Specs:

 SDS

Molecular Weight: 844.02; single compound

CAS: 948595-11-7

Purity: > 98%

Spacers: dPEG® Spacer is 40 atoms and 47.6 Å

Shipping: Ambient

References: 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.

Sphere-Like Protein-Glycopolymer Nanostructures Tailored by Polyassociation. Franka Ennen, Philipp Fenner, Susanne Boye, Albena Lederer, Hartmut Komber, Brigitte Voit, and Dietmar Appelhans. Biomacromolecules. 2015, 16 (12) pp 3731-4032. December 1, 2015. DOI: 10.1021/acs.biomac.5b00975.

Sialylation of IgG Fc domain impairs complement-dependent cytotoxicity. Isaak Quast, Christian W. Keller, Michael A. Maurer, John P. Giddens, Bjorn Tackenberg, Lai-Xi Wang, Christian Munz, Falk Nimmerjahn, Marinos C. Dalakas and Jan D. Lunemann. The Journal of Clinical Investigation. 2015, August 25, 2015. DOI: 10.1172/JCI82695.

NV Center Electron Paramagnetic Resonance of a Single Nanodiamond Attached to an Individual Biomolecule. Richelle M. Teeling-Smith, Young Woo Jung, Nicolas Scozzaro, Jeremy Cardellino, Isaac Rampersaud, Justin A North, Marek Simon, Vidya P. Bhallamudi, Arfaan Rampersaud, Ezekiel Johnston-Halperin, Michael G. Poirier, and P. Chris Hammel. Mesoscale and Nanoscale Physics. 2015. November 21, 2015. DOI: arXiv:1511.06831v1.

Magnetic Separation of Melenoma-Specific Cytoxic T Lymphocytes from a Vaccinated Melanoma Patients’s Blood Using MHC/Peptide Complex-Conjugated Bacterial Magnetic Particles, Masayuki Takahashi, Yasuto Akiyama, Junpei Ikezumi, Takeshi Nagata, Tomoko Yoshino, Akira Iizuka, Ken Yamaguchi, and Tadashi Matsunaga. Bioconjugate Chemistry. 2009, 20 (2) pp 304–309. January 14, 2009. DOI: 10.1021/bc800398d.

Delivery of NADPH-Cytochrome P450 Reductase Antisense Oligos Using Avidin-Biotin Approach. Venkateswaren C. Pillai, Rekha Yesudas, Imam H. Shaik, Thomas J. Thekkumkara, Ulrich Bickel, Kalkunte S. Srivenugopal, and Reza Mehvar. Bioconjugate Chemistry. 2010, 21 (2) pp 203–207. January 11, 2010. DOI: 10.1021/bc900449b.

Trafficking of immature _F508-CFTR to the plasma membrane and its detection by biotinylation. Yishan Luo, Ken McDonald and John W. Hanrahan. Biochem J. 2009, 419 pp 211–219. December 8, 2008. doi:10.1042/BJ20081869.

Characterization of Particle Translocation through Mucin Hydrogels. Oliver Lieleg, Ioana Vladescu, and Katharina Ribbeck. Biophysical Journal. 2010, 98 (9) pp 1782–1789. May 5, 2010. DOI: 10.1016/j.bpj.2010.01.012.

Single and multiple bonds in (strept)avidin–biotin interactions. Jean-Marie Teulon, Yannick Delcuze, Michael Odorico, Shu-wen W. Chen, Pierre Parot and Jean-Luc Pellequer. Journal of Molecular Recognition. 2011, 24 (3) pp 490–502. April 4, 2011. DOI:10.1002/jmr.1109.

Quantitative Label-Free Characterization of Avidin-Biotin Assemblies on Silanized Glass. Li-Jung Chen, Jeong Hyun Seo, Michael J. Eller, Stanislav V. Verkhoturov, Sunny S. Shah, Alexander Revzin, and Emile A. Schweikert. Analytical Chemistry. 2011, 83 (18) pp 7173–7178. August 15, 2011. DOI:10.1021/ac2016085.

Regulation of Integrin Adhesions by Varying the Density of Substrate-Bound Epidermal Growth Factor. Tamar Shahal Benjamin Geiger Iain E. Dunlop Joachim P. Spatz. Biointerphases. 2012, 7 (23) February 13, 2012. DOI 10.1007/s13758-012-0023-0.

Highly bright avidin-based affinity probes carrying multiple lanthanide chelates. Laura Wirpsza, Shyamala Pillai, Mona Batish, Salvatore Marras, Lev Krasnoperov, Arkady Mustaev. Journal of Photochemistry and Photobiology B: Biology. 2012, 116 pp 22-29. November 5, 2012. DOI: 10.1016/j.jphotobiol.2012.07.001.

