Recombinant Human Glutaminase Kidney Isoform, Mitochondrial (GLS) Protein (GST)

Name: Recombinant Human Glutaminase Kidney Isoform, Mitochondrial (GLS) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09473P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Glutaminase Kidney Isoform, Mitochondrial (GLS) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O94925
Target Symbol	GLS
Synonyms	AAD20; DKFZp686O15119; FLJ10358; GAC; GAM; GLS; GLS1; GLSK_HUMAN; Glutaminase C; Glutaminase kidney isoform; Glutaminase phosphate activated; K-glutaminase; KGA; KIAA0838; L glutamine amidohydrolase; L-glutamine amidohydrolase; mitochondrial
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	YVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQTVHKNLDGLL
Expression Range	370-669aa
Protein Length	Partial
Mol. Weight	60.4kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate, the main excitatory neurotransmitter in the brain.; Lacks catalytic activity.
Subcellular Location	[Isoform 1]: Mitochondrion. Cytoplasm, cytosol.; [Isoform 3]: Mitochondrion.; [Glutaminase kidney isoform, mitochondrial 68 kDa chain]: Mitochondrion matrix.; [Glutaminase kidney isoform, mitochondrial 65 kDa chain]: Mitochondrion matrix.
Protein Families	Glutaminase family
Database References	HGNC: 4331 OMIM: 138280 KEGG: hsa:2744 STRING: 9606.ENSP00000317379 UniGene: PMID: 30458442 These results reveal that GAC is post-translationally regulated by phosphorylation, which affects cellular glutamine metabolism and glutaminase-related cell phenotype. PMID: 30092248 In silico analysis potentially links GLS SNPs with Alzheimer disease and type 2 diabetes. PMID: 29441491 Del11q-positive CLL lymphocytes exhibit altered glutamine metabolism and differential response to GLS1 and glucose metabolism inhibition. PMID: 29367649 Overexpression of miR-513c suppresses neuroblastoma cells' migration, invasion, and proliferation. We demonstrate the glutaminase (GLS) is a direct target of miR-513c in human neuroblastoma cells. PMID: 28800318 the present findings enriched our knowledge by demonstrating a significant association of PKM2 and GLS1 with oxaliplatin-resistance in CRC. PMID: 28498807 miR-137 was decreased in melanoma tissue, and the low miR-137 levels and high glutaminase expression are independent risk factors in melanoma. miR-137 suppressed the proliferation and glutamine catabolism of melanoma cells. PMID: 29097210 ZIC5 positively regulated the proliferation, migration (Fig. 2), and survival (Fig. 5) of PCa and CRC cells PMID: 29032577 the crystal structure of full-length KGA and present a small-angle X-ray scattering model for full-length GLS2. These structures explain these proteins' compromised ability to assemble into catalytically active supra-tetrameric filaments, as previously shown for GAC. PMID: 28526749 GLS1 inhibition using BPTES reduced metabolic intermediates including thymidine and carbamoyl phosphate. Reduction of thymidine and carbamoyl-phosphate synthesis by BPTES treatment exacerbated pyrimidine supply by combination with 5-FU, which induced cell death synergistically in NSCLC PMID: 27338638 studies show that the formation of large GAC oligomers is not a pre-requisite for full enzymatic activity. They also offer a mechanism by which the binding of activators like inorganic phosphate enables the activation loop to communicate with the active site to ensure maximal rates of catalysis, and promotes the opening of the lid to achieve optimal product release. PMID: 27542409 Glutaminase expression in tumor cells was significantly associated with a low level of tumor-infiltrating lymphocytesand poor disease-free survival in triple-negative breast cancers presenting with lymph node metastasis and high levels of tumor-infiltrating lymphocytes. PMID: 28185053 Study reports that GLS1 is a direct target of miR-23a in retinal pigment epithelium cells (RPE) providing evidence for a role in maintaining RPE cell function. PMID: 27411920 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. PMID: 28218035 High GLS1 expression is associated with epithelial-mesenchymal transition in cancer. PMID: 26771232 Data suggest that glutaminase C (GAC) inhibition maybe a potential treatment strategy for acquired erlotinib-resistant non-small cell lung cancer (NSCLC). PMID: 26575584 Findings indicate a role for transcription factor c-Jun as a driver of cancer cell metabolic reprogramming, and suggest that cancers overexpressing JUN may be especially sensitive to glutaminase (GLS)-targeted therapies. PMID: 27089238 GLS1 was identified as a potential downstream target of the miR-192/-204-HOTTIP axis in hepatocellular carcinoma. PMID: 26710269 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. PMID: 25880019 GABAergic neurons and astrocytes express Gls and Gls2 isoenzymes in nucleus and mitochondria, in addition to glutamatergic neurons PMID: 25297978 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. PMID: 