Mouse Glutamine Synthetase Monoclonal Antibody | anti-GLUL antibody

Glutamine Synthetase

Cat. Num. AAA370304

• Gene Names: GLUL; GS; GLNS; PIG43; PIG59
• Reactivity: Human, Mouse, Rat
• Applications: Immunohistochemistry
• Synonyms: Glutamine Synthetase; Monoclonal Antibody; anti-GLUL antibody

• Host: Mouse
• Reactivity: Human, Mouse, Rat
• Clonality: Monoclonal
• Isotype: IgG2a
• Clone Number: GS-6
• Form/Format: Glutamine Synthase is a rabbit monoclonal antibody derived from cell culture supernatant that is concentrated, dialyzed, filter sterilized and diluted in buffer pH 7.5, containing BSA and sodium azide as a preservative.
• Sequence Length: 373

• Applicable Applications for anti-GLUL antibody: Immunohistochemistry (IHC) Formalin/Paraffin
• Localization: Cytoplasmic
• Control: Liver, Tonsil, Testis, Prostate, Hepatocellular Carcinoma, Bladder TCC
• Intended Use: This antibody is intended for use in Immunohistochemical applications on formalin-fixed paraffin-embedded tissues (FFPE), frozen tissue sections and cell preparations. Interpretation of results should be performed by a qualified medical professional.
• Immunogen: Human Glutamine Synthetase aa. 1-373.
• Preparation and Storage: Store at 2 to 8 degree C in the dark.

Dilution Information

Immunohistochemistry (IHC)

(IHC of Glutamine Synthetase on an FFPE Hepatocellular Carcinoma Tissue)

Related Product Information for anti-GLUL antibody

Glutamine synthetase (GS) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. GS is present predominantly in the brain, kidneys, and liver. GS in the brain participates in the metabolic regulation of glutamate, the detoxification of brain ammonia, the assimilation of ammonia, recyclization of neurotransmitters, and termination of neurotransmitter signals. In normal liver, GS expression is seen in pericentral hepatocytes, but not in mid-zonal or periportal hepatocytes.

GS positive tumor cells are believed to be derived from GS positive hepatocytes. GS immunoreactivity has been seen in a majority of hepatocellular carcinoma (HCC), including cases of early HCC (70%) and for low grade HCC (59%).In nonmalignant nodules, GS overexpression is only seen in high grade dysplastic nodules (HGDN, 13.6%). In these cases, GS overexpression was restricted to 11.5%-50% of hepatocytes, whereas in HCC the majority of cases (53%), including early HCC (60%), showed diffuse immunostaining (>50% tumor cells). A panel composed of antibodies against HSP70, GPC3, and GS has been proposed to be very useful in distinguishing between dysplastic and early malignant hepatocellular nodules arising in cirrhosis. Staining of hepatocellular lesions with anti-GS antibody have been useful in the differential identification of focal nodular hyperplasia (FNH), hepatic adenoma (HCA), and dysplastic nodules, and low grade hepatocellular carcinoma. In the case of FNH, GS stains in a characteristic "map-like" pattern, thus differentiating it from HCA, in which GS staining is usually absent, but may occasionally be present at the border of the lesion or around the veins inside the tumor.

NCBI and Uniprot Product Information

• NCBI GI #: 74271826
• NCBI GeneID: 2752
• NCBI Accession #: NP_001028228.1
• NCBI GenBank Nucleotide #: NM_001033056.3
• Molecular Weight: 42,064 Da
• NCBI Official Full Name: glutamine synthetase
• NCBI Official Synonym Full Names: glutamate-ammonia ligase
• NCBI Official Symbol: GLUL
• NCBI Official Synonym Symbols: GS; GLNS; PIG43; PIG59
• NCBI Protein Information: glutamine synthetase
• UniProt Protein Name: Glutamine synthetase
• Protein Family: Glutamine synthetase
• UniProt Gene Name: GLUL
• UniProt Synonym Gene Names: GLNS; GS
• UniProt Entry Name: GLNA_HUMAN

NCBI Description

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 Description

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 - arginine and proline; Ligase; EC 4.1.1.15; Amino Acid Metabolism - alanine, aspartate and glutamate; EC 6.3.1.2

Chromosomal Location of Human Ortholog: 1q31

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

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

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

Disease: Glutamine Deficiency, Congenital