Specs:

 SDS

Molecular Weight: 865.92; single compound

CAS: 756525-92-5

Purity: > 97%

Spacers: dPEG® Spacer is 46 atoms and 53.3 Å

Shipping: Ambient

References: 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.

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.

Optimal Surface Chemistry for Peptide Immobilization in On-Chip Phosporylation Analysis.Kazuki Inamori, Motoki Kyo, Kazuki Matsukawa, Yusuke Inoue, Tatsuhiko Sonoda, Kenji Tatematsu, Katsuyuki Tanizawa, Takeshi Mori, and Yoshiki Katayama. Analytical Chemistry. 2008, 80 (3), pp 643–650. January 8, 2008. DOI: 10.1021/ac701667g.

Efficient Transfection of Blood-Brain Barrier Endothelial Cells by Lipoplexes and Polyplexes in the Presence of Nuclear Targeting NLS-PEG-Acridine Conjugates. Hongwei Zhang, Anton Mitin, and Serguei V. Vinogradov. Bioconjugate Chemistry. 2009, 20 (1), pp 120–128. December 9, 2008. DOI: 10.1021/bc8003414.

Improved Biodistribution and Radioimmunoimaging with Poly(ethylene glycol)-DOTA-Conjugated Anti-CEA Diabody. Lin li, Paul J. Yazaki, Anne-Line Anderson, Desiree Crow, David Colcher, Anna M. Wu, Lawrence E. Williams, Jeffrey Y.C. Wong, Andrew Raubitschek, and John E. Shively. Bioconjugate Chemistry. 2006, 17 (1), pp 68–76. December 24, 2005. DOI: 10.1021/bc0502614.

A proof of the specificity of kanamycin-ribosomal RNA interaction with designed synthetic analogs and the antibacterial activity. Yoshio Nishimura, Hayamitsu Adachi, Motoki Kyo, Shoichi Murakami, Seiko Hattori, and Keiichi Ajito. Bioorganic & Medicinal Chemistry Letters. 2005, 15 (8), pp 2159-2162. April 15, 2005. DOI: 10.1016/j.bmcl.2005.02.043.

Recognition Imaging with a DNA Aptamer. Liyun Lin, Hongda Wang, Yan Liu, Hao Yan, and Stuart Lindsay. Biophysical Journal. 2006, 90 (11), pp 4236-4238. June 1, 2006. DOI: 10.1529/biophysj.105.079111.

Genotyping by allele-specific L-DNA-tagged PCR. Gosuke Hayashi, Masaki Hagihara, Kazuhiko Nakatani. Journal of Biotechnology. 2008, 135 (2), pp 157-160. June 1, 2008. DOI: 10.1016/j.jbiotec.2008.03.011.

Single-molecule detection of phosphorylation-induced plasticity changes during ezrin activation. Dan Liu, Ling Ge, Fengsong Wang, Hirohide Takahashi, Dongmei Wang, Zhen Guo, Shige H. Yoshimura, Tarsha Ward, Xia Ding, Kunio Takeyasu, Xuebiao Yao. FEBS Letters. 2007, 581 (18), pp 3563-3571. July 24, 2007. DOI: 10.1016/j.febslet.2007.06.071.

Development of glutathione-coupled cantilever for the single-molecule force measurement by scanning force microscopy. Shige H. Yoshimua, Hirohide Takahashi, Shotaro Otsuka, Kunio Takeyasu. FEBS Letters. 2006, 580 (16), pp 3961-3965. July 10, 2006. DOI: 10.1016/j.febslet.2006.06.032.

Controlled-release system of single-stranded DNA triggered by the photothermal effect of gold nanorods and its in vivo application. Shuji Yamashita, Hiromitsu Fukushima, Yasuyuki Akiyama, Yasuro Niidome, Takeshi Mori, Yoshiki Katayama, Takuro Niidome. Bioorganic & Medicinal Chemistry. 2011, 19 (7), pp 2130-2135. April 1, 2011. DOI: 10.1016/j.bmc.2011.02.042.

