linker length and attachment chemistry to improve experimental reproducibility.
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* For research and manufacturing use only. Not for human or clinical use.
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This PROTAC linker, N-(m-PEG4)-N'-(PEG3-Mal)-Cy5, is designed to connect a targeting ligand to a reactive “handle” while incorporating polyethylene glycol spacers that improve solubility and conformational flexibility. The included Cy5 fluorophore enables tracking of conjugation efficiency and linker behavior in experimental workflows. Its maleimide functionality supports efficient coupling to thiol-bearing partners, making it well suited for assembling targeted protein degradation constructs. Detailed structural and reactivity considerations are provided below.
Structure: The molecule contains a Cy5 chromophore linked through polyethylene glycol (PEG) chains, providing a hydrophilic, flexible scaffold. A maleimide moiety is incorporated as a strained alkene-containing Michael acceptor, enabling selective bond formation with nucleophilic thiols.
Reactivity: The maleimide group reacts with thiols via a Michael-type addition to form a stable thioether linkage. Suitable conjugation is typically performed under mildly basic, aqueous buffer conditions that preserve maleimide reactivity and maintain thiol nucleophilicity. Common approaches use thiol-containing ligands or peptides generated from cysteine residues, often with careful control of pH and exclusion of competing nucleophiles such as primary amines.
* 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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