|Calculated MW||42 kDa|
|Other Names||GLNS, GS, PIG43, PIG59, GLUL|
|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||-20°C;In 20 mM Tris-HCl buffer (pH8.0) containing 10% glycerol 1 mM DTT, 0.1 mM PMSF|
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Provided below are standard protocols that you may find useful for product applications.
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 Human GLUL was expressed in E.coli and purified by using conventional chromatography techniques.
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