| Quantity | 25µg, 50µg | 300U | 50mg, 10mg, 100mg, 5mg, 25mg, 1mg | 100µg, 10µg, 50µg, 1mg, 25µg | 50mg |
| Description | DescriptionTyrosyl-DNA phosphodiesterase-2 (TDP2) functions to remove trapped topoisomerase II/DNA complexes by processing 5′- blocking protein (topo II) at the site of the DNA break (Fig 1). In terms of physiological relevance, there appear to be multiple roles for TDP2, well beyond the DescriptionTyrosyl-DNA phosphodiesterase-2 (TDP2) functions to remove trapped topoisomerase II/DNA complexes by processing 5′- blocking protein (topo II) at the site of the DNA break (Fig 1). In terms of physiological relevance, there appear to be multiple roles for TDP2, well beyond the repair of type II topoisomerase damage and subsequent DNA repair. This is quite different from the Top1/DNA repair protein, TDP1. There are a number of mechanistic differences between TDP1 and 2 as well (see reviews from Pommier, PMID 24856239 and https://www.uniprot.org/uniprot/O95551). In humans, TDP2 should be considered a multi-functional enzyme with roles in TNF and MAPK/JNK/p38 pathways. There is some similarity with APE1 and the superfamily of Mg++/Mn++ dependent phosphodiesterases and there is evidence that picorna viruses pirate TDP2 as a VPg un-linkase function. Given the key role for topo II in anticancer therapy, drugs that inhibit TDP2 might prove useful in combination therapy with established Interfacial Poisons (IFP) such as doxorubicin and etoposide (VP16). Indeed, when the Tdp2 gene is suppressed, cells show enhanced sensitivity to Top2 drugs, making Tdp2 an important anti-cancer target. Shipping&storageHuman TDP-2 is shipped on wet ice and should be stored at -20°C... Read More | Unit Definition One unit will cause a change in A600 of 0.330 per minute at pH 5.7 at 37°C in a 2.0 ml reaction mixture (45 minute assay) | Inquire | Inquire | Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Aladdin Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins... Read More |