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Bis-MAL-dPEG®₃ (QBD-10215)



Bis-MAL-dPEG®3, product number QBD-10215, is a short, homobifunctional, crosslinking reagent that links two molecules (e.g., peptides, proteins) together via the thiol-maleimide reaction (also known as the thiol-Michael addition). Maleimidopropionate groups functionalize each end of the molecule. A single molecular weight, discrete polyethylene glycol (dPEG®) spacer separates the two end groups.

The thiol-maleimide reaction, a type of click chemistry reaction, is a popular way to conjugate molecules. The maleimide functional group rapidly reacts with sulfhydryl groups, and the reaction is chemoselective for sulfhydryls in the pH range of 6.5 – 7.5. The discrete chain length polyethylene glycol (dPEG®) spacer between the two maleimide groups is a single molecular weight compound. Applications for this product include mapping which proteins in a complex are close together; determining ligand-receptor binding relationships; and construction of antibody-drug conjugates (ADCs), among many others.


Unit Size50 mg, 1000 mg
Molecular Weight522.55; single compound
Chemical formulaC₂₄H₃₄N₄O₉
Purity> 98%
SpacersdPEG® Spacer is 28 atoms and 30 Å
Typical solubility properties (for additional information contact Customer Support)Methylene chloride, 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.


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.

Backbone Degradable Multiblock N-(2-Hydroxypropyl)methacrylamide Copolymer Conjugates via Reversible Addition Fragmentation Chain Transfer Polymerization and Thiol-ene Coupling Reaction. Huaizhong Pan, Jiyuan Yang, Pavla Kopečková, and Jindřich Kopeček. Biomacromolecules. 2011, 12 (1) pp 247–252. January 10, 2011. DOI:10.1021/bm101254e.

Quantitative evaluation of the lengths of homobifunctional protein cross-linking reagents used as molecular rulers. NORA S. GREEN, EMIL REISLER, K.N. HOUK. Protein Science. 2001, 10 (7) pp 1293-1304. March 23, 2010. DOI: 10.1101/ps.51201.

Effects of modification at the fifth residue of l-conotoxin GIIIA with bulky tags on the electrically
stimulated contraction of the rat diaphragm. M. Nakamura, Y. Oba, H. Nakamura, Y. Ishida, T. Kohno, K. Sato. Journal Peptide Res. 2004, 64 (3) pp 110-117. May 30, 2004. DOI: 10.1111/j.1399-3011.2004.00175.x.

A Divalent Immunotoxin Formed by the Disulfide Bond between Hinge Regions of Fab Domain. SeongHyeok Choi, JiEun Kim, YongChan Lee, Young-Ju Jang, Ira Pastan, MuHyeon Choe. Bull Korean Chem.Soc. 2001, 22 (12) pp 1361-1365. September 3, 2001. DOI:

Mapping Protein-Protein Interactions between MutL and MutH by crosslinking. Luis Giron-Monzon, Laura Manelyte, Robert Ahrends, Dieter Kirsch, Bernhard Spengler, and Peter Friedhoff. J. Biol. Chem. 2004, 279 ( 47) pp 49338-49345. September 14, 2004. DOI: 10.1074/jbc.M409307200.

SWI/SNF- and RSC-Catalyzed Nucleosome Mobilization Requires Internal DNA Loop Translocation within Nucleosomes. Ning Liu, Craig L. Peterson and Jeffrey J. Hayes. Molecular and Cellular Biology. 2011, 31 (20), pp 4165-4177. August 22, 2011. DOI: 10.1128/MCB.05605-11.

Mitotic Spindle Assembly around RCC1-Coated Beads in Xenopus Egg Extracts. David Halpin, Petr Kalab, Jay Wang, Karsten Weis, Rebecca Heald. PLoS Bio. 2011, 9 (12) pp e1001225. December 27, 2011. DOI: 10.1371/journal.pbio.1001225.

Chemical Trapping of the Dynamic MutS-MutL Complex Formed in DNA Mismatch Repair in Escherichia coli. Ines Winkler, Andreas D. Marx, Damien Lariviere, Roger J. Heinze, Michele Cristovao, Annet Reumer, Ute Curth, Titia K. Sixma, and Peter Friedhoff. JBC. 2011, 286 (19) pp 17326–17337. May 13, 2011. DOI:10.1074/jbc.M110.187641.

