Small Molecule Screening against Phosphatases

Small Molecule Screening against Phosphatases

INQUIRY

Creative BioMart offers a comprehensive selection of tools and technologies to support small molecule screening against phosphatases. Our talented scientific team is able to provide our customers with unparalleled expertise and experience in phosphatase biology and pharmaceutical research.

Background

Phosphatases are an important class of enzymes that mediate signal transduction and control diverse aspects of cellular behavior. They are critical for the maintenance of normal cell function and have also been shown to contribute significantly to disease etiology. Small molecules targeting phosphatases have been developed as important biological tools to fully elucidate the function of these important enzymes and hold promise for treating a wide range of diseases. Information on the classification of phosphatases according to their structures, known substrates and functions helps to identify substrate-based small molecules.

Small molecule screen is the process to systematically test for the ability of small molecules to inhibit, activate, or modulate a target or a biological process. A variety of approaches have been developed to identify small molecules directed to phosphatases. These useful methods can be broadly categorized as rational design based on substrate-like molecules or molecules known to act against phosphatases, or extensive screening in chemical libraries. The development of small molecules against phosphatases is essential for phosphatase research and drug discovery, however, some properties of phosphatases such as high sequence conservation and intrinsic susceptibility to oxidation bring a great challenge for small molecule screening. To overcome such concerns, new methods and tools are continuously developed.

Service Offering

Creative BioMart provides customized services based on different screening methods and strategies for efficiently identifying small molecules targeting phosphatases. We offer our extensively validated in-house small molecule libraries to accelerate the overall drug development process of our customers. Our experienced scientists will work closely with our customers to create the perfect plan for their project.

• Virtual Screening

  Virtual screening is the process of identifying new bioactive molecules by analyzing large databases or collections of compounds through computational methods. We provide both structure-based and ligand-based virtual screening services to select potential small molecules against phosphatases.

• Biochemical Screening

  A focused library of potential compounds generated from virtual screening must be tested experimentally. We have established an integrated platform covering a wide range of phosphatase assays to provide an effective workflow for biochemical screening of small molecules targeting phosphatases.

• High-throughput Screening

  As the chemical libraries increased in size, automated and robotic approaches are required. High-throughput screening is a fast solution enables the screening of large compound libraries. Our advanced HTS platform and experienced scientific team allow us to provide high-quality screening services.

Creative BioMart is an advanced biotech company within the field of kinase/phosphatase biology. We offer our expertise in establishing assays for phosphatase screening & profiling. The extensive experience of our scientific team translates into the robust wealth of knowledge that we use to provide you with the highest quality of service. We also supply a range of high-quality small molecule inhibitors, activators, agonist, and antagonists for your research. If there are any additional requirements needed, please do not hesitate to contact us.

References

• Martin K R, et al. Integrating virtual and biochemical screening for protein tyrosine phosphatase inhibitor discovery. Methods, 2014, 65(2): 219-228.
• He R, et al. Small molecule tools for functional interrogation of protein tyrosine phosphatases. The FEBS journal, 2013, 280(2): 731-750.