Recombinant Human Hepatitis B Virus X-Interacting Protein (LAMTOR5) Protein (GST)

Name: Recombinant Human Hepatitis B Virus X-Interacting Protein (LAMTOR5) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09108P
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 Hepatitis B Virus X-Interacting Protein (LAMTOR5) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O43504
Target Symbol	LAMTOR5
Synonyms	HBV X interacting protein ; HBV X-interacting protein; HBX interacting protein; HBX-interacting protein; hbxip; HBXIP_HUMAN; Hepatitis B virus X interacting protein; Hepatitis B virus X-interacting protein; LAMTOR5; Late endosomal/lysosomal adaptor MAPK and MTOR activator 5; MGC71071; Ragulator complex protein LAMTOR5; XIP
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MEATLEQHLEDTMKNPSIVGVLCTDSQGLNLGCRGTLSDEHAGVISVLAQQAAKLTSDPTDIPVVCLESDNGNIMIQKHDGITVAVHKMAS
Expression Range	1-91aa
Protein Length	Full Length
Mol. Weight	36.6kDa
Research Area	Cell Biology
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	As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. When complexed to BIRC5, interferes with apoptosome assembly, preventing recruitment of pro-caspase-9 to oligomerized APAF1, thereby selectively suppressing apoptosis initiated via the mitochondrial/cytochrome c pathway. Down-regulates hepatitis B virus (HBV) replication.
Subcellular Location	Lysosome. Cytoplasm, cytosol.
Protein Families	LAMTOR5 family
Database References	HGNC: 17955 OMIM: 608521 KEGG: hsa:10542 STRING: 9606.ENSP00000256644 UniGene: PMID: 29174803 Those findings highlight the potential role of SIRT2 in HBV and HBV-mediated HCC by interaction with HBx. PMID: 29366781 HBXIP can modulate the etoposide sensitivity of MCF-7 cell lines. PMID: 29309885 deacetylation of MST1 mediated by HBXIP-enhanced HDAC6 results in MST1 degradation in a CMA manner in promotion of breast cancer growth. PMID: 26657153 high level of expression of HBXIP is associated with the progression of non-small-cell lung cancer and may be a useful biomarker for poor prognostic evaluation and a potential molecular therapy target for patients with non-small-cell lung cancer PMID: 28718367 HBXIP is able to depress the gluconeogenesis in hepatoma cells by suppressing PCK1 to promote hepatocarcinogenesis, involving miR-135a/FOXO1 axis and PI3K/Akt/p-FOXO1 pathway. PMID: 27609066 we conclude that the oncoprotein HBXIP contributes to the abnormal lipid metabolism in breast cancer PMID: 26980761 HBXIP can function as a mediator protein for DNA damage response signals to activate the G2/M checkpoint to maintain genome integrity and prevent cell death. PMID: 28103177 promotes cisplatin resistance and regulates CD147 via Sp1 in ovarian cancer PMID: 28056551 The mRNA levels of ACSL1 were positively associated with those of HBXIP in clinical breast cancer tissues. Thus, we conclude that the oncoprotein HBXIP is able to up-regulate ACSL1 through activating the transcriptional factor Sp1 in breast cancer. PMID: 28132807 Data indicate that hepatitis B virus X-interacting protein (HBXIP) over-expression appears to associate with cervical cancer progression, and may potentially be used as a cervical cancer biomarker for the early diagnosis, prognostic evaluation and therapeutic target for cervical cancer. PMID: 28093193 Multivariate analysis indicated that HBXIP, in addition to the clinical stage, was a significant independent prognostic factor in patients with ovarian cancer. PMID: 28388957 Expression of HBXIP was significantly increased in UCB tissues. Data showed that suppression of HBXIP induced cell cycle arrest and increased cell apoptosis in T24 cells. Also, suppression of HBXIP also decreased T24 and PC3 cell proliferation, migration, and invasion. More importantly, It was found that inhibition of HBXIP reduced the tumorigenesis in vivo, suggesting that HBXIP plays an important role in progression. PMID: 27831760 Upon HBV infection, cellular mechanisms involving SETDB1-mediated H3K9me3 and HP1 induce silencing of HBV cccDNA transcription through modulation of chromatin structure. PMID: 26143443 Thus, we conclude that the oncoprotein HBXIP up-regulates FGF4 through activating transcriptional factor Sp1 to promote the migration of breast cancer cells. Therapeutically, HBXIP may serve as a novel target in breast cancer. PMID: 26828265 Results support a model in which the HBXIP/Hotair/LSD1 complex serves as a critical effector of c-Myc in activating transcription of its target genes, illuminating long-standing questions on how c-Myc drives carcinogenesis. PMID: 26719542 highly expressed HBXIP accelerates the MDM2-mediated degradation of p53 in breast cancer through modulating the feedback loop of MDM2/p53, resulting in the fast growth of breast cancer cells. PMID: 26229107 Our study suggested that high HBXIP is associated with the progression of breast cancer. HBXIP could be a valuable prognostic marker as well as a potential molecular