Alternative mRNA Splicing Generates Two Distinct ADAM12 Prodomain Variants. Sara Duhachek-Muggy, Hui Li, Yue Qi, Anna Zolkiewska. PLOS ONE. 2013, 8 (10) e75730. October 7, 2013. DOI: 10.1371/journal.pone.0075730.

The detection of biomolecules using self-assembled microspheres in an immunoassay. Chen-Hao Chen, Huei-Shian Lin & James R. Carey. Innovation, Communication and Engineering. 2014. January 2, 2014.

Visualizing mechanical tension across membrane receptors with a fluorescent sensor. Daniel R Stabley, Carol Jurchenko, Stephen S Marshall & Khalid S Salaita. Nature Methods. 2011, 9, PP 64–67. October 30, 2011. DOI: 10.1038/nmeth.1747.

Topography and Recognition Imaging with the Agilent 6000ILM, an Integrated AFM/ILM. W. Travis Johnson, Ph.D. Agilent Technologies, Inc. 2011, 5990-8982EN. August 24, 2011. www.agilent.com/find/afm.

Silicon Nanoribbons for Electrical Detection of Biomolecules. Niklas Elfström, Amelie Eriksson Karlström, Jan Linnros. Nano Letters. 2008, 8 (3) pp 945-949. February 12, 2008. DOI: 10.1021/nl080094r.

Engineering of novel tamavidin 2 muteins with lowered isoelectric points and lowered non-specific binding properties. Yoshimitsu Takakura, Naomi Oka, Hitomi Kajiwara, Masako Tsunashima. Journal of Bioscience and Bioengineering. 2012, 114 (5) pp 485-489. November 2012. DOI: 10.1016/j.jbiosc.2012.06.009.

Development of immobilized enzyme reactors based on human recombinant cytochrome P450 enzymes for phase I drug metabolism studies. R. Nicoli, M. Bartolini, S. Rudaz, V. Andrisano, J.-L. Veuthey. Journal of Chromatography A. 2008, 1206 (1) pp 2-10. October 3, 2008. DOI: 10.1016/j.chroma.2008.05.080.

An adsorption chromatography assay to probe bulk particle transport through hydrogels. VLADESCU, O. LIELEG, S. JANG, KATHARINA RIBBECK. Journal of Pharmaceutical Sciences. 2012, 101 (1) pp 436-442. September 8, 2011. DOI: 10.1002/jps.22737.

Selection of human antibody fragments by phage display. Lee, C.M, Iorno, N., Sierro, F. and Christ, D. Nature Protocol. 2007, 2(11) pp 3001-3008. November 15, 2007. DOI:10.1038/nprot.2007.448.

Kinetic Approach to Pathway Attenuation Using XOMA 052, a Regulatory Therapeutic Antibody That Modulates Interleukin-1 b Activity. Marina K. Roell, Hassan Issafras, Robert J. Bauer, Kristen S. Michelson, Nerissa Mendoza, Sandra I. Vanegas, Lisa M. Gross, Paul D. Larsen, Daniel H. Bedinger, David J. Bohmann, Genevieve H. Nonet, Naichi Liu, Steve R. Lee, Masahisa Handa, Seema S. Kantak, Arnold H. Horwitz, John J. Hunter, Alexander M. Owyang, Amer M. Mirza, John A. Corbin and Mark L. White. The Journal of Biological Chemistry. 2010, 285 pp 20607-20614. April 21, 2010. DOI: 10.1074/jbc.M110.115790.

Multiplexed protein analysis using encoded antibody-conjugated microbeads. Nora Theilacker, Eric E. Roller, Kristopher D. Barbee, Matthias Franzreb and Xiaohua Huang. J. R. Soc. Interface. 2011, 12 (109) pp 1104-1111. January 19, 2011. DOI: 10.1098/rsif.2010.0594.

Hepatocyte Targeting of Nucleic Acid Complexes and Liposomes by a T7 Phage p17 Peptide. So C. Wong, Darren Wakefield, Jason Klein, Sean D. Monahan, David B. Rozema, David L. Lewis, Lori Higgs, James Ludtke, Alex V. Sokoloff, and Jon A. Wolff. Molecular Pharmaceutics. 2006, 3 (4) pp 386-397. March 28, 2006. DOI: 10.1021/mp050108r.

Development of recombinant Aleuria aurantia lectins with altered binding specificities to fucosylated glycans. Patrick R. Romano, Andrew Mackay, Minh Vong, Johann deSa, Anne Lamontagne , Mary Ann Comunale , Julie Hafner , Timothy Block, Ryszard Lec, Anand Mehta. Biochemical and Biophysical Research Communications. 2011, 414 (1) pp 84-89. October 14, 2011. DOI: 10.1016/j.bbrc.2011.09.027.

Visualizing mechanical tension across membrane receptors with a fluorescent sensor. Daniel R Stabley, Carol Jurchenko, Stephen S Marshall & Khalid S Salaita. Nature Methods. 2012, 9 (1) pp 64-67. October 30, 2011. DOI:10.1038/nmeth.1747.

