ZNF350 antibody - N-terminal region (ARP37781_P050)
- Known as:
- ZNF350 (anti-) - N-terminal region (ARP37781_P050)
- Catalog number:
- arp37781_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- ZNF350 antibody - N-terminal region (ARP37781_P050)
Related genes to: ZNF350 antibody - N-terminal region (ARP37781_P050)
- Gene:
- ZNF350 NIH gene
- Name:
- zinc finger protein 350
- Previous symbol:
- -
- Synonyms:
- ZBRK1, ZFQR
- Chromosome:
- 19q13.41
- Locus Type:
- gene with protein product
- Date approved:
- 2003-05-16
- Date modifiied:
- 2014-11-19
Related products to: ZNF350 antibody - N-terminal region (ARP37781_P050)
Related articles to: ZNF350 antibody - N-terminal region (ARP37781_P050)
- Vitiligo is an acquired depigmentary disorder caused by the loss of functional melanocytes. Increasing evidence suggests that competing endogenous RNA (ceRNA) interactions participate in this process, yet their global architecture in vitiligo remains unclear. - Source: PubMed
Publication date: 2025/08/30
Yang HedanLi XiuzhenZhang XiaoliGe YipingYang YinLin Tong - The varying individual responses to Pegylated interferon-α (Peg-IFNα) in patients with chronic hepatitis B (CHB) pose significant hurdles in treatment optimization, and the underlying mechanisms remain unclear. - Source: PubMed
Publication date: 2024/11/07
Guo JianhuiGuo ShaoyingChen TianbinZeng YongbinFu YaOu Qishui - TRIP4 is a conserved transcriptional coactivator that is involved in the regulation of the expression of multiple genes. It consists of a classical N-terminal C2HC5-like zinc-finger domain and a conserved C-terminal ASCH domain. Here, we characterized the DNA-binding properties of the human TRIP4 ASCH domain. Our biochemical data show that TRIP4-ASCH has comparable binding affinities toward ssDNA and dsDNA of different lengths, sequences, and structures. The crystal structures reveal that TRIP4-ASCH binds to DNA substrates in a sequence-independent manner through two adjacent positively charged surface patches: one binds to the 5'-end of DNA, and the other binds to the 3'-end of DNA. Further mutagenesis experiments and binding assays confirm the functional roles of key residues involved in DNA binding. In summary, our data demonstrate that TRIP4-ASCH binds to the 5' and 3'-ends of DNA in a sequence-independent manner, which will facilitate further studies of the biological function of TRIP4. - Source: PubMed
Publication date: 2024/06/12
Hu ChengtaoChen ZiyueWang GuanchaoYang HuiDing Jianping - Osteoporosis (OP) is characterized by bone mass decrease and bone tissue microarchitectural deterioration in bone tissue. This study identified potential biomarkers for early diagnosis of OP and elucidated the mechanism of OP. - Source: PubMed
Publication date: 2024/04/18
Zhu NaiqiangHou JingyiSi JingyuanYang NingChen BinWei XuZhu Liguo - Tumor suppression by inducing NCOA4-mediated ferroptosis has been shown to be feasible in a variety of tumors, including gliomas. However, the regulatory mechanism of ferroptosis induced by NCOA4 in glioma has not been studied deeply. HECW1 and ZNF350 are involved in the biological processes of many tumors, but their specific effects and mechanisms on glioma are still unclear. In this study, we found that HECW1 decreased the survival rate of glioma cells and enhanced iron accumulation, lipid peroxidation, whereas ZNF350 showed the opposite effect. Mechanistically, HECW1 directly regulated the ubiquitination and degradation of ZNF350, eliminated the transcriptional inhibition of NCOA4 by ZNF350, and ultimately activated NCOA4-mediated iron accumulation, lipid peroxidation, and ferroptosis. We demonstrate that HECW1 induces ferroptosis and highlight the value of HECW1 and ZNF350 in the prognostic evaluation of patients with glioma. We also elucidate the mechanisms underlying the HECW1/ZNF350/NCOA4 axis and its regulation of ferroptosis. Our findings enrich the understanding of ferroptosis and provide potential treatment options for glioma patients. - Source: PubMed
Publication date: 2023/12/04
Lin YuancaiGong HailongLiu JinliangHu ZhiwenGao MingjunYu WeiLiu Jing