• Synonyms：
  mPEG-Succinimidyl ester
  mPEG-NHS
  
• Purity：
  ≥95%
• Recommended Storage Condition：
  Store at -5°C,keep in dry and avoid sunlight.
• Uses：
  Applicated in medical research, drug-release, nanotechnology and new materials research, cell culture. In the study of ligand, polypeptide synthesis support, a graft polymer compounds, new materials, and polyethylene glycol-modified functional coatings and other aspects of the active compound.

mPEG-SC, also known as mPEG-Succinimidyl ester, is a member of the mPEG-NHS family of reagents. It contains a succinimidyl ester functional group attached to a mPEG chain. The succinimidyl ester group reacts with primary amines to form stable urethane bonds, facilitating the conjugation of mPEG chains to biomolecules or surfaces. mPEG-SC is particularly useful for modifying amine-containing molecules, such as proteins or peptides, to improve their solubility, stability, and biocompatibility. 

Biopharma PEG offers a wide range of PEG products from lab to commercial scale in both non-GMP and GMP grades. Email at sales@biochempeg.com and start using a superior product for your next product R&D project.

Cited Publications

This PEG derivative has been cited in peer-reviewed scientific publications. Browse the references below to learn more.

1. Multifunctional Polypeptide-Based Nanoconjugates for Targeted Mitochondrial Delivery and Nonviral Gene Therapy, Camilla Pegoraro, Esther Masiá Sanchis, Snežana Đorđević, Irene Dolz-Pérez, Cristián Huck-Iriart, Lidia Herrera, Sergio Esteban-Pérez, Inmaculada Conejos-Sanchez, and María J. Vicent, Chemistry of Materials 2025 37 (4), 1457-1467, DOI: 10.1021/acs.chemmater.4c02742  
2. The T-cell niche tunes immune function through modulation of the cytoskeleton and TCR-antigen forces
   Anna V. Kellner, Rae Hunter, Priscilla Do, Joel Eggert, Maya Jaffe, Delaney K. Geitgey, Miyoung Lee, Jamie A. G. Hamilton, Anthony J. Ross, Raira S. Ank, Rachel L. Bender, Rong Ma, Christopher C. Porter, Erik C. Dreaden, Byron B. Au-Yeung, Karmella A. Haynes, Curtis J. Henry, Khalid Salaita
   bioRxiv 2024.01.31.578101; doi: https://doi.org/10.1101/2024.01.31.578101 
3. Wang D, Hedayati M, Stuart JD, et al. Ligand Presentation Inside Protein Crystal Nanopores: Tunable Interfacial Adhesion Noncovalently Modulates Cell Attachment. Mater Today Nano. 2023;24:100432. doi:10.1016/j.mtnano.2023.100432
4. Mechanical force regulates ligand binding and function of PD-1, Kaitao Li, Paul Cardenas-Lizana, Anna V. Kellner, Zhou Yuan, Eunseon Ahn, Jintian Lyu, Zhenhai Li, Khalid Salaita, Rafi Ahmed, Cheng Zhu, bioRxiv 2023.08.13.553152; doi: https://doi.org/10.1101/2023.08.13.553152  
5. Balfourier, A., Tsolaki, E., Heeb, L., L. Starsich, F. H., Klose, D., Boss, A., Gupta, A., Gogos, A., & Herrmann, I. K. (2023). Multiscale Multimodal Investigation of the Intratissural Biodistribution of Iron Nanotherapeutics with Single Cell Resolution Reveals Co-Localization with Endogenous Iron in Splenic Macrophages. Small Methods, 7(2), 2201061. https://doi.org/10.1002/smtd.202201061 
6. Fluorescence-Shadowing Nanoparticle Clusters for Real-Time Monitoring of Tumor Progression, Oanh-Vu Pham-Nguyen, JiUn Shin, Yeonju Park, Sila Jin, Song Rae Kim, Young Mee Jung, and Hyuk Sang Yoo, Biomacromolecules 2022 23 (8), 3130-3141, DOI: 10.1021/acs.biomac.2c00169 
7. Boss, A., Heeb, L., Vats, D., L. Starsich, F. H., Balfourier, A., Herrmann, I. K., & Gupta, A. (2022). Assessment of iron nanoparticle distribution in mouse models using ultrashort-echo-time MRI. NMR in Biomedicine, 35(6), e4690. https://doi.org/10.1002/nbm.4690 
8. Lim, K., Kim, H. K., Le, X. T., Nguyen, N. T., Lee, E. S., Oh, K. T., Choi, H., & Youn, Y. S. (2020). Highly Red Light-Emitting Erbium- and Lutetium-Doped Core-Shell Upconverting Nanoparticles Surface-Modified with PEG-Folic Acid/TCPP for Suppressing Cervical Cancer HeLa Cells. Pharmaceutics, 12(11), 1102. https://doi.org/10.3390/pharmaceutics12111102

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