Alternative PROTAC Technology Development

* Please be kindly noted that our services and products can only be used for research to organizations or companies and not intended for any clinical or individuals.

BOC Sciences is a leading CRO providing innovative PROTAC services. We focus on drug discovery based on our comprehensive PROTAC platform, providing research tools and solutions for targeted protein degradation. To date, PROTAC technology has attracted increasing attention from the scientific and pharmaceutical industries, and innovative models of alternative PROTACs have emerged rapidly. In recent years, BOC Sciences has kept abreast of the cutting edge of PROTAC technology and is able to provide customized services for the development of alternative PROTACs.


The classical model of PROTAC is composed of a linker and two traditional small-molecule ligands, one of which targets the E3 ligase and the other targets protein of interest (POI). PROTAC is a targeted protein degradation technology that has the potential to challenge targets previously considered 'undruggable'.

Although classical PROTACs are expected to become an important method for certain target classes, some POIs do not possess the required small molecule binding sites. Therefore, alternative PROTAC methods capable of degrading these POIs have emerged, including RNA-PROTAC, oligonucleotide-based PROTAC, and TRAFTACs (transcription factor-targeting chimeras). In addition, new PROTAC formation models have been expanded, including light-controllable PROTACs (e.g., photoswitchable PROTACs, Photo-Cage PROTACs) and CLIPTACs (In-cell click-formed proteolysis targeting chimeras).

Alternative PROTAC Technologies

RNA-binding proteins (RBPs) play a central role in biological processes, and defective RBP function leads to various diseases. However, RBPs are usually not treatable by conventional PROTACs. RNA-PROTACs, a novel PROTAC technology, have been reported to degrade RBPs selectively.

oligonucleotide-based PROTACs (O'PROTACs) has been developed as a therapeutic means to target DNA binding proteins. Transcription factor-targeting chimeras (TRAFTACs) consist of a chimeric oligonucleotide that binds to both the transcription factor of interest (TOI) and HaloTag-fused dCas9 protein, which can induce TOI degradation.

Conventional PROTAC has a high molecular weight, which may limit its cellular permeability and solubility. PROTAC molecules can be formed intracellularly by the bioorthogonal reaction of two smaller precursors. CLIPTACs have successfully induced ubiquitination and degradation of target proteins.

Photoswitchable PROTAC (photoPROTAC) is obtained by adding an azobenzene linker between the two warhead ligands of PROTAC. This new strategy provides durable spatiotemporal control of induced protein degradation.

Photo-caged PROTACs (pc-PROTACs) are a new class of protein degradation strategies that use light to induce degradation activity, thus increasing the toolbox for studying disease-related proteins.

Our Services

  • We provide customized and alternative PROTAC services for protein degradation to meet Individual customer needs.
  • We offer traditional and alternative PROTAC molecules design, synthesis and optimization services.
  • We utilize innovative PROTAC technologies in order to aid our clients' research and drug discovery.

Our Advantages

  • Multiple alternative PROTAC technologies to meet different customer needs
  • Advanced technology and experienced scientific team
  • Highly reliable and reproducible result
  • Data analysis, detailed report with results and discussion
  • Quality one-stop service
  • Short turn-around time and competitive price

Project Workflow

Alternative PROTAC Technology Development


  1. Békés, M., Langley, D.R. & Crews, C.M., PROTAC targeted protein degraders: the past is prologue, Nat Rev Drug Discov, 2022, 21, 181-200.
  2. Lebraud, H., et al. Protein Degradation by In-Cell Self-Assembly of Proteolysis Targeting Chimeras, ACS Cent Sci., 2016, 2(12): 927-934.

* PROTAC® is a registered trademark of Arvinas Operations, Inc., and is used under license.

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