Product Details of 152942-06-8On November 7, 2018 ,《Single-Site Labeling of Native Proteins Enabled by a Chemoselective and Site-Selective Chemical Technology》 appeared in Journal of the American Chemical Society. The author of the article were Adusumalli, Srinivasa Rao; Rawale, Dattatraya Gautam; Singh, Usha; Tripathi, Prabhanshu; Paul, Rajesh; Kalra, Neetu; Mishra, Ram Kumar; Shukla, Sanjeev; Rai, Vishal. The article conveys some information:
Chem. biol. research often requires precise covalent attachment of labels to the native proteins. Such methods are sought after to probe, design, and regulate the properties of proteins. At present, this demand is largely unmet due to the lack of empowering chem. technol. Here, we report a chem. platform that enables site-selective labeling of native proteins. Initially, a reversible intermol. reaction places the “”chem. linchpins”” globally on all the accessible Lys residues. These linchpins have the capability to drive site-selective covalent labeling of proteins. The linchpin detaches within physiol. conditions and capacitates the late-stage installation of various tags. The chem. platform is modular, and the reagent design regulates the site of modification. The linchpin is a multitasking group and facilitates purification of the labeled protein eliminating the requirement of addnl. chromatog. tag. The methodol. allows the labeling of a single protein in a mixture of proteins. The precise modification of an accessible residue in protein ensures that their structure remains unaltered. The enzymic activity of myoglobin, cytochrome C, aldolase, and lysozyme C remains conserved after labeling. Also, the cellular uptake of modified insulin and its downstream signaling process remain unperturbed. The linchpin directed modification (LDM) provides a convenient route for the conjugation of a fluorophore and drug to a Fab and monoclonal antibody. It delivers trastuzumab-doxorubicin and trastuzumab-emtansine conjugates with selective antiproliferative activity toward Her-2 pos. SKBR-3 breast cancer cells. In the experimental materials used by the author, we found Ethyl 4-(4-formyl-3-hydroxyphenoxy)butanoate(cas: 152942-06-8Product Details of 152942-06-8)
Ethyl 4-(4-formyl-3-hydroxyphenoxy)butanoate(cas: 152942-06-8) belongs to esters. They are important in biology, being one of the main classes of lipids and comprising the bulk of animal fats and vegetable oils.Product Details of 152942-06-8 They perform as high-grade solvents for a broad array of plastics, plasticizers, resins, and lacquers, and are one of the largest classes of synthetic lubricants on the commercial market. Polyesters are important plastics, with monomers linked by ester moieties.
Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics