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GLUL recombinant protein :: Glutamine Synthetase Recombinant Protein

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Catalog # MBS143992
Unit / Price
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  0.005 mg  /  $140 +1 FREE 8GB USB
  0.02 mg  /  $205 +1 FREE 8GB USB
  1 mg  /  $2,665 +3 FREE 8GB USB
GLUL recombinant protein
Product Name

Glutamine Synthetase (GLUL), Recombinant Protein

Popular Item
Full Product Name

Recombinant Human Glutamine Synthetase

Product Synonym Names
GLUL Human; Glutamine Synthetase Human Recombinant; GLNS; EC 6.3.1.2; EC 4.1.1.15; GLUL; Glutamine Synthetase; GS; Glutamate decarboxylase; Glutamate--ammonia ligase; PIG43; PIG59
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence
MGSSHHH HHH 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
OMIM
138290
3D Structure
ModBase 3D Structure for P15104
Host
E Coli
Purity/Purification
Greater than 90.0% as determined by SDS-PAGE.
Form/Format
GLUL Human solution containing 20mM Tris-HCl pH-8, 5mM DTT, 0.2M NaCl & 20% glycerol.
Sterile filtered colorless solution.
Other Notes
Small volumes of GLUL recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
GLUL recombinant protein
Description: GLUL Recombinant Human produced in E Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-373 a.a.) and having a molecular mass of 44.2 kDa. The GLUL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Introduction: GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.
NCBI/Uniprot data below describe general gene information for GLUL. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
42,064 Da
NCBI Official Full Name
glutamine synthetase
NCBI Official Synonym Full Names
glutamate-ammonia ligase
NCBI Official Symbol
NCBI Official Synonym Symbols
GS; GLNS; PIG43; PIG59
  [Similar Products]
NCBI Protein Information
glutamine synthetase; cell proliferation-inducing protein 59; glutamate decarboxylase; glutamine synthase; proliferation-inducing protein 43
UniProt Protein Name
Glutamine synthetase
UniProt Synonym Protein Names
Glutamate decarboxylase (EC:4.1.1.15); Glutamate--ammonia ligase
Protein Family
UniProt Gene Name
UniProt Synonym Gene Names
GLNS; GS  [Similar Products]
UniProt Entry Name
GLNA_HUMAN
NCBI Summary for GLUL
The protein encoded by this gene belongs to the glutamine synthetase family. It catalyzes the synthesis of glutamine from glutamate and ammonia in an ATP-dependent reaction. This protein plays a role in ammonia and glutamate detoxification, acid-base homeostasis, cell signaling, and cell proliferation. Glutamine is an abundant amino acid, and is important to the biosynthesis of several amino acids, pyrimidines, and purines. Mutations in this gene are associated with congenital glutamine deficiency, and overexpression of this gene was observed in some primary liver cancer samples. There are six pseudogenes of this gene found on chromosomes 2, 5, 9, 11, and 12. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2014]
UniProt Comments for GLUL
GLUL: This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner. Essential for proliferation of fetal skin fibroblasts. Defects in GLUL are the cause of congenital systemic glutamine deficiency (CSGD). CSGD is a rare developmental disorder with severe brain malformation resulting in multi-organ failure and neonatal death. Glutamine is largely absent from affected patients serum, urine and cerebrospinal fluid. Belongs to the glutamine synthetase family.

Protein type: Energy Metabolism - nitrogen; Amino Acid Metabolism - alanine, aspartate and glutamate; EC 6.3.1.2; Amino Acid Metabolism - arginine and proline; Ligase; EC 4.1.1.15

Chromosomal Location of Human Ortholog: 1q31

Cellular Component: protein complex; mitochondrion; rough endoplasmic reticulum; cytoplasm; perikaryon; nerve terminal; nucleus; cytosol

Molecular Function: glutamate-ammonia ligase activity; identical protein binding; dynein light chain binding; glutamate binding; glutamate decarboxylase activity; manganese ion binding; magnesium ion binding; ATP binding

Biological Process: cell proliferation; glutamate catabolic process; synaptic transmission; glutamine biosynthetic process; response to glucose stimulus; positive regulation of insulin secretion; neurotransmitter uptake; amino acid biosynthetic process; cellular response to starvation; positive regulation of synaptic transmission, glutamatergic; positive regulation of epithelial cell proliferation; protein homooligomerization

Disease: Glutamine Deficiency, Congenital
Precautions
All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
Disclaimer
While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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