Interaction of Synaptotagmin with Lipid Bilayers, Analyzed by Single-Molecule Force Spectroscopy. Hirohide Takahashi, Victor Shahin, Robert M. Henderson, Kunio Takeyasu, and J. Michael Edwardson. Biophysical Journal. 2010, 99 (8), pp 2550–2558, October 20, 2010. DOI: 10.1016/j.bpj.2010.08.047.

Cyclic and dimeric gluten peptide analogues inhibiting DQ2-mediated antigen presentation in celiac disease. Jiang Xia, Elin Bergseng, Burkhard Fleckenstein, Matthew Siegel, Chu-Young Kim, Chaitan Khosla and Ludvig M. Sollid. Bioorganic & Medicinal Chemistry. 2007, 15 (20), pp 6565-6573. October 15, 2007. DOI: 10.1016/j.bmc.2007.07.001.

Directed Intermixing in Multicomponent Self-Assembling Biomaterials. Joshua Z. Gasiorowski and Joel H. Collier. Biomacromolecules. 2011, 12 (10), pp 3549–3558. August 25, 2011. DOI: 10.1021/bm200763y.

Design of a Modular Tetrameric Scaffold for the Synthesis of Membrane-Localized D-Peptide Inhibitors of HIV-1 Entry. J. Nicholas Francis, Joseph S. Redman, Debra M. Eckert, and Michael S. Kay. Bioconjugate Chemistry. 2012, 23 (6), pp 1252-1258. May 1, 2012. DOI: 10.1021/bc300076f.

Single-molecule Structural and Functional Analyses of Nuclear Pore Complex. Otsuka, S, Takahashi, H, Yoshimura, Shige H. Micro-NanoMechatronics and Human Science. 2006. November 5, 2006. DOI:10.1109/MHS.2006.320314.

Effect of Compressive Force on Unbinding Specific Protein−Ligand Complexes with Force Spectroscopy. Carleen M. Bowers, David A. Carlson, Monica Rivera, Robert L. Clark, and Eric J. Toone. Journal of Physical Chemistry B. 2013, 117 (17) pp 4755-4762. March 28, 2013. DOI: 10.1021/jp309393s.

Single-molecule anatomy by atomic force microscopy and recognition imaging. Hirohide Takahashi, Kohji Hizume, Masahiro Kumeta, Shige H. Yoshimura and Kunio Takeyasu. Archives of Histology and Cytology. 2009, 72 (4/5) pp 217-225. January 27, 2009. DOI: 10.1679/aohc.72.217.

Attaching Antibodies to AFM Probes with the Sulfhydryl Reactive PEG Tether, NHS-PEG18-PDP. W. Travis Johnson, Ph.D. Agilent Technologies, Inc. 2007, 5989-7702EN. December 18, 2007.

Cell recruitment and transfection in gene activated collagen matrix. Silvia Orsi, Antonia De Capua, Daniela Guarnieri, Daniela Marasco, Paolo A. Netti. Biomaterials. 2010, 31 (3) pp 570–576. January 2010. DOI: 10.1016/j.biomaterials.2009.09.054.

Structural characterization and functionalization of engineered spider silk films. Kristina Spieß, Stefanie Wohlrab and Thomas Scheibel. Soft Matter. 2010, 6 (17) pp 4168-4174. June 16, 2010. DOI: 10.1039/b927267d.

Nanoparticle Self-Assembly Directed by Antagonistic Kinase and Phosphatase Activities. Geoffrey von Maltzahn, Dal-Hee Min, Yingxin Zhang, Ji-Ho Park, Todd J. Harris, Michael Sailor, Sangeeta N. Bhatia. Advance Materials. 2007, 19 (21) pp 3579-3583. October 16, 2007. DOI: 10.1002/adma.200701183.

Cetuximab-conjugated magneto-fluorescent silica nanoparticles for in vivo colon cancer targeting and imaging. Young-Seok Cho, Tae-Jong Yoon, Eue-Soon Jang, Kwan Soo Hong, Shin Young Lee, Ok Ran Kim, Cheongsoo Park, Yong-Jin Kim, Gyu-Chul Yi, Kiyuk Chang. Cancer Letters. 2010, 299 (1) pp 63-71. December 18, 2010. DOI: 10.1016/j.canlet.2010.08.004.

