Recombinant Human Glutaminase Liver Isoform, Mitochondrial (GLS2) Protein (His-SUMO)

Name: Recombinant Human Glutaminase Liver Isoform, Mitochondrial (GLS2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09472P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) GLS2.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Glutaminase Liver Isoform, Mitochondrial (GLS2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9UI32
Target Symbol	GLS2
Synonyms	breast cell glutaminase; GA; GLS; Gls2; GLSL_HUMAN; glutaminase 2 (liver mitochondrial); glutaminase 2; glutaminase GA; glutaminase I; Glutaminase liver isoform; Glutaminase liver isoform; mitochondrial; hLGA; L glutaminase; L glutamine amidohydrolase; L-glutaminase; L-glutamine amidohydrolase; LGA; mitochondrial; phosphate activated glutaminase; phosphate-dependent glutaminase
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	GSHCGRGGWGHPSRSPLLGGGVRHHLSEAAAQGRETPHSHQPQHQDHDSSESGMLSRLGDLLFYTIAEGQERIPIHKFTTALKATGLQTSDPRLRDCMSEMHRVVQESSSGGLLDRDLFRKCVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDVKELTGGKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFVGKEPSGLRYNKLSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFHNYDNLRHCARKLDPRREGAEIRNKTVVNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFAKDRWGNIPLDDAVQFNHLEVVKLLQDYQDSYTLSETQAEAAAEALSKENLESMV
Expression Range	15-602aa
Protein Length	Full Length of Mature Protein
Mol. Weight	80.7kDa
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	Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation.
Subcellular Location	Mitochondrion.
Protein Families	Glutaminase family
Database References	HGNC: 29570 OMIM: 606365 KEGG: hsa:27165 STRING: 9606.ENSP00000310447 UniGene: Hs.212606
Tissue Specificity	Highly expressed in liver. Expressed in brain and pancreas. Not observed in heart, placenta, lung, skeletal muscle and kidney. Expression is significantly reduced in hepatocellular carcinomas.

Gene Functions References

This study assessed the relation of GLS2 downregulation in glioblastoma cells to its methylation and TP53 status. Aberrant methylation of CpG islands, appear to contribute to silencing of GLS2 in glioblastoma cells by a mechanism bypassing TP53 mutations. PMID: 26258493
observe that while miR-23 is capable of down-regulating the shortened KGA 3'UTR, it has only minor impact on the full-length KGA 3'UTR, demonstrating that additional potent negative regulation of GLS expression exists beyond this single microRNA targeting site PMID: 27095025
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
Cox multivariate regression analysis demonstrated that DUOX1, GLS2, FBP1 and age were independent risk factors for the prognosis of HCC patients after surgery PMID: 27079415
As a p53 target, GLS2 mediates p53's function in metastasis suppression through inhibiting Rac1. PMID: 26751560
IDO, through GCN2 kinase activation, downregulates the levels of TCRcomplex tchain and cMyc, resulting in the suppression of Tcell proliferation and a reduction in the levels of LDHA and GLS2 PMID: 26647830
GABAergic neurons and astrocytes express Gls and Gls2 isoenzymes in nucleus and mitochondria, in addition to glutamatergic neurons PMID: 25297978
Phosphate-activated glutaminase and GAD65/67 concentrations are compared in Alzheimer's disease cerebellum versus normal cerebellum controls PMID: 24950944
GLS2 expression is significantly decreased in hepatocellular carcinoma. PMID: 24797434
Silencing GLS or overexpressing GLS2 induces growth inhibition in glioma cell lines. PMID: 24276018
GLS2 is acting, at least in part, downstream of p73 in neuronal differentiation and highlight a possible role of p73 in regulating neurotransmitter synthesis. PMID: 24121663
combination of negative modulation of glutaminase isoforms arising from GLS gene with the introduction of the GLS2 gene product, GAB, may in the future provide a useful means to curb glioblastoma growth in situ PMID: 24096582
Epigenetic silencing of Gls2 via promoter hypermethylation is common in human liver and colon cancers. PMID: 24330717
The present study was to investigate the potent effect of GLS2 on radioresistance of cervical carcinoma. PMID: 23954443
GLS2 is a bona fide TAp63 target gene. PMID: 23574722
LGA circumvents, by an as yet unknown route, the most common mechanism of O6-methylguanine-DNA methyltransferase (MGMT) gene silencing. PMID: 22888977
Study demonstrated expression of alternative transcripts of the mammalian Gls2 gene. Transcriptional mechanisms giving rise to GLS2 variants and isolation of novel GLS2 transcripts in human, rat and mouse are presented. PMID: 22679499
GLS2 is resistant to BPTES; GLS1 mutants created reflecting differences between GLS2 and GLS1 sequence in region of BPTES binding; mutant proteins lost inhibition by BPTES; amino acid sequence alignment GLS2 versus GLS1 PMID: 22049910
as a unique p53 target gene, GLS2 is a mediator of p53's role in energy metabolism and antioxidant defense, which can contribute to its role in tumor suppression PMID: 20378837
Phosphate-activated glutaminase (GLS2) is a p53-inducible regulator of glutamine metabolism and reactive oxygen species PMID: 20351271
results show L-type glutaminase is expressed in the brain with a nuclear localization and that this nuclear enzyme is catalytically active and displays kinetic properties different from both liver and kidney glutaminases PMID: 12163477
Data describe the characterization of the human liver-type glutaminase (hLGA) gene. PMID: 12444921
High levels of glutamate were produced by monocyte-derived macrophages infected with HIV-1 strains and inhibited by a glutaminase inhibitor and AZT thus implicating a glutamate-generating enzyme such as phosphate-activated mitochondrial glutaminase PMID: 14675161
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
These data implicate mitochondrial glutaminase in the induction of glutamate-mediated neuronal apoptosis during HIV-associated dementia, and provides a possible therapeutic strategy for HAD treatment. PMID: 18088378
presence of LGA mRNA in transfected glioma cells coincided with depression of basic physiological parameters: Cell migration, proliferation, and survival as assessed with colony formation assay and the mitochondrial activity test PMID: 19062176

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.