Selvita has expanded its portfolio of protein chemistry services.
Analysis, production and purification of recombinant proteins remain the major activities of Selvita’s Protein Chemistry Laboratory. These projects require high expertise in the design of genetic constructs, determination and selection of the optimal expression conditions and finally production and purification of recombinant proteins with highest purity and biological activity.
“Being aware of the importance of the protein targets at every step of the preclinical drug discovery process, we place a great emphasis on the quality of our protein products. The highest purity and biological activity of the proteins, which we deliver to our customers, are our major objective and concern,” said Dr Justyna Stec-Niemczyk, Head of the Protein Chemistry Laboratory.
Due to the dynamic development of the Protein Chemistry Laboratory and constantly increasing portfolio of customers, Selvita is currently increasing its capabilities in terms of proteomic analyses. These analyses can be used for instance for biosimilar product characterization, which are currently of high interest to many biotechnology companies. Expansion of the service offer is possible due to the access to the extended range of the state of the art scientific equipment. This includes highly sophisticated mass spectrometers (e.g., MALDI-TOF MS microflex LT, LC/MS ESI/Apci Q-TOF plus, LC/MS/TSQ, LC/RAPID/MS/DAD/ESI/IT), additional ultra HPLC systems with the range of the specialized detectors (e.g. UV-VIS, RI, DAD, ELSD, Corona CAD, MALS, DLS, FLD); and microscale thermophoresis measurement devices (Nanotemper Monolith NT).
Selvita’s protein chemistry offer, in addition to already available services such as, protein assays and PAGE patterns, LC services, N-terminal protein sequencing and amino acid analyses, CD spectra analyses and the crystallographic studies, now also includes
• Determination of intact mass of proteins including large proteins,
• Analysis of the posttranslational modifications,
• Determination of protein oligomeric state (quaternary structure) and aggregation
• Protein conformation stability
• Biophysical methods for the determination of various parameters of protein-protein and protein-ligand interactions.