Chemoaffinity capture of pre-targeted prostate cancer cells with magnetic beads. Lisa Y. Wu, Tiancheng Liu, Mark R. Hopkins, William C. Davis, and Clifford E. Berkman. The Prostate. 2012, 72 (14) pp 1532-1541. April 4, 2012. DOI: 10.1002/pros.22508.

Secretome protein enrichment identifies physiological BACE1 protease substrates in neurons. Peer-Hendrik Kuhn, Katarzyna Koroniak, Sebastian Hogl, Alessio Colombo, Ulrike Zeitschel, Michael Willem, Christiane Volbracht, Ute Schepers, Axel Imhof, Albrecht Hoffmeister, Christian Haass, Steffen Roßner, Stefan Brase and Stefan F Lichtenthaler. The EMBO Journal. 2012, 31 pp 3157–3168. June 22, 2012. DOI: 10.1038/emboj.2012.173.

Additional Search Phrases:

dPEG12-biotin acid, 948595117, PEG, dPEG, discrete PEG, polyethylene glycol, PEGylation reagent, biotin, biotin label, biotin labeling, biotin avidin, biotin streptavidin, amine reactive, biotinylation, PEG12, Biotin-PEG12-acid, Biotin-PEG12-COOH, PEG12-biotin acid, Carboxy-PEG12-biotin, Biotin-PEG600-COOH, Biotin-PEG-acid



 SDS    Datasheet

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dPEG®₁₂-biotin acid

$150.00 – $975.00

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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.

Email Sales@QuantaBioDesign.com for Bulk Pricing and Custom Syntheses
Product#: 10197 Categories: , ,

Product number 10197, dPEG®12 biotin acid, is a biotinylation reagent containing a single molecular weight polyethylene glycol (PEG) spacer. This product is a free acid rather than an active ester. The terminal propionic acid group couples to amines directly using a carbodiimide such as EDC. Also, the terminal carboxylic acid can be functionalized as an N-hydroxysuccinimidyl (NHS) or 2,3,5,6-tetrafluorophenyl (TFP) ester for reaction with amines.

Biotinylation is the process of covalently attaching biotin to a molecule such as a peptide, protein, or nucleic acid, or a surface such as glass or gold. Biotinylation finds extensive use in bioconjugation research and product development. Biotin usually is poorly soluble in water, but the amphiphilic dPEG® linker imparts excellent solubility in water or aqueous buffer and organic solvent. In the past, many experiments have coupled aminocaproic acid to biotin to use as a spacer between biotin and the surface to be modified. Unfortunately, aminocaproic acid (often abbreviated as LC, for “long chain”) is highly hydrophobic. Insoluble in water, LC-biotin must be dissolved in an organic solvent such as DMF or DMSO before using it in an aqueous buffer. When conjugated to proteins or other biomacromolecules, LC-biotin can trigger aggregation and precipitation of conjugated molecules due to hydrophobic interactions. In assays, the hydrophobicity of LC-biotin also increases background noise through non-specific binding.

Amphiphilic dPEG®12 biotin acid can be dissolved both in water or aqueous buffer and in organic solvents. It does not cause aggregation or precipitation of biomolecules. Using 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) chemistry, PN10197 can be coupled directly to free primary amines in aqueous media. These free amines can be on a protein, peptide, or the treated surface of a nanoparticle. Moreover, the functionalization of the carboxylic acid with other reactive groups permits coupling directly to surfaces such as glass, gold, or magnetic nanoparticles. The linker length of dPEG®12 biotin acid (50.7 – 51.7 Å) is longer than the linker length of LC-biotin and longer than the linker length of LC-LC-biotin. The performance characteristics of dPEG®12-biotin acid are quite superior to both LC-biotin and LC-LC-biotin.

Product number 10197 is the precursor product of our popular products PN10198, NHS-dPEG®12-biotin, and PN10008, Biotin-dPEG®12-TFP ester. Many applications use this product to take advantage of the strong avidin-biotin binding interaction. Such applications include single-cell imaging of protein secretion, developing biosensors, isolating specific cell types by separation with magnetic beads, characterizing and understanding the streptavidin-biotin interaction, creating affinity-based probes, and assembling supramolecular nanostructures.

If you need bulk product in a larger package size than our standard sizes, please contact us for a quote. Our commercial capabilities permit us to manufacture this product at any scale that you need.

Application References:

  1. Hermanson, G. T. Chapter 11, (Strept)avidin-Biotin Systems. Bioconjugate Techniques, 3rd edition. Academic Press: New York, 2013, 465-505. Click here for a review of Greg’s book and a link to purchase it.
  2. Hermanson, G. T. Chapter 18, PEGylation and Synthetic Polymer Modification. Bioconjugate Techniques, 3rd edition. Academic Press: New York, 2013, 787-838.

Additional information

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

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