111In-Labeled Immunoconjugates (Ics) Bispecific for the Epidermal Growth Factor Receptor (EGFR) and Cyclin-Dependent Kinase Inhibitor, p27Kip1. Bart Cornelissen, Veerle Kersemans, Kristin McLarty, Lara Tran, Raymond M. Reilly. Cancer Biotherapy and Radiopharmaceuticals. 2009, 24 (2) pp 163-173. May 1, 2009. DOI: 10.1089/cbr.2008.0553.

U1 Adaptor Oligonucleotides Targeting BCL2 and GRM1 Suppress Growth of Human Melanoma Xenografts In Vivo. Rafal Goraczniak, Brian A Wall, Mark A Behlke, Kim A Lennox, Eric S Ho, Nikolas H Zaphiros, Christopher Jakubowski, Neil R Patel, Steven Zhao, Carlo Magaway, Stacey A Subbie, Lumeng Jenny Yu, Stephanie LaCava, Kenneth R Reuhl,Suzie Chen, and Samuel I Gunderson. Molecular Therapy–Nucleic Acids. 2013, 2 (e92). May 14, 2013. DOI: 10.1038/mtna.2013.24.

Small-Animal SPECT/CT of HER2 and HER3 Expression in Tumor Xenografts in Athymic Mice Using Trastuzumab Fab–Heregulin Bispecific Radioimmunoconjugates. Eva J. Razumienko, Deborah A. Scollard, and Raymond M. Reilly. The Journal of Nuclear Medicine. 2012, 53 (12) pp 1943–1950. October 24, 2012. DOI: 10.2967/jnumed.112.106906.

Mass Spectrometry-Guided Optimization and Characterization of a Biologically Active Transferrin−Lysozyme Model Drug Conjugate. Son N. Nguyen, Cedric E. Bobst, and Igor A. Kaltashov. Molecular Pharmaceutics. 2013, 10 (5) pp 1998−2007. March 27, 2013. DOI: org/10.1021/mp400026y.

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/s00217-012-1767-y.

A homogeneous fluorescent sensor for human serum albumin. Rongsheng E. Wang, Ling Tian, Yie-Hwa Chang. Journal of Pharmaceutical and Biomedical Analysis. 2012, 63 pp 165-169. April 7, 2012. DOI :10.1016/j.jpba.2011.12.035.

Extracellular Antibody Drug Conjugates Exploiting the Proximity of Two Proteins. David J Marshall, Scott S Harried, John L Murphy, Chad A Hall, Mohammed S Shekhani, Christophe Pain, Conner A Lyons, Antonella Chillemi, Fabio Malavsi, Homer L Pearce, Jon S Thorson, and James R Prudent. MT Open. 2016. July 19, 2016. DOI: 10.1038/mt.2016.119.

Additional Search Phrases:

PEG, dPEG, discrete PEG, polyethylene glycol, PEGylation reagent, maleimide, maleimido, N-hydroxysuccinimide, NHS, NHS ester, crosslinking, crosslinker, cross linker, heterobifunctional, amine reactive, thiol reactive, PEG12, sulfhydryl reactive, maleimide thiol, PEG thiol, active ester, MAL-PEG12-NHS ester, Maleimide-PEG12-NHS ester, NHS-PEG12-maleimide, SM(PEG)12, NHS-PEG600-maleimide, Maleimide-PEG-NHS ester



 SDS    Datasheet

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MAL-dPEG®₁₂-NHS ester

$225.00 – $650.00

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PRODUCT IS SOLD STRICTLY FOR INTERNAL LABORATORY AND RESEARCH PURPOSES ONLY AND HAS NOT BEEN REVIEWED BY THE FDA. PRODUCT IS NOT FOR RESALE AND CANNOT BE INCORPORATED INTO COMMERCIAL GOODS FOR ANY USE OR USED IN THE DEVELOPMENT OF COMMERCIAL PRODUCTS OR IN THE PERFORMANCE OF COMMERCIAL SERVICES UNLESS UNDER A SEPARATE LICENSING, SUPPLY, OR DISTRIBUTOR AGREEMENT WITH QUANTA BIODESIGN, LTD. For information pertaining to the commercial use of our products, please click here to contact us.

