FXR2 (Human) Recombinant Protein (P01)
- Known as:
- FXR2 (Human) Recombinant Protein (P01)
- Catalog number:
- H00009513-P01-25
- Product Quantity:
- 25 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- FXR2 (Human) Recombinant Protein (P01)
Related genes to: FXR2 (Human) Recombinant Protein (P01)
- Gene:
- BZW2 NIH gene
- Name:
- basic leucine zipper and W2 domains 2
- Previous symbol:
- -
- Synonyms:
- HSPC028, MST017, MSTP017
- Chromosome:
- 7p21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-08-05
- Date modifiied:
- 2016-10-05
- Gene:
- C2CD3 NIH gene
- Name:
- C2 calcium dependent domain containing 3
- Previous symbol:
- -
- Synonyms:
- DKFZP586P0123
- Chromosome:
- 11q13.4
- Locus Type:
- gene with protein product
- Date approved:
- 2007-10-17
- Date modifiied:
- 2016-06-08
- Gene:
- FXR2 NIH gene
- Name:
- FMR1 autosomal homolog 2
- Previous symbol:
- FMR1L2
- Synonyms:
- -
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-17
- Date modifiied:
- 2019-04-23
- Gene:
- MBTD1 NIH gene
- Name:
- mbt domain containing 1
- Previous symbol:
- -
- Synonyms:
- SA49P01, FLJ20055
- Chromosome:
- 17q21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2003-01-15
- Date modifiied:
- 2015-04-21
- Gene:
- TMEM63C NIH gene
- Name:
- transmembrane protein 63C
- Previous symbol:
- C14orf171
- Synonyms:
- DKFZp434P0111, CSC1, hsCSC1
- Chromosome:
- 14q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-10
- Date modifiied:
- 2017-10-17
Related products to: FXR2 (Human) Recombinant Protein (P01)
Related articles to: FXR2 (Human) Recombinant Protein (P01)
- Nuclear receptors are central regulators of metabolism, yet therapeutic strategies that enforce continuous receptor activation frequently lead to reduced efficacy and unacceptable toxicity. Here we report a first-principles drug design strategy that aligns pharmacokinetics with physiological signalling cycles. We developed linafexor, a potent non-bile-acid agonist of the farnesoid X receptor (FXR); it is engineered for rapid systemic clearance, which enables pulsatile receptor activation that mirrors endogenous bile acid dynamics. Linafexor has robust efficacy across multiple preclinical models of metabolic dysfunction-associated steatohepatitis, liver fibrosis, primary biliary cholangitis and primary sclerosing cholangitis. Transcriptomic analyses reveal that, unlike long-acting FXR agonists, linafexor preserves cyclic FXR signalling, avoids receptor downregulation and prevents broad transcriptional dysregulation. Direct manipulation of delivery patterns demonstrates that sustained FXR activation-independent of compound identity-induces severe toxicity, establishing activation duration as a determinant of therapeutic index. In phase 1 clinical studies (ClinicalTrials.gov; NCT05082779), linafexor administered once daily produces transient FXR pathway engagement, marked by (1) induction of FGF19, a key endocrine mediator of bile acid feedback regulation; and (2) suppression of C4, an intermediate reflecting hepatic bile acid synthesis, with no treatment-related adverse events. Together, these findings identify pulsatile FXR activation as a mechanistically grounded and clinically translatable strategy, and establish linafexor as a first-in-class therapeutic for bile acid-related liver diseases. - Source: PubMed
Publication date: 2026/06/10
Zang YiShi JingjingZhao GuanguanTang BixiLiu MingliangYao BenqiangWang GaihongPan HualingYang ShengshengDeng RongZhao YishuangZhang ZhenweiGuo Hao-RanSun Dan-DanWang HanlinGao LixinYu JinghuaDiao XingxingLi YongLi JiaXu H Eric - It has long been recognized that the intracellular replication of alphaviruses critically relies on several key host RNA-binding proteins (RBPs), including G3BP1/2 and FXR1/FXR2/FMR1. But how these RBPs modulate alphaviral replication, and whether it would be possible to target them for antiviral treatment, is less explored. Here, using Semliki Forest virus (SFV) as a model, we report that SFV non-structural protein 3 (nsP3) exploits G3BP to drive its condensation and transforms antiviral stress granules into proviral nsP3-G3BP co-condensates. The gel-like co-condensates enrich and protect viral genomic RNAs from host RNase degradation and promote viral translation and replication. nsP3-RBP co-condensation is widespread among alphaviruses, and condensate disruption is a plausible antiviral approach. Thus, these findings uncover a general anti-alphavirus strategy based on the conserved reliance of virus-host protein co-condensation. - Source: PubMed
