Tuesday, 13 January 2015

Creative Proteomics - Proteome-Related Services



Creative Proteomics is the proteomics division of CD Inc, an integrated CRO company that provides a full range of drug development services, including Molecular Biology, Biochemistry, Systems Biology, Organic Chemistry, Genomics, Bioinformatics, Structural Biology, Preclinical and Clinical studies.

Creative Proteomics offers iTRAQ proteinquantification analysis service suited for unbiased untargeted biomarker discovery. Relative quantification of proteins for biomarker discovery in complex mixtures by mass spectrometry can easily and quickly be achieved using iTRAQ technology. iTRAQ is ideally suited for comparing normal, diseased, and drug-treated samples, time course studies, biological replicates and provides relative quantitation.




SILAC-basedquantitative proteomics (SILAQ) is an innovative technology used in high throughput quantitative analysis of large protein complexes, protein-protein and protein-small molecule interactions. SILAC service of Creative Proteomics provides an unbiased strategy that can reveal how specifically either inhibitors, or other perturbations, affect the dynamic properties and cellular distributions of proteins. It can also be used as a sensitive and effective method to determine the specific interaction partners of proteins in the cell.

Di-Sulfide Bond Localization
For many proteins and peptides, disulfide bridges are prerequisite for their proper biological function. Many commercialized proteins are cross-linked by disulfide bridges that increase their resistance to destructive effects of extreme environment used in industrial processes or protect protein-based therapeutics from rapid proteolytic degradation. Manufacturing of these products must take into account oxidative refolding—a formation of native disulfide bonds by specific pairs of cysteines located throughout a sequence of linear protein.

Disulfidebonds play an important role in the folding and stability of some proteins, usually proteins secreted to the extracellular medium. Since most cellular compartments are reducing environments, in general, disulfide bonds are unstable in the cytosol, with some exceptions as noted below, unless a sulfhydryl oxidase is present