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Buccutite™ FOL, maleimide [FOLM]

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Telephone1-800-990-8053
Fax1-800-609-2943
Emailsales@aatbio.com
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ShippingStandard overnight for United States, inquire for international
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Physical properties
Molecular weight523.63
SolventDMSO
Storage, safety and handling
H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageFreeze (< -15 °C); Minimize light exposure
UNSPSC12171501
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Show More (38)

OverviewpdfSDSpdfProtocol


Molecular weight
523.63
Buccutite™crosslinking technology provides the most convenient and effective crosslinking method to link two biomolecules with a high conjugation yield. The method uses one pair of crosslinkers: Buccutite™ MTA and Buccutite™ FOL. MTA is added to one molecule, while FOL is added to another molecule. The cross-linking reaction is initiated by mixing Molecule-1-Buccutite ™ MTA and Molecule-2-Buccutite ™ FOL under neutral conditions. Many of our customer have requested us to offer the stand-alone Buccutite™ MTA and Buccutite™ FOL reagents to expand the application of Buccutite™crosslinking technology. Buccutite™ FOL maleimide (FOLM) can be used the same way as the widely used SMCC for crosslinking proteins. One end of the FOLM reacts (via maleimide) with thiols (-SH) of cysteineS found in the reduced antibodies (by TCEP or DTT) to give FOL-modified reduced antibodies. Buccutite™ crosslinking reaction occurs under extremely mild and neutral conditions without any catalyst required while the SMCC crosslinking requires high concentration of proteins. In addition, SMCC-modified protein is extremely unstable and often self-reactive since proteins often contain both amine and thiol groups that cause significant amount of homo-crosslinking. Buccutite™ crosslinking is robust and efficient.

Calculators


Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of Buccutite™ FOL, maleimide [FOLM] to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.

0.1 mg0.5 mg1 mg5 mg10 mg
1 mM190.975 µL954.873 µL1.91 mL9.549 mL19.097 mL
5 mM38.195 µL190.975 µL381.949 µL1.91 mL3.819 mL
10 mM19.097 µL95.487 µL190.975 µL954.873 µL1.91 mL

Molarity calculator

Enter any two values (mass, volume, concentration) to calculate the third.

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References


View all 21 references: Citation Explorer
N-Hydroxysuccinimide-Modified Ethynylphosphonamidates Enable the Synthesis of Configurationally Defined Protein Conjugates.
Authors: Kasper, Marc-André and Gerlach, Marcus and Schneider, Anselm F L and Groneberg, Christiane and Ochtrop, Philipp and Boldt, Stefanie and Schumacher, Dominik and Helma, Jonas and Leonhardt, Heinrich and Christmann, Mathias and Hackenberger, Christian P R
Journal: Chembiochem : a European journal of chemical biology (2020): 113-119
MicroSPECT/CT Imaging of Cell-Line and Patient-Derived EGFR-Positive Tumor Xenografts in Mice with Panitumumab Fab Modified with Hexahistidine Peptides To Enable Labeling with 99mTc(I) Tricarbonyl Complex.
Authors: Ku, Anthony and Chan, Conrad and Aghevlian, Sadaf and Cai, Zhongli and Cescon, David and Bratman, Scott V and Ailles, Laurie and Hedley, David W and Reilly, Raymond M
Journal: Molecular pharmaceutics (2019): 3559-3568
Understanding How the Stability of the Thiol-Maleimide Linkage Impacts the Pharmacokinetics of Lysine-Linked Antibody-Maytansinoid Conjugates.
Authors: Ponte, Jose F and Sun, Xiuxia and Yoder, Nicholas C and Fishkin, Nathan and Laleau, Rassol and Coccia, Jennifer and Lanieri, Leanne and Bogalhas, Megan and Wang, Lintao and Wilhelm, Sharon and Widdison, Wayne and Pinkas, Jan and Keating, Thomas A and Chari, Ravi and Erickson, Hans K and Lambert, John M
Journal: Bioconjugate chemistry (2016): 1588-98
2-(Maleimidomethyl)-1,3-Dioxanes (MD): a Serum-Stable Self-hydrolysable Hydrophilic Alternative to Classical Maleimide Conjugation.
Authors: Dovgan, Igor and Kolodych, Sergii and Koniev, Oleksandr and Wagner, Alain
Journal: Scientific reports (2016): 30835
Preparation and characterization of albumin conjugates of a truncated peptide YY analogue for half-life extension.
Authors: Ehrlich, George K and Michel, Hanspeter and Truitt, Theresa and Riboulet, William and Pop-Damkov, Petar and Goelzer, Petra and Hainzl, Dominik and Qureshi, Farooq and Lueckel, Barbara and Danho, Waleed and Conde-Knape, Karin and Konkar, Anish
Journal: Bioconjugate chemistry (2013): 2015-24
Enhanced extravasation, stability and in vivo cardiac gene silencing via in situ siRNA-albumin conjugation.
Authors: Lau, Shannen and Graham, Bim and Cao, Nga and Boyd, Ben J and Pouton, Colin W and White, Paul J
Journal: Molecular pharmaceutics (2012): 71-80
Protein labeling with the labeling precursor [(18)F]SiFA-SH for positron emission tomography.
Authors: Wängler, Björn and Kostikov, Alexey P and Niedermoser, Sabrina and Chin, Joshua and Orchowski, Katy and Schirrmacher, Esther and Iovkova-Berends, Liuba and Jurkschat, Klaus and Wängler, Carmen and Schirrmacher, Ralf
Journal: Nature protocols (2012): 1964-9
Commercially Supplied Amine-Modified siRNAs May Require Ultrafiltration prior to Conjugation with Amine-Reactive Compounds.
Authors: Lau, Shannen and Graham, Bim and Boyd, Ben J and Pouton, Colin W and White, Paul J
Journal: Journal of nucleic acids (2011): 154609
Comparison of hydrazone heterobifunctional cross-linking agents for reversible conjugation of thiol-containing chemistry.
Authors: Christie, R James and Anderson, Diana J and Grainger, David W
Journal: Bioconjugate chemistry (2010): 1779-87
Synthesis, characterization and in vitro evaluation of a bone targeting delivery system for salmon calcitonin.
Authors: Bhandari, Krishna Hari and Newa, Madhuri and Uludag, Hasan and Doschak, Michael R
Journal: International journal of pharmaceutics (2010): 26-34