Biotin-labelled peptides have many important applications in immunology and histochemistry, such as affinity purification and FRET-based flow cytometry, solid-phase immunoassays, and receptor localization, that exploit the high affinity of streptavidin and avidin for biotin.
The most popular reagent for cleavage of peptides from Boc-based resins is anhydrous HF. Of all the cleavage procedures HF appears to be the most versatile and least harmful to a wide variety of peptides synthesized on Boc-based resins.
Novabiochem® product range has one of the largest collections of orthogonally and quasi-orthogonally protected tri-functional amino acids. These derivatives are useful tools for the synthesis of cyclic and branched peptides and peptides carrying side-chain modifications.
The Novabiochem® product line has one of the most extensive ranges of polymer-supports for solid phase peptide synthesis. They range from high-loaded, lows welling for the large-scale production of relatively short peptides to high-swelling, low-loaded for the synthesis of long
Novabiochem® offers a large number of coupling reagents for in situ activation. In situ activating reagents are easy to use, fast reacting – even with sterically hindered amino acids, and their use is generally free of side reactions.
Novabiochem® has one of the most extensive ranges of linkers and derivatized resins for Fmoc solid phase peptide synthesis. These resins have varied properties with special protocols for loading and cleaving.
Our long peptide purification utilizes a combination of chemoselective purification tags and standard RP-HPLC. The method is especially effective at removing impurities that are closely eluting or hidden under the isolated product peak
Review methods and resins for attaching amino acids and peptides, including Merrifield, trityl-based, and hydroxymethyl-functionalized resins. Resin-immobilized peptides can be used for various downstream applications.
Fmoc resin cleavage and deprotection follows the difficult task of detaching the peptide from the resin support and removing all the side-chain protecting groups of the amino acid residues to yield the desired peptide.