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|Product Name||GLUL, 1-373aa, Human|
|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|
|Background||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. Recombinant GLUL protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.|
|Concentration||1 mg/ml (determined by Bradford assay)|
|Form||Liquid, in 20 mM Tris-HCl Buffer (pH 8.0) containing 10% Glycerol|
|Intended Use||For Research Use Only|
|Molecular Weight||39.9 kDa(362aa), confirmed by MALDI-TOF|
|NCBI Accession #||NP_001028216|
|Purity||> 90% by SDS-PAGE|
|References||Vermeulen T., et al, (2008) Arch Biochem Biophys. 478:96-102
Liaw SH., et al. (1995) Protein Sci. 4 (11): 2358-65.
|Storage||Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -20C or -70C. Avoid repeated freezing and thawing cycles.|
|Synonyms||GS, GLNS, Glutamine synthetase, Glutamate-ammonia ligase, Glutamate decarboxylase|
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