Functional Characterization of Rhodopsin Monomers and Dimers in Detergents. Beata Jastrzebska, Tadao Maeda, Li Zhu, Dimitrios Fotiadis, Slawomir Filipek, Andreas Engel, Ronald E. Stenkamp, and Krzysztof Palczewskia. JBC. 2004, 279 (52) pp 54663-54675. December 24, 2004. DOI: 10.1074/jbc.M408691200.

Enhanced Fluorescence resonance energy transfer immunoassay with improved sensitivity based on the Fab’-based immunoconjugates. Yoshiyuki Ohiro, Hiroshi Ueda, Norio Shibata, Teruyuki Nagamune. Analytical Biochemistry. 2007, 360 (2) pp 266-272. January 15, 2007. DOI:10.1016/j.ab.2006.10.025.

Purification, characterization and cloning of a ricin B-like lectin from mushroom Clitocybe nebularis with antiproliferative activity against human leukemic T cells. Jure Pohleven, Nataša Obermajer, Jerica Sabotič, Sabina Anžlovar, Kristina Sepčić, Janko Kos , Bogdan Kralj, Borut Štrukelj, Jože Brzin. Biochimica et Biophysica Acta (BBA) – General Subjects. 2009, 1790 (3) pp 173-181. December 8, 2008. DOI: 10.1016/j.bbagen.2008.11.006.

Development of a homogeneous competitive immunoassay for phosphorylated protein antigen based on the enhanced fluorescence resonance energy transfer technology. Yoshiyuki Ohiro,1,⁎ Hiroshi Ueda,2,3 Norio Shibata,1 and Teruyuki Nagamune. Journal of Bioscience and Bioengineering. 2010, 109 (1), pp 15–19. July 29, 2009. DOI: 10.1016/j.jbiosc.2009.07.004.

Analysis of the Quaternary Structure of the MutL C-terminal Domain. Jan Kosinski, Ina Steindorf, Janusz M. Bujnicki, Luis Giron-Monzon and Peter Friedhoff. Journal of Molecular Biology. 2005, 351 (4) pp 895-909. August 26, 2005. DOI: 10.1016/j.jmb.2005.06.044.

X-ray Photoelectron Spectroscopy and Differential Capacitance Study of Thiol-Functional Polysiloxane Films on Gold Supports. Patrick A. Johnson and Rastislav Levicky. Langmuir. 2004, 20 (22) pp 9621-9627. September 28, 2004. DOI: 10.1021/la048458s.

Polymercaptosiloxane Anchor Films for Robust Immobilization of Biomolecules to Gold Supports. Patrick A. Johnson and Rastislav Levicky. Langmuir . 2003, 19 (24) pp10288-10294. October 30, 2003. DOI: 10.1021/la035102s.

X-ray photoelectron spectroscopy and infrared spectroscopy study of maleimide-activated supports for immobilization of oligodeoxyribonucleotides. Gang Shen, Maria Francis G. Anand and Rastislav Levicky. Nucleic Acids Research. 2004, 32 (20) pp 5973-5980. November 10, 2004. DOI: 10.1093/nar/gkh932.

Disulfide Sensitivity in the Env Protein Underlies Lytic Inactivation of HIV-1 by Peptide Triazole Thiols. Lauren D. Bailey, Ramalingam Venkat Kalyana Sundaram, Huiyuan Li, Caitlin Duffy, Rachna Aneja, Arangassery Rosemary Bastian, Andrew P. Holmes, Kantharaju Kamanna, Adel A. Rashad and Irwin Chaiken. ACS Chemical Biology. 2015, October 12, 2015. DOI: 10.1021/acschembio.5b00381.

In vivo mapping of a dynamic ribonucleoprotein granule interactome in early Drosophila embryos. Jimiao Zheng, Ming Gao, Nhan Huynh, Samuel J. Tindell, Hieu D. L. Vo, W. Hayes McDonald, and Alexey L. Arkov. Febs Open Bio. 2016, pp 1-9. October 3, 2016. DOI: 10.1002/2211-5463.12144.

Applicable patents and legal notices are available at legal notices.

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