Immunohistochemistry (IHC) : Formalin-fixed, paraffin-embedded human liver stained with anti-glutamine synthetase antibody using peroxidase-conjugate and DAB chromogen. Note the cytoplasmic staining of hepatocytes around a central vein.

rabbit anti-Glutamine synthetase monoclonal antibody (ZR431) 6426

$160.00 – $528.00

Antibody summary

Rabbit monoclonal to Glutamine synthetase
Suitable for: Immunohistochemistry (formalin-fixed, paraffin-embedded tissues)
Reacts with: Human
Isotype:IgG
Control: Normal liver
Visualization: Cytoplasmic
0.1, 0.5, 1.0 mL concentrated, 7 mL prediluted

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SKU: 6426parent Category: antibody Tags: anatomy, GI Pathology, Glutamine synthetase

Weight	1 lbs
Dimensions	9 × 5 × 2 in
host	mouse
isotype	IgG
clonality	monoclonal
concentration	concentrate, predilute
applications	IHC
reactivity	human
available size	0.1 mL, 0.5 mL, 1 mL concentrated, 7 mL prediluted

rabbit anti-Glutamine synthetase monoclonal antibody ZR431 6426

antibody
Database link: human P15104
Tested applications IHC
Recommended dilutions Concentrated 1:100-200
Application Notes Normal liver
Immunogen Recombinant fragment (around aa 50-250) of human GLUL protein
Size and concentration 7 mL prediluted or 0.1, 0.5, 1.0 mL and concentrated
Form liquid
Storage Instructions 2-8°C for short term, for longer term at -20°C. Avoid freeze / thaw cycles.
Purity affinity purified
Clonality monoclonal
Isotype IgG
Compatible secondaries goat anti-rabbit IgG, H&L chain specific, peroxidase conjugated, conjugated polyclonal antibody 9512 goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody 2079 goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody 7863 goat anti-rabbit IgG, H&L chain specific, Cross Absorbed polyclonal antibody 2371 goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1715 goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1720
Isotype control Rabbit polyclonal - Isotype Control

target relevance
Protein names Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Palmitoyltransferase GLUL) (EC 2.3.1.225)
Gene names GLUL,GLUL GLNS
Protein family Glutamine synthetase family
Mass 42064Da
Function FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (PubMed:16267323, PubMed:30158707, PubMed:36289327). 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 (By similarity). Plays a key role in ammonium detoxification during erythropoiesis: the glutamine synthetase activity is required to remove ammonium generated by porphobilinogen deaminase (HMBS) during heme biosynthesis to prevent ammonium accumulation and oxidative stress (By similarity). Essential for proliferation of fetal skin fibroblasts (PubMed:18662667). 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 (PubMed:30158707). May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (PubMed:30158707). Plays a role in ribosomal 40S subunit biogenesis (PubMed:26711351). Through the interaction with BEST2, inhibits BEST2 channel activity by affecting the gating at the aperture in the absence of intracellular L-glutamate, but sensitizes BEST2 to intracellular L-glutamate, which promotes the opening of BEST2 and thus relieves its inhibitory effect on BEST2 (PubMed:36289327). {ECO:0000250\|UniProtKB:P15105, ECO:0000269\|PubMed:16267323, ECO:0000269\|PubMed:18662667, ECO:0000269\|PubMed:26711351, ECO:0000269\|PubMed:30158707, ECO:0000269\|PubMed:36289327}.
Catalytic activity CATALYTIC ACTIVITY: Reaction=L-glutamate + NH4(+) + ATP = L-glutamine + ADP + phosphate + H(+); Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000269\|PubMed:16267323, ECO:0000269\|PubMed:30158707, ECO:0000269\|PubMed:36289327}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + hexadecanoyl-CoA = S-hexadecanoyl-L-cysteinyl-[protein] + CoA; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000305\|PubMed:30158707};
Subellular location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269\|PubMed:30158707, ECO:0000269\|PubMed:36289327}. Microsome {ECO:0000250\|UniProtKB:P09606}. Mitochondrion {ECO:0000250\|UniProtKB:P09606}. Cell membrane {ECO:0000269\|PubMed:30158707}; Lipid-anchor {ECO:0000269\|PubMed:30158707}. Note=Mainly localizes in the cytosol, with a fraction associated with the cell membrane. {ECO:0000269\|PubMed:30158707}.
Tissues TISSUE SPECIFICITY: Expressed in endothelial cells. {ECO:0000269\|PubMed:30158707}.
Structure SUBUNIT: Decamer; composed of two pentamers (PubMed:18005987). Interacts with PALMD (By similarity). Interacts with RHOJ (PubMed:30158707). Interacts with BEST2; this interaction tethers a fraction of GLUL to the membrane, causing a decrease of cytosolic glutamine synthase (GS) activity and inhibits the chloride channel activity of BEST2 by affecting the gating at the aperture in the absence of intracellular glutamate (PubMed:36289327). {ECO:0000250\|UniProtKB:P15105, ECO:0000269\|PubMed:18005987, ECO:0000269\|PubMed:30158707, ECO:0000269\|PubMed:36289327}.
Post-translational modification PTM: Acetylated by EP300/p300; acetylation is stimulated by increased glutamine levels and promotes ubiquitin-mediated proteasomal degradation. {ECO:0000269\|PubMed:26990986}.; PTM: Palmitoylated; undergoes autopalmitoylation. {ECO:0000305\|PubMed:30158707}.; PTM: Ubiquitinated by ZNRF1 (By similarity). Ubiquitinated by the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex called CRL4(CRBN), leading to proteasomal degradation (PubMed:26990986). {ECO:0000250\|UniProtKB:P15105, ECO:0000269\|PubMed:26990986}.
Involvement in disease DISEASE: Glutamine deficiency, congenital (GLND) [MIM:610015]: An autosomal recessive disorder characterized by variable brain malformations, encephalopathy, severe developmental delay, seizures, and decreased glutamine levels in bodily fluids. Death in early infancy may occur. {ECO:0000269\|PubMed:16267323, ECO:0000269\|PubMed:26711351, ECO:0000269\|PubMed:38579670}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Developmental and epileptic encephalopathy 116 (DEE116) [MIM:620806]: A form of epileptic encephalopathy, a heterogeneous group of early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE116 is autosomal dominant form characterized by severe developmental delay, seizures, and white matter abnormalities. {ECO:0000269\|PubMed:38579670}. Note=The disease is caused by variants affecting the gene represented in this entry. DEE116 is caused by variants that disrupt the canonical translation start codon in GLUL resulting in initiation of translation at Met-18 (PubMed:38579670). The resulting protein is enzymatically competent but insensitive to negative feedback regulation via glutamine-induced degradation. {ECO:0000269\|PubMed:38579670}.
Target Relevance information above includes information from UniProt accession: P15104
The UniProt Consortium

Data

Formalin-fixed, paraffin-embedded human liver stained with anti-glutamine synthetase antibody using peroxidase-conjugate and DAB chromogen. Note the cytoplasmic staining of hepatocytes around a central vein.

Publications

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Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.