| Thymidylate synthase is an intracellular enzyme critical for de novo synthesis of DNA. This function maintains the dTMP(thymidine-5-prime monophosphate) pool critical for DNA replication and repair. In cancer, expression of this protein is often elevated and becomes further elevated as a result of treatment with the most commonly used chemotherapeutic, 5-fluorouracil (5-FU). Resistance or lack of response to 5-FU is attributed to the elevation of thymidylate synthase activity. Recombinant human Thymidylate synthase protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques. Recombinant human Thymidylate synthase protein, fused to His-tag at N-terminus, was expressed in E. coli AA sequence: MGSSHHHHHH SSGLVPRGSH MPVAGSELPR RPLPPAAQER DAEPRPPHGE LQYLGQIQHI LRCGVRKDDR TGTGTLSVFG MQARYSLRDE FPLLTTKRVF WKGVLEELLW FIKGSTNAKE LSSKGVKIWD ANGSRDFLDS LGFSTREEGD LGPVYGFQWR HFGAEYRDME SDYSGQGVDQ LQRVIDTIKT NPDDRRIIMC AWNPRDLPLM ALPPCHALCQ FYVVNSELSC QLYQRSGDMG LGVPFNIASY ALLTYMIAHI TGLKPGDFIH TLGDAHIYLN HIEPLKIQLQ REPRPFPKLR ILRKVEKIDD FKAEDFQIEG YNPHPTIKME MAV Enzyme Activity: Not determined. This product is recommended for use in applications that do not require a catalytically active form of the protein. Storage and Stability: May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20C. Aliquots are stable for 6 months after receipt at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer. |
