Recombinant Human Fructose-2,6-Bisphosphatase Tigar Protein (TIGAR) Protein (TAT), Active

Name: Recombinant Human Fructose-2,6-Bisphosphatase Tigar Protein (TIGAR) Protein (TAT), Active
Brand: Beta LifeScience
SKU: BLC-05560P
Availability: InStock

Collections: Featured enzyme molecules, High-quality recombinant proteins

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Product Overview

Description	Recombinant Human Fructose-2,6-Bisphosphatase Tigar Protein (TIGAR) Protein (TAT), Active is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 96% as determined by SDS-PAGE and HPLC.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	Fully biologically active when compared to standard. The biological activity determined by its ability to protect U2OS cells from apoptosis induced by hydrogen peroxide is in a concentration range of 0.1-5.0 μg/ml, after pretreating with rHuTIGAR-TAT for 4 hours.
Uniprotkb	Q9NQ88
Target Symbol	TIGAR
Synonyms	6-bisphosphatase TIGAR; C12ORF5; chromosome 12 open reading frame 5; FR2BP; Fructose-2,6-bisphosphatase TIGAR; Fructose-2,6-bisphosphate 2-phosphatase; Probable fructose 2,6 bisphosphatase TIGAR; Probable fructose-2; tigar; TIGAR_HUMAN; TP53 induced glycolysis and apoptosis regulator; TP53 induced glycolysis regulatory phosphatase; TP53-induced glycolysis and apoptosis regulator; Transactivated by NS3TP2 protein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-TAT
Complete Sequence	MARFALTVVRHGETRFNKEKIIQGQGVDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHGILERSKFCKDMTVKYDSRLRERKYGVVEGKALSELRAMAKAAREECPVFTPPGGETLDQVKMRGIDFFEFLCQLILKEADQKEQFSQGSPSNCLETSLAEIFPLGKNHSSKVNSDSGIPGLAASVLVVSHGAYMRSLFDYFLTDLKCSLPATLSRSELMSVTPNTGMSLFIINFEEGREVKPTVQCICMNLQDHLNGLTETR+GGYGRKKRRQ
Expression Range	1-270aa
Protein Length	Full Length
Mol. Weight	31.7 kDa
Research Area	Cell Biology
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 m filtered 30 Acetonitrile, 0.1% TFA
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	Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate. Acts as a negative regulator of glycolysis by lowering intracellular levels of fructose-2,6-bisphosphate in a p53/TP53-dependent manner, resulting in the pentose phosphate pathway (PPP) activation and NADPH production. Contributes to the generation of reduced glutathione to cause a decrease in intracellular reactive oxygen species (ROS) content, correlating with its ability to protect cells from oxidative or metabolic stress-induced cell death. Plays a role in promoting protection against cell death during hypoxia by decreasing mitochondria ROS levels in a HK2-dependent manner through a mechanism that is independent of its fructose-bisphosphatase activity. In response to cardiac damage stress, mediates p53-induced inhibition of myocyte mitophagy through ROS levels reduction and the subsequent inactivation of BNIP3. Reduced mitophagy results in an enhanced apoptotic myocyte cell death, and exacerbates cardiac damage. Plays a role in adult intestinal regeneration; contributes to the growth, proliferation and survival of intestinal crypts following tissue ablation. Plays a neuroprotective role against ischemic brain damage by enhancing PPP flux and preserving mitochondria functions. Protects glioma cells from hypoxia- and ROS-induced cell death by inhibiting glycolysis and activating mitochondrial energy metabolism and oxygen consumption in a TKTL1-dependent and p53/TP53-independent manner. Plays a role in cancer cell survival by promoting DNA repair through activating PPP flux in a CDK5-ATM-dependent signaling pathway during hypoxia and/or genome stress-induced DNA damage responses. Involved in intestinal tumor progression.
Subcellular Location	Cytoplasm. Nucleus. Mitochondrion.
Protein Families	Phosphoglycerate mutase family
Database References	HGNC: 1185 OMIM: 610775 KEGG: hsa:57103 STRING: 9606.ENSP00000179259 UniGene: PMID: 28338004 findings demonstrate that the HTLV-1 latency-maintenance factor p30(II) induces the TP53-induced glycolysis and apoptosis regulator (TIGAR) and counters the oxidative stress, mitochondrial damage, and cytotoxicity caused by the viral oncoproteins Tax and HBZ PMID: 29777913 simultaneous mutations at all four acetylation sites completely abolish its ability to regulate metabolic targets, such as TIGAR and SLC7A11. Moreover, p53(4KR) is still capable of inducing the p53-Mdm2 feedback loop, but p53-dependent ferroptotic responses are markedly abrogated PMID: 27705786 High TIGAR expression was an independent predictor of poor survival and high incidence of relapse in adult patients with CN-AML. TIGAR also showed high expression in multiple human leukemia cell lines and knockdown of TIGAR activated glycolysis through PFKFB3 upregulation in human leukemia cells. PMID: 27884166 the upregulation of hsamiR101 in ccRCC was induced by hypoxia. Its expression deceased the protein expression of TIGAR and promoted glycolysis. This regulatory pathway may represent a novel mechanism of carcinogenesis and requires further investigation. PMID: 28138701 