Sulfation of tyrosine residues is an important post-translational modification that occurs on manysecretory as well as transmembrane proteins. It has been suggested that up to 1% of all tyrosine residues of the overall protein content in an organism are sulfated which makes this modification essential for numerous biological processes. However, one of the factors hindering the study of the significance of sulfotyrosine (sTyr) within a protein is the absence of a general method that enables the synthesis of sTyr peptides in satisfactory yields and purity.

Cyclic peptides can reduce the backbone flexibility of the linear peptides, therefore increase the rigidity of the molecular and limit the possible conformations of the peptides. These kinds of structural constrain is very important to the structural stability and biological activity.

  1. D-Amino Acid
  2. Aib, Abu, Ahx, Abz,β-Ala, Cit, Cha, Chg, Dab, Hyp, Har, Nle, Nva, Nal, Pyr, Orn, Phg, Sar
  3. Cys(tBu), Cys(Acm), Lys(Ac), Lys(Biotin), Lys(TFA)
  4. Seleno-Met

MAP (Multiple-Antigen peptide)

The main goal of the MAP is to bring small antigen peptides together in close proximity so that the molecular will have higher antigenicity which in turn gives higher antigen response.

Inter-chain disulfide

Usually, the antigen peptides are too small to generate adequate immunological response. Therefore they need to be conjugated to a carrier protein. Most commonly used carrier proteins include KLH, BSA and OVA.

We provide the service of peptide conjugation to all above three carrier proteins.