USF2 antibody - N-terminal region (ARP33482_P050)
- Known as:
- USF2 (anti-) - N-terminal region (ARP33482_P050)
- Catalog number:
- arp33482_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- USF2 antibody - N-terminal region (ARP33482_P050)
Related genes to: USF2 antibody - N-terminal region (ARP33482_P050)
- Gene:
- USF2 NIH gene
- Name:
- upstream transcription factor 2, c-fos interacting
- Previous symbol:
- -
- Synonyms:
- FIP, bHLHb12
- Chromosome:
- 19q13
- Locus Type:
- gene with protein product
- Date approved:
- 1994-10-25
- Date modifiied:
- 2014-11-19
Related products to: USF2 antibody - N-terminal region (ARP33482_P050)
Related articles to: USF2 antibody - N-terminal region (ARP33482_P050)
- The rational design of optical crystals with large birefringence, deep-ultraviolet (DUV) transparency, and strong nonlinear optical effects remains a significant challenge, primarily due to the difficulty in precisely controlling the alignment of functional anisotropic units within the crystal lattice. Herein, we propose and demonstrate a hydrogen-bond-directed assembly strategy to regulate the packing density and orientation of π-conjugated cations in urea derivatives, achieving a synergistic enhancement of optical properties. Four novel urea derivative crystals, CO(NH)HCO (UCO), C(OH)(NH)NO (UNO), [C(OH)(NH)]SiF (USF-1), and [C(OH)(NH)]CO(NH)SiF (USF-2), were synthesized. Among them, UNO exhibits a record-high birefringence of 0.372 at 546 nm within the urea family, while USF-1 and USF-2 achieve DUV transparency with cutoff edges below 200 nm (193 and 195 nm, respectively). Structural and theoretical analyses reveal that the introduced groups ([HCO], [NO], [SiF] ) reconstruct the hydrogen-bonding network, steering the planar [CO(NH)] from the vertical and antiparallel arrangement found in pristine urea into a highly parallel alignment within layered structures. This significantly enhances macroscopic optical anisotropy. This work establishes a hydrogen-bond engineering paradigm for the rational design of high-performance UV/DUV optical crystals by controlling π-conjugated unit assembly. - Source: PubMed
Publication date: 2026/04/14
Jiang PengQin YuqiFeng JunweiGai MinqiangPan Shilie - The SERPINE1 gene encodes the serine protease inhibitor plasminogen activator inhibitor type-1 (PAI-1), a major negative regulator of the plasmin-dependent pericellular proteolytic cascade and a crucial determinant in the program of stromal remodeling. Recent omics approaches confirmed that high tumor SERPINE1 levels are prognostic for poor disease outcomes and shorter disease-free survival in various malignancies. Kinetic analysis of biomarkers of cell cycle transit in growth-synchronized p53 dual mutant human keratinocytes confirmed that PAI-1 transcription occurred early after growth activation of quiescent (G) cells and prior to G1 entry. Previous evidence has confirmed that differential residence of USF family members (USF1→USF2 switch) at the PE2 region hexanucleotide E box motif (CACGTG) in the SERPINE1 proximal promoter characterizes the G→G transition period and the transcriptional status of the SERPINE1 gene. A consensus PE2 E box motif (5'-CACGTG-3') at nucleotides -566 to -561 is required for USF occupancy of the PE2 E box and serum-stimulated SERPINE1 transcription. Interference with USF2 occupancy of the PE2 E Box site by a double-stranded PE2 "decoy", or induced expression of a dominant-negative USF (A-USF) construct, attenuate serum- and TGF-β1-stimulated SERPINE1 synthesis. Tet-Off activation of an A-USF insert reduced both PAI-1 and PAI-2 transcripts while increasing the fraction of proliferating (Ki-67 cells). Conversely, overexpression of USF2 or adenoviral delivery of a PAI-1 vector inhibited HaCaT colony expansion. These findings are discussed in this review and collectively suggest that the USF1→USF2 transition at the PE2 E box site and subsequent SERPINE1 transcription impact serum-stimulated keratinocyte growth and, likely, cell cycle progression. - Source: PubMed
Publication date: 2026/03/22
