Glutamine synthetase (GLUL), which is therefore able to regulate intracellular concentrations of glutamate. GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a main source of energy and is involved in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is essential for proliferation of fetal skin fibroblasts and plays an important role in controlling body pH by removing ammonia from circulation. Mutations in GLUL are associated with congenital glutamine deficiency. Source: Recombinant protein corresponding to aa1-373 from human GLUL, fused to His-Tag at N-terminal, expressed in E. coli. Molecular Weight: ~44.2kD (393aa), confirmed by MALDI-TOF Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH 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 Specific Activity: >2800pmol/min/ug, and is defined as the amount of enzyme that convert 1pmole of L-glutamate to L-glutamine/minute at pH 7.5 at 37C in coupled system with PK/LDH. 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.