Publication date: 2026/05/21
Liu YiYao ZhiyingZhang YunZhu ZhenshuoWang ZiqiuChen QiYang ZeminHe YexuanChen XiaoxinTian LeDu JiangWu JinjunKim Hong JooHuang JingZhang YongdengMa WeiruiFan WenchunTaylor J PaulYang Peiguo - N-methyladenosine (mA) modification constitutes a crucial layer of post-transcriptional regulations, but the landscape of its downstream readout effects remains less comprehensively understood. Therefore, we systematically assess the readout effects of mA on mRNA half-life, translation efficiency, and alternative splicing across five cell lines (A549, HEK293T, HUVEC, JURKAT, and human embryonic stem cells (hESCs)) using actinomycin D-disrupted temporal transcriptome, ribosome sequencing, and ultra-high-depth transcriptome sequencing, respectively. Our analysis, coupled with the integration of public and newly profiled mA methylome data, reveals high cell type specificity in mA readouts where mA level alone is insufficient to predict mA readouts. Nonetheless, machine learning models focusing on RNA-binding protein (RBP) binding context can effectively predict the readouts and prioritize four novel mA-associated proteins (FUBP3, FXR2, L1TD1, and DDX6). Their mA-binding ability is validated by mA RNA pull-down, transcriptome-wide binding site mapping, and electrophoretic mobility shift assay, while FUBP3 and L1TD1 are further suggested as mA readers regulating mRNA stability based on half-life profiling of knockout cells. Finally, FUBP3, FXR2, and L1TD1 are demonstrated to regulate hESC differentiation without affecting self-renewal. Together, this study bridges the gap in understanding mA functional readouts and lays the groundwork for future research on mA-mediated stem cell fate decisions. - Source: PubMed
Publication date: 2026/01/20
Huang ZhouLiu RucongWubulikasimu ZibaguliZhao WanqingHuang JiaqiWang JiaxuanZhang TianyuanFan RuiKong WeiCui QinghuaLi YangZhou Yuan - Trained immunity confers innate immune memory via metabolic and epigenetic reprogramming, yet the intercellular mediators regulating this process in host defense remain largely elusive. Here, through plasma exosomal profiling of tuberculosis (TB)-resistant individuals, we identify a trained immunity-inducing long non-coding RNA (lncRNA), termed tuberculosisresister-derived CLOCK regulator 1 (TRCR1). Mechanistically, exosome-derived TRCR1 collaborates with the RNA-binding protein FXR2 to stabilize CLOCK mRNA by forming lncRNA-protein-mRNA complexes in monocytes, thus enhancing circadian regulator CLOCK expression and promoting CLOCK-mediated histone H3 acetylation (K9/K14) at immune gene promoters, ultimately establishing epigenetic memory-mediated antimicrobial activity. We further reveal that Mycobacterium tuberculosis (Mtb)-secreted protein MPT53 induces lung epithelial cells to release TRCR1-enriched exosomes. In mice, TRCR1 training strengthens host anti-Mtb immunity and improves Bacille Calmette-Guérin (BCG) vaccine efficacy. Collectively, our findings unveil an intercellular TRCR1-FXR2-CLOCK axis driving trained immunity at the lung-systemic immune interface, providing a strategy for refining BCG vaccination and preventing infectious diseases. - Source: PubMed
Publication date: 2025/12/30
Yu ShanshanChai QiyaoLu ZheQiu ChanggenZhong YanzhaoWang YiruLei ZehuiQiang LihuaFang YingxuZhang XinwenLi BingxiGao MengqiuZhang LingqiangCheng GongWang JingLiu Cui HuaPang Yu - Loss of isozyme diversity (LID) refers to the selective dependency on a single isozyme following the functional collapse of its redundant counterparts, uncovering a metabolic vulnerability. This metabolic liability establishes LID as a novel framework for precision targeting strategy in cancer therapy. - Source: PubMed
Publication date: 2025/12/12
Ding RuiYu Tian-JianJiang Yi-ZhouXiao YiShao Zhi-Ming