Higgins Stephen PCzekay Ralf-PeterHiggins Craig EHiggins Paul J - Autophagy serves as a crucial defense mechanism against Mycobacterium tuberculosis (Mtb) survival within infected macrophages. Transcription factor EB (TFEB) and upstream stimulatory factor 2 (USF2) belong to the bHLH-Zip family and regulate the transcription of autophagy-related genes, thereby modulating host-pathogen interactions. However, the mechanisms by which Mtb regulates these transcriptional regulatory factors to inhibit infection remain largely unexplored. This study demonstrated that PE_PGRS23 protein of Mtb impairs macrophage autophagy by inhibiting the transcription of the autophagy gene, thereby enhancing Mtb intracellular survival. Importantly, PE_PGRS23 facilitates the nuclear translocation of TFEB through PI3K-AKT-mTOR-mediated dephosphorylation. Concurrently, PE_PGRS23 promotes the nuclear translocation of USF2, which competes with TFEB for binding to the MAPLC3 promoter, ultimately suppressing MAPLC3 transcription and inhibiting autophagy. Furthermore, murine infection models demonstrated that PE_PGRS23 enhances Mtb survival and exacerbates Mtb-induced lung tissue damage. These findings underscore the critical role of the Mtb PE_PGRS23 protein in inhibiting autophagy by competitively binding of TFEB and USF2 at the MAPLC3 promoter. This mechanism facilitates the intracellular persistence of Mtb, providing theoretical insights into how the pathogen evades innate immune responses. - Source: PubMed
Feng TingtingZhang ZhenjunWang HuiZang XinxinZhang JiajunJiang YanyanCui YingyingDuan YifanGuo RuonanGao YunjieChen ChunwenDang GuanghuiLiu Siguo - Atherosclerosis (AS) is the primary cause of most cardiovascular diseases, such as coronary artery disease (CAD), myocardial infarctions and strokes. S-nitrosylation (SNO), a prototypic redox-based posttranslational modification, is involved in cardiovascular diseases. Histidine triad nucleotide-binding protein 1 (HINT1) was identified S-nitrosylated at cysteine 84 (Cys84) in oxidized low-density lipoprotein (ox-LDL)-stimulated macrophages. S-nitrosylation of HINT1 (SNO-HINT1) in macrophages exacerbates lipid uptake and foam cell formation through upregulating SR-A1 and CD36. Furthermore, SNO-HINT1 was determined to inhibit degradation of SR-A1 mediated by lysosome pathway and promote CD36 transcription mediated by USF2. Mechanistically, comparing to unmodified HINT1, S-nitrosylation of HINT1 drives its CRM1 dependent nuclear export, which resulted in its more interaction with SR-A1 in cytoplasm and less interaction with USF2 in nucleus. Furthermore, inducible nitric oxide synthase (iNOS) was demonstrated as the enzyme that mediates the S-nitrosylation of HINT1. SNO-HINT1 was demonstrated to drive the development of atherosclerosis in LDLR mice fed with high fat diet. Overall, SNO-HINT1 drives foam cell formation and atherosclerosis through reducing degradation of SR-A1 mediated by lysosome pathway and promoting CD36 transcription mediated by USF2. Our findings suggest that SNO-HINT1 can be a potential therapeutic target for atherosclerosis. - Source: PubMed
Publication date: 2026/01/28
Tang KeZheng TianshuZhu HaoXu FanMa CongcongQi ZhenhuaCao SiyiDa QiangYan KeWu WenchengHan YiXie LipingZhang YanJi Yong - Melanocyte-derived cutaneous malignant melanoma (MM) is the most common malignancy of the skin and the leading cause of skin cancer-related deaths worldwide. Although SIRPB1 is involved in tumorigenesis and development in various cancers, its role in cutaneous MM is still not elucidated. Our work investigates the role of SIRPB1 in the pathogenesis of cutaneous MM and explores its specific function mechanism. SIRPB1 downregulation inhibited the proliferation, migration, and invasion of melanoma cells, both and . SIRPB1 knockdown could significantly upregulate SOSC1 expression in melanoma cells, negatively regulating STAT3. STAT3 agonists reversed the SIRPB1 gene knockdown-induced tumor inhibition. USF2 played a transcriptional regulatory role by binding to the SIRPB1 promoter sequence. SIRPB1 is an oncogene of cutaneous MM, transcriptionally regulated by USF2. It promotes cutaneous MM tumorigenicity by regulating the SOCS1/STAT3 signaling. Hence, the targeted regulation of SIRPB1 and USF2 could be a promising therapeutic strategy for MM. - Source: PubMed
Publication date: 2025/11/17
Ning DanmeiXie DongHuang ShuqiHe PingxiuChen XiaoxiaoFeng NanfeiWan Chuan