GLUL also known as Glutamine synthetase. It is a trimetallic enzyme containing two divalent cation sites and one monovalent cation site per subunit. GLUL is able to regulate intracellular concentrations of glutamate and catalyzes the synthesis of glutamine form glutamate and ammonia. It is ubiquitously expressed in the human and plays a major role for many metabolic pathways such as cell proliferation, inhibition of apoptosis, and cell signaling. Recombinant protein corresponding to aa1-373 from human CLUL expressed in E. coli. Accession: NP_001028216 Molecular Weight: ~42kD (373aa), confirmed by MALDI-TOF Specific Activity: >2000pmol/min/ug, and is defined as the amount of enzyme that convert L-glutamate to L-glutamine/minute at pH 7.5 at 37C in coupled system with PK/LDH. Amino Acid Sequence: MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL LNETGDEPFQ YKN 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.