25915584 GLS1 has a key role in coupling glutaminolysis of the TCA cycle with elevated glucose uptake and consequently the growth of prostate cancer cells PMID: 25482439 These results suggest that the expression of GLS1 is upregulated and correlates with clinicopathological factors in colorectal cancer. PMID: 24696726 Silencing GLS or overexpressing GLS2 induces growth inhibition in glioma cell lines. PMID: 24276018 our data indicate that ErbB2 activation promotes GLS1 expression via a PI3K-Akt-independent NF-kappaB pathway in breast cancer cells, identifying another oncogenic signaling pathway which stimulates GLS1 expression PMID: 24122876 The rate of Glu decarboxylation into GABA by Glnase is an order of magnitude lower than that of Glutamate decarboxylase. Potential impact on the mechanistic aspects of Gln-Glu shuttle in neuroscience and glutaminolysis in tumors, is discussed. PMID: 24755074 STAT1 regulates human glutaminase 1 promoter activity PMID: 24086752 Inhibition of glutaminase selectively suppresses the growth of primary acute myeloid leukemia cells with IDH mutations. PMID: 24333121 A glutaminase inhibitor reduced conversion of (13)C-pyruvate to alanine. PMID: 23722553 HER2- type breast cancer had the highest expression of stromal GLS1, tumoral GDH, stromal GDH, and tumoral ASCT, while TNBC had the lowest tumoral GDH expression. PMID: 23507704 activated glutaminase C (GAC) self-assembles into a helical, fiber-like double-stranded oligomer and propose a molecular model consisting of seven tetramer copies per turn per strand interacting via the N-terminal domains PMID: 23935106 stromal expression of the glutamine-metabolism-related proteins GLS1, GDH, ASCT2 increases with worsening histological phyllodes tumor grade. PMID: 23636801 neuronal glutaminase is a potential component of neurotoxicity during inflammation and modulation of glutaminase may provide therapeutic avenues for neurodegenerative diseases. PMID: 23578284 NSCLC cell lines depend on Gln for glutaminolysis to a varying degree, in which the GLS1 splice variant GAC plays an essential role and is a potential target for cancer metabolism-directed therapy. PMID: 22892846 Data indicate that both HIV-1 infection and IFN-alpha treatment increase glutaminase 1 (GLS1) expression through STAT1 phosphorylation and by binding to the GLS1 promoter. PMID: 22479354 KGA activity in cells is stimulated by EGF, and KGA associates with all three kinase components of the Raf-1/Mek2/Erk signaling module. PMID: 22538822 Inhibition of Gls1 kills lung cancer cells that overexpress MYC and catabolize glutamine. PMID: 22326218 GLS1 differs from PFKFB3 in that its recognition by APC/C-Cdh1 during S phase requires the presence of both a Lys-Glu-Asn box (KEN box) and a destruction box (D box) rather than a KEN box alone. PMID: 22106309 first report of full-length crystal structure of a splice variant of GLS1 in presence/absence of BPTES, an allosteric inhibitor: 2 BPTES molecules bind at interface of GLS1 tetramer; appear to lock GLS1 tetramer into nonproductive conformation PMID: 22049910 Glutamine synthetase is a genetic determinant of cell type-specific glutamine independence in breast epithelia PMID: 21852960 This studt demonistrated that the genetic variation in the glutaminase gene GLS1 is related the glutamine/glutamate ratio in brain. PMID: 21457947 Glutaminase: a hot spot for regulation of cancer cell metabolism. PMID: 21234284 Data show that the ability to selectively slow growth in cells with IDH1 mutations by inhibiting glutaminase suggesting a unique reprogramming of intermediary metabolism and a potential therapeutic strategy. PMID: 21045145 This study identifies mutations in the gene sequence for glutaminase that are associated with development of hepatic encephalopathy in patients with cirrhosis PMID: 20820037 Data suggest that glutaminase is an important factor in melanoma cell proliferation. PMID: 12579526 human neutrophils appeared to utilize glutamine and posess the appropriate glutaminase enzyme for metabolizing glutamine. PMID: 14722097 possible role for intestinal glutaminase in the pathogenesis of hepatic encephalopathy PMID: 15246207 K glutaminase isoform is up-regulated with increased rates of proliferation in cancer cells, whereas prevalence of the L isoform seems to be related with resting or quiescent cell states PMID: 15496140 c-Myc transcriptionally represses miR-23a and miR-23b, resulting in greater expression of their target protein, mitochondrial glutaminase, in human P-493 B lymphoma cells and PC3 prostate cancer cells PMID: 19219026 Release of glutaminase from dysfunctional macrophages is a possible mechanism of glutaminase-mediated production of excitotoxic glutamate during the pathogenic process of human immunodeficiency virus (HIV)-1 associated dementia. PMID: 19222703

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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