Recombinant Rat Glutamine synthetase (Glul)

Code CSB-YP009553RA
MSDS
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Source Yeast
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Code CSB-EP009553RA
MSDS
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Source E.coli
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Code CSB-EP009553RA-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP009553RA
MSDS
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Source Baculovirus
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Code CSB-MP009553RA
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Glul
Uniprot No.
Alternative Names
Glul; GlnsGlutamine synthetase; GS; EC 6.3.1.2; Glutamate--ammonia ligase; Palmitoyltransferase GLUL; EC 2.3.1.225
Species
Rattus norvegicus (Rat)
Expression Region
2-373
Target Protein Sequence
ATSASSHLN KGIKQMYMNL PQGEKIQLMY IWVDGTGEGL RCKTRTLDCD PKCVEELPEW NFDGSSTFQS EGSNSDMYLH PVAMFRDPFR RDPNKLVFCE VFKYNRKPAE TNLRHSCKRI MDMVSSQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY RACLYAGIKI TGTNAEVMPA QWEFQIGPCE GIRMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLRCI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRIVG QEKKGYFEDR RPSANCDPYA VTEAIVRTCL LNETGDEPFQ YKN
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine. Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia. Essential for proliferation of fetal skin fibroblasts. Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation. May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ. Plays a role in ribosomal 40S subunit biogenesis.
Gene References into Functions
  1. Results showed that status epilepticus (SE) induced in immature rats elicits a persistent decrease in glutamine synthetase-immunoreactivity in the dentate hilus, which can be detected as early as 2 weeks and persists up to at least 19 weeks after SE PMID: 25350774
  2. The portacaval shunt caused a marked decrease in glutamine synthetase activity and an increase in ornithine aminotransferase activity. PMID: 23656379
  3. the results provided evidence for the temporospatial expression and location of GS following spinal cord injury. PMID: 23525248
  4. Prolonged hyposmotic challenge transiently increases astrocyte-specific glutamine synthetase levels in the supraoptic nucleus, followed by a rebound increase of their activity. PMID: 23361961
  5. we also show that the upstream enhancer of the rat GS gene can confer pericentral activity to a linked reporter gene, and that the activity of this enhancer is also beta catenin dependent. PMID: 22544812
  6. Manganese exposure inhibited glutamine uptake and glutamine synthetase expression in rat astrocytes. PMID: 22391793
  7. Significantly increased expression of glutamine synthetase and glutamate aspartate transporter at 40 mmHg pressure was observed in Muller cells. PMID: 22134673
  8. deficient glial glutamate transporters and glutamine synthetase significantly attenuate GABAergic synaptic strength in the spinal dorsal horn PMID: 22339645
  9. Glutamine synthetase may modulate motility and substrate adhesion through transmembrane integrin beta1 signaling to the cytoskeleton and by membrane type 1-matrix metalloproteinase-mediated proteolysis of the extracellular matrix. PMID: 21193003
  10. The testicular GLUL (glutamate-ammonia ligase )is the first testicular protein shown to be affected by nickel exposure. PMID: 21254280
  11. In mimicked diabetic condition, IL-1 beta decreases the expression of glutamine synthetase in retinal Muller cells. PMID: 18001575
  12. Glutamine synthase (GS) expression in neurons occurs in response to reduced availability of glutamine from astrocytes; neuronal GS expression represents a default phenotype which is normally suppressed via direct contacts with astrocytes. PMID: 20557426
  13. These results suggest that Glns in astrocytes may represent a novel target for neuroprotection against neuronal dysfunction PMID: 20064572
  14. Glutamine synthetase expression after glucocorticoid administration in hepatoma cells PMID: 12200152
  15. glutamine synthetase is an important regulatory component of the availability of the ammonium ions to be excreted for defending systemic acid-base balance PMID: 12871952
  16. Glutamine synthetase silencer elements is absent in liver cells that respond to glucocortoids with enhanced expression of the enzyme. PMID: 14563934
  17. Lipopolysaccharide impairs hepatic ammonia detoxification by both downregulation of GS and its inactivation because of tyrosine nitration PMID: 15830392
  18. The investigators studied the interactions between the upstream enhancer, regulatory regions in the first intron, and the 3'-untranslated region and immediate downstream genomic sequences of the GS gene (the GS "tail"). PMID: 16839656
  19. Glns activity was determined in skeletal muscle and liver 24h after the last psychological stress and immobilization stress. PMID: 17170234
  20. glutamine synthetase has a role in control of glutamate signalling through Wnt3A and steroid pathways in osteoblastic cells PMID: 18555765
  21. GS localization was investigated using immunohistochemistry and double-labeling of young and adult human and rat skin sections as well as skin cells in culture. PMID: 19204801
  22. Results describe glutamine synthetase activity and glutamate uptake in the hippocampus and frontal cortex from rats with prehepatic portal vein hypertension. PMID: 19533812
  23. Glutamate at >or=1 mM induced a prolonged increase of GS expression in contrast to glutamate transporters. PMID: 19728998

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Subcellular Location
Cytoplasm, cytosol. Microsome. Mitochondrion. Cell membrane; Lipid-anchor.
Protein Families
Glutamine synthetase family
Tissue Specificity
In the adult liver, expression is restricted to a small population of hepatocytes which form only a small rim of one to three hepatocytes around the central veins. Expressed in lung microvascular endothelial cells.
Database Links
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