TIGAR expression in breast carcinoma cells promotes metabolic compartmentalization and tumor growth with a mitochondrial metabolic phenotype with lactate and glutamine catabolism. PMID: 27803158 we investigate the crosstalk between PFKFB3 and TIGAR (TP53-Induced Glycolysis and Apoptosis Regulator), a protein known to protect cells from oxidative stress. Our results show consistent TIGAR induction in HeLa cells in response to PFKFB3 knockdown PMID: 27491040 The study showed that miR-101 inhibited viability, induced apoptosis, pushed glucose metabolism flux from the pentose phosphate pathway into glycolysis in prostate cancer PC3 cell line by decreasing NADPH levels by throughly directly binding to 3'-UTR of TIGAR mRNA and repressing TIGAR expression. PMID: 28384067 This study demonstrated that a high p53 expression could be associated with the promotion of glycolysis in gastric cancer via the modulation of TIGAR expression. PMID: 27499152 TIGAR expression may be used as a bio-marker for detection of colorectal cancer and can be used as a target for developing therapeutics for the treatment of colorectal cancer. PMID: 26675982 TIGAR knockdown reduced tumor growth rate. PMID: 26691054 Geranylgeranoic acid induced upregulation of the TIGAR gene, which might inhibit the glycolysis in HuH-7 cells with p53 mutation. PMID: 26700591 TIGAR over-expression could diminish the radiosensitivity of Hs 917.T cells, and the autophagy level induced by ionizing radiation (IR) was also decreased by TIGAR transfection. PMID: 26191173 The Cdk5-AMT signal pathway involved in regulation of DDR by TIGAR. PMID: 25928429 miR-144 targeted TIGAR, inhibited proliferation, enhanced apoptosis, and increased autophagy in A549 and H460 cells PMID: 25660220 Results revealed that TIGAR inhibits both apoptosis and autophagy. PMID: 25085248 TIGAR is correlated with maximal standardized uptake value on FDG-PET and survival in non-small cell lung cancer. PMID: 24363807 Data show targeting MUC1-C is synergistic with bortezomib (BTZ) in suppressing p53-inducible regulator of glycolysis and apoptosis (TIGAR)-mediated regulation of reactive oxygen species levels for combining GO-203 with BTZ in BTZ resistance. PMID: 24632713 The kinetic properties and the structural similarity of the best substrates of TIGAR make it unlikely that TIGAR modulates cellular fructose 2,6-bisphosphate levels directly. PMID: 24423178 CREB regulates TIGAR expression via a CRE-binding site at the TIGAR promoter. PMID: 24036271 oroxylin A could increase protein and mRNA expression of TP53-induced glycolysis and apoptosis regulator (TIGAR) and synthesis of cytochrome c oxidase 2 (SCO2), which are the key metabolic modulators regulated by p53. PMID: 23612020 TIGAR gene expression is down regulated by oxidative stress through the mediation of reactive oxygen species PMID: 23832602 TIGAR regulates akt and erk phosphorylation but hase no effect on NF-kappa B activation in neocazinostatin-treated cells. PMID: 23640457 data provide the first evidence that targeted silencing of TIGAR induces apoptotic and autophagic cell death in HepG2 cells PMID: 23817040 TIGAR has roles in efficient intestinal regeneration and tumorigenesis PMID: 23726973 The ability of TIGAR to function as a Fru-2,6-BPase was independent of hexokinase 2 binding and mitochondrial localization, although activities can contribute to the activity of TIGAR in limiting mitochondrial ROS levels and protecting from cell death. PMID: 23185017 TIGAR regulates the expression of genes involved in cell-cycle progression. PMID: 22782351 Tp53-induced glycolysis and apoptosis regulator (TIGAR) protects glioma cells from starvation-induced cell death by up-regulating respiration and improving cellular redox homeostasis PMID: 22887998 SP1 can interact with the SP1-binding site within TIGAR promoter in vitro and in vivo. Conclusively, SPl is indispensable for basal activity of TIGAR promoter. PMID: 21761199 TIGAR abrogation provides a novel adjunctive therapeutic strategy against glial tumors by increasing radiation-induced cell impairment, thus allowing the use of lower radiotherapeutic doses. PMID: 21864926 These results suggest that p53 can modulate the metabolic pathways via the proteins SCO2 and TIGAR in human breast cancer. PMID: 21820150 Inhibition of TIGAR by c-Met results in reduction of cellular NADPH and cell death. PMID: 21057531 The decrease of intracellular ROS levels in response to TIGAR may also play a role in the ability of p53 to protect from the accumulation of genomic damage. PMID: 16839880 correlation between the recently described p53-inducible apoptosis gene TIGAR and both sensitivity to fludarabine and hENT2 expression in chronic lymphocytic leukemia cells. PMID: 18945750 TIGAR can modulate reactive oxygen species in response to nutrient starvation or metabolic stress, and functions to inhibit autophagy. PMID: 19713938

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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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