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Press Release

Advanced Disulfide Bond Analysis Developed by Creative Proteomics

Creative proteomics
Posted on: 15 Oct 18

New York – October 15, 2018- Creative Proteomics announced the launching of advanced disulfide bond analysis service. Creative Proteomics has established has established a highly sensitive and reliable HPLC-MS/MS platform that can analyze disulfide bonds in multiple samples and in both eukaryotic and prokaryotic organisms.

A disulfide bond is a covalent bond between two sulfur atoms, which can be prevalent in biology and found in a range of biological molecules. However, the other sulfur-containing amino acid, methionine, cannot construct disulfide bonds as it is a covalent bond, disulfide bond is normally considered to be the primary structure. Because of the particularity of protein disulfide bonds, they can fulfill a wide range of functions including promoting protein stability and regulating protein activity or function. It is also notable that the function of disulfide bonds are far more than components of primary protein structure, they are very critical in stabilizing the tertiary and quartenary structures, and are the prerequisite of proteins’ proper biological function.

To be specific, disulfide bonds play an important role in biological physiology which is not only at tertiary structure level but also quartenary structure level. Due to the ability to stabilize overall structure of proteins, disulfide bridges are cross-linked in many commercialized proteins, which could increase their resistance to destructive effects of the extreme environment used in industrial processes or protect protein-based therapeutics from rapid proteolytic degradation. Manufacturing of these products must consider oxidative refolding—a formation of native disulfide bonds by specific pairs of cysteines located throughout a sequence of the linear protein. Thus, based on their characteristics, disulfide bond analysis is widely used in the biological research area. For example, they can be applied in studying unknown disulfide bonds in novel proteins and analyze disulfide bonds in refolded proteins to test whether a protein is correctly folded. Our company provides reliable, rapid and cost-effective disulfide bond analysis services based on optimized protocol combine with excellent reproducibility, high and ultra-sensitivity process to enable more fast and sensitive site mapping service for disulfide bond analysis.

Creative Proteomics is continuing to optimize analytical HPLC-MS/MS platform and continued modification including developing mapping service reducing turnaround time to make it more efficient and effective. The final goal of our company is to provide a tailor-made service with rapid analysis procedures and clearly report by applying sensitive, reliable, and accurate analysis methods, which allows us to build an ideal scientific model to speed up your Protein Post-translational Modification Analysis related research.

 

About Creative Proteomics:

Creative Proteomics is programming a full range of services to support various proteome-related researches from identification of single proteins to large-scale proteomic studies. The advancement of our proteomics analysis platforms and our specialized employees allows us to provide efficient high throughput and super-sensitivity services. Our service includes a thorough discussion and counseling of your projects, in order to offer you the optimal service to meet your needs. In close cooperation with our partners, we will find out the best professional proteomics solutions. In addition to offering analyses of protein post-translational modifications such as Di-Sulfide Bond Localization analysis and protein sumoylation. Our team is committed to providing you with the optimal service for your research needs basing at the lowest cost level in the industry. More information is available at Creative Proteomics website.

Editor's Details

sherry cryer
Creative proteomics
www.creative-proteomics.com
1-631-619-7922
contact@creative-proteomics.com

Last updated on: 15/10/2018

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