PUM2 (Human) Recombinant Protein (Q01)
- Known as:
- PUM2 (Human) Recombinant Protein (Q01)
- Catalog number:
- H00023369-Q01-25
- Product Quantity:
- 25 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- PUM2 (Human) Recombinant Protein (Q01)
Related genes to: PUM2 (Human) Recombinant Protein (Q01)
- Gene:
- PUM2 NIH gene
- Name:
- pumilio RNA binding family member 2
- Previous symbol:
- -
- Synonyms:
- PUMH2, KIAA0235
- Chromosome:
- 2p24.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-27
- Date modifiied:
- 2015-11-05
Related products to: PUM2 (Human) Recombinant Protein (Q01)
Related articles to: PUM2 (Human) Recombinant Protein (Q01)
- Loss of the RNA-binding proteins PUM1 and PUM2 leads to gastrulation failure and embryonic lethality, but the mechanisms underlying this phenotype remain unclear. Using embryoid bodies as an in vitro model of early embryogenesis, we show that PUM proteins maintain lineage balance by post-transcriptionally repressing germline fate, silencing pluripotency networks, and promoting somatic differentiation. They directly inhibit Prdm1 to prevent premature germline specification and activate Wnt signaling to support germ layer formation. PUM-deficient cells exhibit impaired patterning along both the anterior-posterior and dorsoventral axes, along with defective neural differentiation. RIP-seq analyses identify key developmental mRNAs directly regulated by PUM1 and PUM2, linking these proteins to multiple regulatory modules. These findings establish PUM proteins as essential post-transcriptional regulators of early embryogenesis, demonstrating how RNA-binding proteins coordinate cell fate and patterning. - Source: PubMed
Publication date: 2026/07/09
Lu TingYang YiyingLi XiajunShi Shuo - Sevoflurane preconditioning (SPC) is a common protective strategy against myocardial ischemia-reperfusion injury (MI/RI). MIR210HG is a hypoxia-induced long non-coding RNA and involves multiple molecular pathways. - Source: PubMed
Publication date: 2026/07/01
Gan LuDu XiaobingLu LuWang XiaomingChai Fei - Ectoine is a compatible solute originally discovered in desert microorganisms and serves as a key weapon for microbes to cope with extreme environmental threats, such as drought and high salinity. Owing to its exceptional water-binding capacity and protective properties, ectoine is extensively used in biomedicine, cosmetics, and industrial biocatalysis. To overcome the efficiency bottleneck of heterologous ectoine biosynthesis in non-halophilic strains, we introduced a synthetic biomolecular condensate system that has been successfully employed in protein overexpression to enhance ectoine formation in pathways constructed with biosynthetic ancestral enzymes in the engineering of Vibrio natriegens. First, the ancestral core metabolic enzymes EctA, EctB, and EctC were reconstructed using an integrated bioinformatics process, and the selected ancestral enzymes were analyzed using molecular dynamics simulations. Subsequently, ectoine biosynthesis via 27 combinatory pathways involving core metabolic enzymes was systematically evaluated. The Pum2-ELP fusion protein system was then introduced to construct membraneless biomolecular condensates within the cells. Such a design was justified by the report that the interaction between the tandem PRS tags at the 3' ends of mRNAs of metabolic enzymes and Pum2 in the condensate of Pum2-ELP could recruit ribosomes and metabolic enzymes into the condensates, enabling substrate channeling in the biosynthetic pathway because of the physical approximation of the relevant components. The experimental results demonstrated that the optimal hybrid pathway exhibited synergistic catalytic efficiency. Upon introducing the Pum2-ELP system, the ectoine yield increased by approximately 1.7 folds, which should be ascribed to the substrate channeling effect. In a 5-L bioreactor batch fermentation, the engineered strain achieved a final titer of ∼50 g/L within 24 h, reaching a high volumetric productivity of 2.08 g/(L·h). This study demonstrates that integrating evolution-derived ancestral metabolic enzymes with engineered spatial assembly can significantly optimize metabolic flux, providing an efficient platform strategy for the rapid and high-titer industrial production of ectoine and other high-value compatible solutes under controlled fermentation conditions. - Source: PubMed
Publication date: 2026/06/24
Fang TianzhiLi DandanHu MengkaiLiu KunChen YuWu ChuanchaoLi XiangfeiZhang HuiminZhao MingLiu YanXue ZhenglianLiu QingtaoWang Tianwen - The engraftment of induced cells from human pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs) for myocardial infarction therapy is critically hindered by their low cell-cycle activity and survival rates. In this study, we explored the role of the long noncoding RNA activated by DNA damage (NORAD) in enhancing the cell-cycle activity and engraftment of hiPSC-CMs, providing new insights into myocardial repair. - Source: PubMed
Publication date: 2026/06/25
Huan KanghuiJiang YujianXie XinXu WeifengDuan XiaoleiYao SaiCheng YanliLi ShaomengDuan YanfangYuan YingxinSun YeyingZhao MengBian Weihua - Oxaliplatin resistance remains a significant therapeutic challenge in the treatment of colon adenocarcinoma (COAD). In this study, we identified the RNA-binding protein PUM2 as a key driver of oxaliplatin resistance. Bioinformatics analysis revealed that PUM2 was upregulated in tumor tissues, which correlated with poor patient prognosis. Knockdown of PUM2 inhibited cell proliferation and migration and enhanced oxaliplatin sensitivity by promoting ferroptosis. These findings were validated in vivo, where PUM2 knockdown potentiated the anti-tumor efficacy of oxaliplatin in mouse xenograft models. Mechanistically, PUM2 was found to bind to the mRNA of the E3 ubiquitin ligase NEDD4L. Downregulation of NEDD4L reduced the ubiquitination and degradation of the transcription factor NRF2, leading to NRF2 accumulation and inhibiting ferroptosis. Furthermore, combining an NRF2 inhibitor (ML385) with oxaliplatin promoted ferroptosis and suppressed the growth of resistant tumors in vivo. In conclusion, our findings elucidate a novel PUM2/NEDD4L/NRF2 axis that promotes oxaliplatin resistance in COAD by inhibiting ferroptosis, thereby providing a preclinical rationale for future investigation into this pathway to overcome chemoresistance. - Source: PubMed
Publication date: 2026/06/18
Xie JiachengDong KaiWu JialinCheng XinshengWang ShikaiZhang Hongzhen