Recombinant Human Oxysterols Receptor Lxr-Beta (NR1H2) Protein (His)

Name: Recombinant Human Oxysterols Receptor Lxr-Beta (NR1H2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07215P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Oxysterols Receptor Lxr-Beta (NR1H2) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P55055
Target Symbol	NR1H2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GEGEGVQLTAAQELMIQQLVAAQLQCNKRSFSDQPKVTPWPLGADPQSRDARQQRFAHFTELAIISVQEIVDFAKQVPGFLQLGREDQIALLKASTIEIMLLETARRYNHETECITFLKDFTYSKDDFHRAGLQVEFINPIFEFSRAMRRLGLDDAEYALLIAINIFSADRPNVQEPGRVEALQQPYVEALLSYTRIKRPQDQLRFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHE
Expression Range	212-460aa
Protein Length	Partial
Mol. Weight	32.7 kDa
Research Area	Cardiovascular
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	Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity. Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism. Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis. Via LPCAT3, triggers the incorporation of arachidonate into phosphatidylcholines of ER membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles. Via LPCAT3 also counteracts lipid-induced ER stress response and inflammation, likely by modulating SRC kinase membrane compartmentalization and limiting the synthesis of lipid inflammatory mediators. Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex.
Subcellular Location	Nucleus.
Protein Families	Nuclear hormone receptor family, NR1 subfamily
Database References	HGNC: 7965 OMIM: 600380 KEGG: hsa:7376 STRING: 9606.ENSP00000253727 UniGene: Hs.432976
Tissue Specificity	Ubiquitous.