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MAL-dPEG®12-NHS ester, product number 10284, is one of our top crosslinking reagents. This product joins a sulfhydryl to a free amine through 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 long, discrete-length polyethylene glycol chain (dPEG®).

Among the most popular[1], most useful[2] crosslinking reactions in bioconjugate chemistry are reactions that join free amines with free thiols. These reactions require heterobifunctional reagents that bridge the two groups. Traditional crosslinkers are hydrophobic molecules. Quanta BioDesign’s dPEG® crosslinking products are water-soluble, amphiphilic, single molecular weight PEG compounds with discrete chain lengths.

The conjugation of conventional hydrophobic crosslinking reagents to biomolecules almost inevitably triggers problems such as aggregation and precipitation of the conjugates. These problems do not occur with our water-soluble,non-immunogenic dPEG® crosslinkers. For more information about our dPEG® products, please see our “What is dPEG®?” page. Also, click here for answers to our most frequently asked questions.

How to Use MAL-dPEG®12-NHS ester

Because NHS esters hydrolyze readily in water or aqueous buffer, the NHS ester end of the molecule must conjugate to a target molecule before conjugating the maleimide end of the molecule. At pH 7.0 – 7.5, NHS esters react optimally with free amines. However, NHS esters can react with free amines with pH as low as 6.0. As the pH increases, the hydrolysis rate of the NHS ester increases. Indeed, at pH 7 and 0°C, the NHS ester half-life is four (4) to five (5) hours in aqueous buffer, while at pH 8 and 25°C, the half-life of an NHS ester is one hour.[3] Thus, we strongly discourage storing MAL-dPEG®12-NHS ester, product number 10284, in water or aqueous buffer. Instead, we recommend that customers make new solutions of the product as needed, use them immediately, and discard unused solutions after use.

The reaction of the maleimide end of MAL-dPEG®12-NHS ester, product number 10284, with a sulfhydryl proceeds best at pH 6.5 – 7.5. Conduct the conjugation at the lowest reasonable pH within this range. Above pH 7.5, free amines compete with free thiols at the maleimide reaction site, which can cause confusing results. Moreover, at higher pH values, the maleimide ring may open to form unreactive maleamic acid.[4] For details about maleimide-thiol reaction chemistry, please click here.

Uses of MAL-dPEG®12-NHS ester

The use of MAL-dPEG®12-NHS ester, product number 10284, has been published in numerous scientific paper and patents. The following list highlights some of the more important uses of this product:

  • development of various imaging applications;
  • development of antibody-drug conjugates and extracellular antibody-drug conjugates;
  • modification of diabodies and bispecific antibody fragments;
  • development of different types of assays for peptides, proteins, and oligonucleotides;
  • attachment of antibodies to atomic force microscopy probes;
  • creation of a scaffold for HIV inhibitors;
  • development of biosensors; and,
  • surface coating of nanoparticles.

Also, in a radioimaging application, MAL-dPEG®12-NHS ester demonstrably improved both the biodistribution and image quality of a DOTA-conjugated diabody. See, Improved Biodistribution and Radioimmunoimaging with Poly(ethylene glycol)-DOTA-Conjugated Anti-CEA Diabody.

What can you do with this product?

Please click the “Add to Cart” button now to order MAL-dPEG®12-NHS ester, product number 10284.

Application References:

[1] Hermanson, G. T. Chapter 6, Heterobifunctional Crosslinkers. In Bioconjugate Techniques, 3rd ed.; Academic Press: New York, NY, 2013; pp 299–340, specifically page 300. Many scientists engaged in bioconjugation work consider Greg Hermanson’s book to be the definitive reference on the subject. Click here now to read a review of Greg’s book and to purchase it.

[2] Hermanson, G. T. Chapter 18, PEGylation and Synthetic Polymer Modification. In Bioconjugate Techniques, 3rd ed.; Academic Press: New York, NY, 2013; pp 787–838, specifically page 794.

[3] Hermanson, G. T. Chapter 3, The Reactions of Bioconjugation. In Bioconjugate Techniques; Academic Press: New York, NY, 2013; pp 229–258, specifically page 234.

[4] Hermanson, G. T. Chapter 6, op. cit., page 304.

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Additional information

Weight .5 oz
Dimensions .75 × .75 × 2 in

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