therapy target for breast cancer patients. PMID: 25178941 HBXIP promotes the migration of breast cancer cells through modulating microtubule acetylation mediated by GCN5. PMID: 25686500 Dta show that HBXIP was able to stimulate the activity of Skp2 promoter via transcription factor Sp1 thus promoting the migration of ovarian cancer cells. PMID: 24788380 Hepatitis B protein HBx accelerates hepatocarcinogenesis with partner survivin through modulating tumor suppressor miR-520b and oncoprotein HBXIP. PMID: 24886421 HBXIP facilitates the proliferation of hepatoma cells by up-regulating SCG3 via E2F1 and miR-509-3p modulation. PMID: 24882622 The oncoprotein HBXIP enhances angiogenesis and growth of breast cancer through modulating FGF8 and VEGF. PMID: 24464787 HBXIP nuclear import requires interaction with c-Fos and phosphorylation of both proteins in breast cancer cells PMID: 23667255 conclude that the oncoprotein HBXIP as a co-activator of TF II D transactivates Lin28B promoter via directly binding to TBP to upregulate the expression of Lin28B in promotion of proliferation of breast cancer cells PMID: 23494474 knockdown of HBXIP rescued the inhibition of HBV that occurred after the loss of miR-501 in HepG2.2.15 cells, suggesting that miR-501 induced HBV replication partially by targeting HBXIP. PMID: 23266610 HBXIP promotes the proliferation of breast cancer cells via upregulating PDGFB. PMID: 23537647 oncoprotein HBXIP is able to activate the transcriptional coregulatory protein LMO4 through transcription factor Sp1 in promotion of proliferation of breast cancer cells. PMID: 23291272 found that HBXIP was able to stimulate the promoter of Skp2 through binding to the -640/-443 region in Skp2 promoter involving activating E2F transcription factor 1 PMID: 23352642 Study identified HBXIP and C7orf59 as two additional Ragulator components that are required for mTORC1 activation by amino acids. PMID: 22980980 HBXIP up-regulates S100A4 through activating S100A4 promoter involving STAT4 and inducing PTEN/PI3K/AKT signaling to promote growth and migration of breast cancer cells. PMID: 22740693 overexpression of HBXIP increased HepG2 cell-induced endothelial cells migration, proliferation, and angiogenesis, which may be related to increasing phosphorylation of endothelial NO synthase in HUVECs. PMID: 22209835 Data suggest that HBXIP upregulates CD46, CD55 and CD59 through p-ERK1/2/NF-kappaB signaling to protect breast cancer from complement-dependent cytotoxicity. PMID: 22293503 The different structure forms of HBx protein influence their intracellular distribution in hepatocellular carcinoma HepG2 cells PMID: 21651858 miR-520b is involved in regulating breast cancer cell migration by targeting HBXIP and IL-8 via a network in which HBXIP promotes migration by stimulating NF-kappaB-mediated IL-8 expression. PMID: 21343296 The x gene of HBV (HBx) is the most common open reading frame integrated into the host genome in hepatocellular carcinoma and the integrated HBx is frequently mutated in hepatocellular carcinoma. PMID: 20811532 Hepatitis B virus pX interacts with HBXAP PMID: 11788598 Elevated levels of GDN/PN1 and XIP mRNAs induced by Allitridi provide valuable molecular evidence for elucidating garlic's efficacies against neurodegenerative and inflammatory diseases. PMID: 11925594 Survivin-HBXIP complexes, but neither survivin nor HBXIP individually, bind pro-caspase-9, preventing its recruitment to Apaf1, and thereby selectively suppressing apoptosis. PMID: 12773388 HBXIP up-regulates LTA expression in hepatocytes. PMID: 15955450 HBXIP sensitizes HepG2 cells to UV light-induced DNA damage. PMID: 16055925 suppressor of var1, 3-like 1 protein interacts with HBXIP, previously identified as a cofactor of survivin in suppression of apoptosis PMID: 16176273 The codon-38 change in genotype C is an independent risk factor for the development of HCC and may serve as a useful molecular marker for predicting the clinical outcomes in patients infected with HBV. PMID: 17050029 One of the functions of HBXIP is its involvement in cell proliferation PMID: 17303008 Hepatitis B virus X protein stimulates the mitochondrial translocation of Raf-1 via oxidative stress PMID: 17428866 HBXIP is a critical target of viral HBx for promoting genetic instability through formation of defective spindles and subsequent aberrant chromosome segregation. PMID: 18032378 HBXIP significantly stimulated the transcription and expression of telomerase reverse transcriptase and increased the activity of telomerase PMID: 18158869 the overexpression of survivin in the majority of NSCLCs together with the abundant or upregulated expression of HBXIP and XIAP suggest that tumours are endowed with resistance against a variety of apoptosis-inducing conditions. PMID: 19885569

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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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