Gene Functions References

The authors report that, in Mycobacterium tuberculosis-infected macrophages, IL-36 signaling modulates cholesterol biosynthesis and efflux via LXR. PMID: 29367626
The results suggest that in gestational diabetes mellitus cellular cholesterol homeostasis in the fetoplacental endothelium is modulated via LXR activation and helps to maintain its proper functionality. PMID: 29778664
These findings provide basic information for evaluating the efficacy of LXR-targeted treatment in refractory carcinoma tissues of the human lung and pancreas PMID: 29181837
LXR gene expression was significantly increased in obese children with obstructive sleep apnea-hypopnea syndrome (OSAHS). The severity of OSAHS was positively correlated with COX-2 levels. PMID: 28676625
ULK1 has a role in RPS6KB1-NCOR1 repression of NR1H/LXR-mediated Scd1 transcription and augments lipotoxicity in hepatic cells PMID: 27846372
These data suggest that high doses of insulin downregulate apoA-I gene expression in HepG2 cells through redistribution of FOXO1/LXRbeta complex, FOXA2, and LXRalpha on hepatic enhancer of apoA-I gene. PMID: 27404023
Expression of some LXR-dependent genes of cholesterol trafficking is related to breast tumor characteristics, but not time to recurrence. PMID: 28982861
a positive association of placental PPARgamma mRNA levels and placental DHA levels with baby weight PMID: 27578106
GW3965 significantly increases the expression of liver X nuclear receptor beta (LXRbeta) mRNA, while the liver X nuclear receptor alpha (LXRalpha( mRNA expression did not change a lot, and sensitizes gefitinib by inhibiting NF-kappa B (NF-kappaB) activation. PMID: 28178657
The effects of LXR agonist on interleukin-8 (IL-8) secretion and nuclear factor-kappa B (NF-kappaB) activation in human umbilical vein endothelial cells (HUVECs), is reported. PMID: 27489081
Interactions among SNPs in nucleotide excision repair (NER) genes. PMID: 28115302
we demonstrate that joint deletion of two short conserved motifs that bind UNR and DDX6 relieves repression of 4E-T-bound mRNA, in part reliant on the 4E-T-DDX6-CNOT1 axis. PMID: 27342281
These results suggested that 25-HC promoted ADC cell migration and invasion in an LXR-dependent manner in the monoculture system but that in the coculture system, the 25-HC-induced IL-1beta secretion enhanced the effect of 25-HC in an LXR-independent manner. PMID: 28167281
Protein level of LXRbeta protein was markedly reduced in focal cortical dysplasia. PMID: 27437943
Distinct gene regulatory programs define the inhibitory effects of liver X receptors, NR1H2/NR1H3 and PPARG on cancer cell proliferation. PMID: 27401066
These data describe a novel role for Unr in regulating cellular gene expression. PMID: 26936655
predominant cytoplasmic localization of LXRbeta, which occurs in colon cancer cells but not in normal colon epithelial cells, allowed LXR ligand-induced pyroptosis PMID: 26450852
these data identify a new mechanism of LXR regulation that involves TIPARP, ADP-ribosylation and MACROD1. PMID: 26814197
Intestinal activation of LXR reduces the production of chylomicrons by a mechanism dependent on the apical localization of SR-B1. PMID: 26602218
the release of NER components such as DNA damage binding protein 2 (DDB2) and Xeroderma Pigmentosum complementation group C protein (XPC) following oxidative stress might putatively involve their apoptotic role rather than DNA repair function. PMID: 26263968
LXRalpha expression was not altered in NAFLD. PMID: 26019035
Recent high-throughput analyses of RNA-protein interactions indicate that Unr binds to a large subset of cellular mRNAs, suggesting that Unr may play a wider role in translational responses to cellular signals than previously thought. PMID: 26009170
Destabilization of the torsioned conformation of a ligand side chain inverts the LXRbeta activity. PMID: 26434697
LXRb is the dominant isoform in the rat myocardium and the expression of both LXR isoforms (LXRa and LXRb) did not change after administration of T0901317 PMID: 25659329
This study provides the first evidence to show LXR activation reduces cadmium-induced apoptotic cell death of human renal proximal tubular cells by inhibition of reactive oxygen species production and JNK activation. PMID: 25980575
Activation of LXRs interfered with the release of interleukin-6 from macrophages and, thus, inhibited fibroblast activation and collagen release. PMID: 24618263
LXR-b, through pannexin 1 interaction, can specifically induce caspase-1-dependent colon cancer cell death by pyroptosis. PMID: 25124554
Data show that phospholipase C epsilon 1 (PLCE1) and liver X receptor-beta (LXR-beta) network interactions as important contributory factors for genetic predisposition in gallbladder cancer. PMID: 24863943
Studies indicate that no liver X receptor (LXR) modulator has successfully progressed beyond phase I clinical trials. PMID: 24832115
Report significant reduction in LXR-beta transcript in testes of men with azoospermia. PMID: 24842676
structural analysis of human retinoid X receptor alpha-liver X receptor beta (RXRalpha-LXRbeta) heterodimer on its cognate element, an AGGTCA direct repeat spaced by 4 nt PMID: 24561505
Treatment of human THP-1 macrophages with endogenous or synthetic LXR ligands stimulates both transcriptional and posttranscriptional pathways that result in the selective recruitment of the LXRalpha subtype to LXR-regulated promoters. PMID: 23686114
LXR-beta has roles in regulation of endothelial cellular senescence, related to its antiatherogenic properties PMID: 24398515
Data indicate that LXR-beta genotypes (rs35463555) and (rs2695121) were associated with risk of gallbladder cancer (GBC) as compared to healthy controls whereas LXR-alpha (rs7120118) was not associated with GBC risk. PMID: 23838803
Variants in LXRalpha and LXRbeta genes are not potential contributors to the risk of metabolic syndrome and related traits in an Iranian population. PMID: 24100084
Activation of LXR-alpha and LXR-beta Suppresses Proliferation of Human Colon Cancer Cells. PMID: 22610535
LXRbeta has nonnuclear function in endothelial cell caveolae/lipid rafts that entails crosstalk with estrogen receptor alpha. PMID: 23867501
Molecular modeling of interaction of 17(20)Z- and 17(20)E-pregna-5,17(20)-dien-21-oyl amides with the nuclear receptor LXRbeta PMID: 23987069
In human primary melanocytes, MNT-1, and B16 melanoma cells, TO901317, a synthetic LXR ligand, inhibited melanogenesis. PMID: 23223141
Both LXRalpha and LXRbeta are expressed in rheumatoid arthritis fibroblast-like synoviocytes during inflammatory responses. FLS PMID: 22990668
Activation of LXR reduced the binding of the transcriptional factors AP-1 and NF-kappaB to the ET-1 gene promoter region, thereby regulating gene expression. PMID: 23018104
Discussion of the role of LXR in orchestrating lipid homeostasis and neuroinflammation in the brain. The ability of LXR to attenuate Alzheimer disease pathology makes them potential therapeutic targets for this neurodegenerative disease. [Review Article] PMID: 22766509
Pharmacological activation of endothelial LXRs reduces angiogenesis by restraining cholesterol-dependent vascular endothelial growth factor receptor-2 compartmentation and signaling. PMID: 22723445
liver x receptors are activated by phospholipase A2 modified low density lipoproteins in human macrophages PMID: 22367754
Te results of this study suggested taht genetic variations in MMEL1, ECE1, ECE2, AGER, PLG, PLAT, NR1H3, MMP3, LRP1, TTR, NR1H2, and MMP9 genes do not play major role among the Finnish AD patient cohort. PMID: 22027013
LXR are involved in the metabolism and inflammation in human diseases; nonalcoholic fatty liver disease (NAFLD) is classically associated with lipid metabolic disorders and inflammatory responses. PMID: 22257474
RXRalpha and LXR activate two promoters in placenta- and tumor-specific expression of PLAC1. PMID: 21937108
Concomitant activation of ERbeta and inhibition of LXRbeta prevents 27-hydroxycholesterol effects and reduces the progression of Parkinson's disease by precluding tyrosine hydroxylase reduction and alpha-synuclein accumulation. PMID: 21951066
There was no association between NR1H3 SNPs and pre-eclampsia, but the NR1H2 polymorphism rs2695121 was strongly associated with preeclampsia. PMID: 22029530
we concluded that LXR-alpha/beta gene expression ratio is a critical factor to activate POMC gene expression in ACTH-secreting pituitary adenomas. PMID: 21356276

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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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