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MAL-dPEG®₆-NHS ester (QBD-10064)



MAL-dPEG®6-NHS ester, product number QBD-10064, is a crosslinking reagent that joins a sulfhydryl to a free amine across a hydrophilic bridge. The sulfhydryl groups react with a maleimide group via a Michael addition reaction. The amines form amide bonds with the crosslinker by nucleophilic substitution of the N-hydroxysuccinimidyl (NHS) ester of a carboxylic acid group. The maleimide and NHS functional groups on the crosslinking compound sit at either end of a short, discrete-length polyethylene glycol chain (dPEG®).


Unit Size 100 mg, 1000 mg
Molecular Weight 601.60; single compound
Chemical formula C₂₆H₃₉N₃O₁₃
Purity > 98%
dPEG® Spacer is 28 atoms and 31.7 Å
Typical solubility properties (for additional information contact Customer Support) Methylene chloride, Acetonitrile, DMAC or DMSO.
Storage and handling -20°C; Always let come to room temperature before opening; be careful to limit exposure to moisture and restore under an inert atmosphere; stock solutions can be prepared with dry solvent and kept for several days (freeze when not in use). dPEG® pegylation compounds are generally hygroscopic and should be treated as such. This will be less noticeable with liquids, but the solids will become tacky and difficult to manipulate, if care is not taken to minimize air exposure.


  1. Greg T. Hermanson, Bioconjugate Techniques, 2nd Edition, Elsevier Inc., Burlington, MA 01803, April, 2008 (ISBN-13: 978-0-12-370501-3; ISBN-10: 0-12-370501-0); See pp. 276-335 for general description and use of heterobifunctional crosslinkers, as well as his specific discussion with protocols of our MAL-dPEG®x-NHS esters on pp. 718-722.
  2. Greg T. Hermanson, Bioconjugate Techniques, 3rd Edition, Elsevier, Waltham, MA 02451, 2013, ISBN 978-0-12-382239-0; See Chapter 18, Discrete PEG Reagents, pp. 787-821, for a full overview of the dPEG® products.
  3. Direct Cell Surface Modification with DNA for the Capture of Primary Cells and the Investion of Myotube Formation on Defined Patterns. Sonny C. Haiso, Betty J. Shaun, Hiroaki Onoe, Erik S. Douglas, Zev J. Gartner, Richard A. Mathies, Carolyn R. Bertozzi, and Matthew B. Francis. Langmuir. 2009, 25 (12), pp 6985–6991. April 29, 2009. DOI: 10.1021/la900150n.
  4. A sandwich-type DNA array platform for detection of GM targets in multiplex assay. Sena Cansız, Can Ozen, Ceren Bayrac, A. Tahir Bayrac, Fatma Gul, Murat Kavruk, Remziye Yılmaz, Fusun Eyidogan, Huseyin, Avni Oktem. European Food Research and Technology. 2012, 235 (3) pp 429-437. July 6, 2012. DOI:10.1007/s00217-0121767y.
  5. A virus-like particle vaccine platform elicits heightened and hastened local lung mucosal antibody production after a single dose. Laura E. Richert, Amy E. Servidb, Ann L. Harmsen, Agnieszka Rynda-Apple, Soo Han, James A. Wiley, Trevor Douglas, Allen G. Harmsen. Vaccine. 2012, 30 (24) pp 3653-3665. May 21, 2012. DOI: 10.1016/j.vaccine.2012.03.035.
  6. New Assay for Quantification of PEGylated Proteins During in Vitro Permeability Studies. Spela Jalen,Vanja Smilovic, Katarina Fidler, Barbara Podobnik, Maja Marusic, Radovan Komel, Vladka Gaberc-Porekar and Simona Jevsevar. Acta Chimica Slovenica. 2014, 61 (3) pp 615-622. January 15, 2014.
  7. Optimization, Production and Characterization of a CpG-Oligonucleotide-Ficoll Conjugate Nanoparticle Adjuvant for Enhanced Immunogenicity of Anthrax Protective Antigen. Bob Milley, Radwan Kiwan, Gary S. Ott, Carlo Calacsan, Melissa Kachura, John D Campbell, Holger Kanzler, and Robert L. Coffman. Bioconjugate Chemistry. 2016, April 13, 2016. DOI: 10.1021/acs.bioconjchem.6b00107.
  8. Immune Response Modulation of Conjugated Agonists with Changing Linker Length. Keun Ah Ryu, Katarzyna Slowinska, Troy Moore, and Aaron Esser-Kahn. ACS Chemical Biology. 2016, October 17, 2016. DOI: 10.1021/acschembio.6b00895.
  9. Surface Coating of Nanoparticles Reduces Background Inflammatory Activity while Increasing Particle Uptake and Delivery. Brittany A Moser, Rachel C Steinhardt, and Aaron P Esser-Kahn. ACS Biomaterials Science and Engineering. 2016. December 1, 2016. DOI: 10.1021/acsbiomaterials.6b00473.
  10. New Perspectives in the Renin-Angiotensin-Aldosterone System (RAAS) II: Albumin Suppresses Angiotensin Converting Enzyme (ACE) Activity in Human. Miklos Fagyas, Katalin Uri, Ivetta M. Siket, Gabor A. Fulop, Viktoria Csato, Andrea Darago, Judit Boczan, Emese Banyai, Istvan Elek Szentkiralyi, Tamas Miklos Maros, Tamas Szerafin, Istvan Edes, Zoltan Papp, Attila Toth. PLoS ONE. 2014, 9 (4) e87844. April, 1 2014. DOI: 10.1371/journal.pone.0087844.

Applicable patents and legal notices are available at legal notices.

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