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GLS encodes the K-type mitochondrial glutaminase. Additionally we are shipping Glutaminase Kits (19) and Glutaminase Proteins (4) and many more products for this protein.
Showing 10 out of 80 products:
Human Monoclonal Glutaminase Primary Antibody for IF, ELISA - ABIN561056
Unterluggauer, Mazurek, Lener, Hütter, Eigenbrodt, Zwerschke, Jansen-Dürr: Premature senescence of human endothelial cells induced by inhibition of glutaminase. in Biogerontology 2008
Show all 4 references for ABIN561056
Human Polyclonal Glutaminase Primary Antibody for WB - ABIN2786054
Sahai: Glutaminase in human platelets. in Clinica chimica acta; international journal of clinical chemistry 1983
Human Polyclonal Glutaminase Primary Antibody for ELISA, WB - ABIN561055
Shajahan-Haq, Cook, Schwartz-Roberts, Eltayeb, Demas, Warri, Facey, Hilakivi-Clarke, Clarke: MYC regulates the unfolded protein response and glucose and glutamine uptake in endocrine resistant breast cancer. in Molecular cancer 2014
Human Polyclonal Glutaminase Primary Antibody for ICC, IF - ABIN4314688
Tanaka, Sasayama, Irino, Takata, Nagashima, Satoh, Kyotani, Mizowaki, Imahori, Ejima, Masui, Gini, Yang, Hosoda, Sasaki, Mischel, Kohmura: Compensatory glutamine metabolism promotes glioblastoma resistance to mTOR inhibitor treatment. in The Journal of clinical investigation 2015
Human Polyclonal Glutaminase Primary Antibody for FACS, IF - ABIN652757
Swierczyński, Bereznowski, Makarewicz: Phosphate-dependent glutaminase of rat skeletal muscle. Some properties and possible role in glutamine metabolism. in Biochimica et biophysica acta 1993
findings suggest that glutaminase Heterozygote mice have a pro-cognitive profile in the trace fear conditioning paradigm, and this phenotype involves activation of both hippocampus and Anterior Cingulate Cortex.
studies demonstrate that GLS is required for tumorigenesis and support small molecule and genetic inhibition of GLS as potential approaches for targeting the tumor cell-autonomous dependence on GLS for cancer therapy.
The Phosphate-Activated Glutaminase (show GLS2 Antibodies)(PAG (show PRDX1 Antibodies)) is mainly active in mouse kidney, brain and liver, and shows different kinetics depending on which type of PAG (show PRDX1 Antibodies) is expressed.
The network identified in glutaminase deficient fetal mouse brain involves (a) cellular assembly and organization and (b) cell signaling and cell cycle, suggesting that Gls is crucial for neuronal maturation.
kidney-type glutaminase (KGA) as a novel partner of Bmcc1s
The up-regulation of neuronal glutaminase was demonstrated in situ in a murine model of HIV-1 encephalitis.
identified a novel distant regulatory element located approximately 120kb downstream of the gls promoter, and examined its regulatory relevance to gls gene expression in C2C12 cells
Study demonstrated expression of alternative transcripts of the mammalian Gls2 (show GLS2 Antibodies) gene. Transcriptional mechanisms giving rise to GLS2 (show GLS2 Antibodies) variants and isolation of novel GLS2 (show GLS2 Antibodies) transcripts in human, rat and mouse are presented.
In wild-type (WT) mice, GLS1 gene expression was highest in the hippocampus and cortex, where it was reduced by about 50% in Glutaminase-deficient mice.
Phosphate-activated glutaminase (GLS2 (show GLS2 Antibodies)) is a p53 (show TP53 Antibodies)-inducible regulator of glutamine (show GFPT1 Antibodies) metabolism and reactive oxygen species
The memory deficits observed in nemy are because of reduced function of CytB561 (show CYB561 Antibodies) in specific brain regions that are involved in learning and memory.
Study reports that GLS1 is a direct target of miR (show MLXIP Antibodies)-23a in retinal pigment epithelium cells (RPE (show RPE Antibodies)) providing evidence for a role in maintaining RPE (show RPE Antibodies) cell function.
The relative expression of microRNA-153 and glutaminase in glioblastoma versus matched non-tumor tissues showed a reverse correlation, further indicating that microRNA-153 may negatively regulate glutaminase in vivo.
High GLS1 expression is associated with epithelial-mesenchymal transition in cancer.
Data suggest that glutaminase C (GAC) inhibition maybe a potential treatment strategy for acquired erlotinib-resistant non-small cell lung cancer (NSCLC).
Findings indicate a role for transcription factor c-Jun (show JUN Antibodies) as a driver of cancer cell metabolic reprogramming, and suggest that cancers overexpressing JUN (show JUN Antibodies) may be especially sensitive to glutaminase (GLS)-targeted therapies.
GLS1 was identified as a potential downstream target of the miR (show MLXIP Antibodies)-192/-204-HOTTIP axis in hepatocellular carcinoma.
In the present study it was determined whether three key enzymes for glycolysis, glutaminolysis and de novo synthesis of FAs (show FAS Antibodies), hexokinase-2 (show HK2 Antibodies), glutaminase and fatty acid synthase (show FASN Antibodies)
Our findings support the role of the GLS long microsatellite in the development of HE; this could be important for identifying susceptible patients and for the prevention of this condition.
GABAergic neurons and astrocytes express Gls and Gls2 (show GLS2 Antibodies) isoenzymes in nucleus and mitochondria, in addition to glutamatergic neurons
This gene encodes the K-type mitochondrial glutaminase. The encoded protein is an phosphate-activated amidohydrolase that catalyzes the hydrolysis of glutamine to glutamate and ammonia. This protein is primarily expressed in the brain and kidney plays an essential role in generating energy for metabolism, synthesizing the brain neurotransmitter glutamate and maintaining acid-base balance in the kidney. Alternate splicing results in multiple transcript variants.
glutaminase kidney isoform, mitochondrial
, phosphate-activated glutaminase
, glutaminase C
, hypothetical protein
, L-glutamine amidohydrolase
, glutaminase, phosphate-activated
, glutaminase liver isoform, mitochondrial
, liver mitochondrial glutaminase