GENOSPHERE BIOTECHNOLOGIES

  Antibody Production Services   Genosphere Biotechnologies offers complete polyclonal antibody production services packages, including peptide or protein antigen synthesis, choice of hosts immunization, antibody purification, and quality control analyses.   Our polyclonal antibody production services are designed to meet a variety of experimental requirements. For example, depending of the planned experiments, antisera or purified antibodies can be provided. Multiple purification methods are available, including protein A and antigen affinity purification.   Purification of the antisera is used to enrich the antibody activities.   Genosphere Biotechnologies has long experience in successful polyclonal antibody development and guarantees an ELISA titer above 1:100,000.   We offer multiple packages that can fit various customer needs. Our featured development packages can guarantee the delivery of fully-validated rabbit, guinea pig, rat, or mouse   polyclonal antibodies within 70

  Phosphorylated peptide   One of the most prominent post-translational modification (PTM) is the phosphorylation of Ser, Thr and Tyr (Table 1).   These modifications that are easily reversible allow for the in vivo production of a myriad of proteins and thus manifold biological fonctions from a singly translated polypeptide that varies in their phosphorylation patterns.     Phosphorylation of serine or threonine - and to a lesser extent tyrosine- residues prompts conformational changes of the protein that modify their biological activity.   For example, it has long been recognized that hormones transmit information across the external membrane of the cells by activating transmembrane signalling systems that regulate the production of a fairly small number of chemical mediators, called second messengers. These messengers trigger the activities of protein kinases and phosphatases that modify the phosphorylation states of many intracellular proteins, thus accounting for the variety

  Peptides are molecules of biological origin that shows various activities and have diverse functions in organisms.   The incorporation of peptide modifications may have various purposes such as improving activity, tracking the peptide in the biological system under study, etc. A large variety of peptide modifications are available which are usually classified on the basis of chemical structure or chemical site of modification (Figure 1).   The peptide modifications include N-terminal modification, C-terminal modification, amino acid side chain modification, amino acid  -carbone modification and backbone modification.   Figure 1.   Peptide modifications chart.   The modifications of the peptide backbone chain or of the individual amino acids have notable effects on the physical and chemical properties of the peptide overall. It may affect the hydrophobicity and thus it can enhance water-solubility.   Figure 2.   Peptide modifications have significant effect on peptide b