ZRANB2 antibody - middle region (ARP35779_P050)
- Known as:
- ZRANB2 (anti-) - middle region (ARP35779_P050)
- Catalog number:
- arp35779_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- ZRANB2 antibody - middle region (ARP35779_P050)
Related genes to: ZRANB2 antibody - middle region (ARP35779_P050)
- Gene:
- ZRANB2 NIH gene
- Name:
- zinc finger RANBP2-type containing 2
- Previous symbol:
- ZNF265
- Synonyms:
- ZIS, ZIS1, ZIS2
- Chromosome:
- 1p31.1
- Locus Type:
- gene with protein product
- Date approved:
- 1999-07-19
- Date modifiied:
- 2016-10-05
Related products to: ZRANB2 antibody - middle region (ARP35779_P050)
Related articles to: ZRANB2 antibody - middle region (ARP35779_P050)
- Zinc finger Ran-binding domain-containing protein 2 (ZRANB2) is an RNA-binding protein that plays a key role in alternative splicing. It contains two N-terminal RanBP2-type ZF domains in which four cysteine residues coordinate Zn(II) in a tetrahedral geometry to afford proper folding and function. Persulfidation, a post-translational modification in which cysteine thiols (-SH) are converted to persulfides (-SSH) by hydrogen sulfide (HS), has emerged as a means for regulating ZF activity. ZRANB2 is frequently identified as persulfidated in chemoselective proteomics screens, and here, we evaluate the direct modification of ZRANB2 by HS. Using a recombinantly expressed two-domain construct (ZRANB2-2D), we report that Zn(II)-bound ZRANB2-2D undergoes persulfidation when exposed to HS and oxygen with superoxide generated as an intermediate. This modification induces a loss of Zn(II)-dependent structure and abrogates binding to an RNA oligonucleotide from exon 3 of the transformer-2 protein homolog beta (TRA2B) RNA, a splicing target of ZRANB2, as well as to an optimized RNA oligonucleotide. Consistent with impaired RNA binding, cellular treatment with HS leads to decreased formation of a TRA2B splice product, suggesting a connection to persulfidation of ZRANB2 in cells. Notably, addition of a reductant restores ZRANB2-2D RNA-binding activity in vitro. These results position persulfidation as a rheostat for modulating ZF protein function, exemplified here by its role in regulating ZRANB2 RNA binding and splicing. - Source: PubMed
Publication date: 2026/01/03
Hursey Matthew SReitz Abigail DFidler Samuel EMichel Sarah L J - Bladder cancer (BC) is a highly prevalent form of cancer worldwide, and cisplatin (CDDP) resistance poses a major challenge to patients. Cytoplasmic linker-associated protein 2 (CLASP2) is a member of the microtubule plus-end tracking protein family and is involved in the regulation of microtubule dynamics. In this study, we evaluated the influence of CLASP2 on BC progression and cisplatin resistance. Levels of CLASP2, HNRNPA1, NONO, ZRANB2, FUS, KHSRP and QKI in BC tissues and cells were tested by RT-qPCR. Protein levels of CLASP2 and KHSRP were detected by Western blot. Cell viability and IC50 of cisplatin-treated BC cells were measured by CCK-8. Cell proliferation and apoptosis were determined using colony formation assay and flow cytometry, respectively. RNA immunoprecipitation (RIP) and Co-immunoprecipitation (Co-IP) experiments were adopted to verify target genes of CLASP2. Cellular localization of CLASP2 and MAPRE1 was detected utilizing immunofluorescence staining. The xenograft tumor model was established in BALB/c nude mice. We found that iCLASP2 levels were increased in CDDP-resistant BC tissues and cells. Suppression of CLASP2 impeded BC cell proliferation and alleviated their resistance to CDDP. KHSRP positively influenced the stability of CLASP2 mRNA. There was a protein interaction between CLASP2 and MAPRE1. Silencing KHSRP or MAPRE1 reversed the effect exerted of CLASP2 on BC cells. CLASP2 decreased the sensitivity of BC to CDDP in vivo. Our results imply that CLASP2 contributes to tumorigenesis and cisplatin resistance in BC via targeting MAPRE1, thereby promoting BC progression and providing a new therapeutic target for BC treatment. - Source: PubMed
Publication date: 2025/05/17
Wang RuizheZhao ChengOu ZhenyuChen Lingxiao - LncRNA has been implicated in the regulation of diabetes. We identified a novel lncRNA that inhibits phosphorylation of acetyl-CoA carboxylase 1 to modulate the dysfunction of vascular endothelial cells under high glucose conditions. In vitro experiments were performed to investigate the effects of lnc RNA ZRANB2-AS2 on ACC1 phosphorylation, free fatty acid and triglyceride levels, angiogenesis, cell apoptosis, cell proliferation and migration rate. Further, in vivo experiments were designed to examine the effects of lnc RNA ZRANB2-AS2 on the level of ACC1, the limb ischemia and foot movement of mice, as well as on apoptosis, cell proliferation, and migration of vascular endothelial cells under conditions of high glucose.By RNA sequencing, we identified a lncRNA, ZRANB2-AS2, which is highly expressed in human umbilical vein endothelial cells (HUVECs) under high glucose condition. We demonstrated that it could promote apoptosis and inhibit angiogenesis, proliferation and migration of endothelial cells. Using RNA pull-down and RIP assays, the binding specificity of lncRNA ZRANB2-AS2 and acetyl-CoA carboxylase 1(ACC1) was determined. We further established the rescue assay by adding CMS-121, a specific ACC1 inhibitor. These findings suggested that CMS-121 could reverse the inhibition of lncRNA ZRANB2-AS2 on ACC1 phosphorylation, decrease intracellular free fatty acid and triglyceride levels. We conducted in vivo experiments to determine the inhibitory effect of lncRNA ZRANB2-AS2 in diabetic mice model. Lnc ZRANB2-AS2 inhibits cell proliferation, migration and angiogenesis while accelerates apoptosis of endothelial cells by regulating the phosphorylation of acetyl-CoA carboxylase 1 in diabetes. - Source: PubMed
Publication date: 2025/04/22
Chen TianchiWang BingLi DonglinYu XinyuLv KejiaZhu QianqianQiu ChenyangHe YangyanZhang HongkunWu Ziheng - Ran-binding domain-containing protein 2 (ZRANB2) is a zinc finger (ZF) protein that plays a key role in alternative splicing. ZRANB2 is composed of two ZF domains that contain four invariant cysteine residues per domain. ZRANB2 binds RNA targets that contain AGGUAA sequence motifs. Three constructs of ZRANB2, ZRANB2-ZF1 (first ZF domain), ZRANB2-ZF2 (second ZF domain), and ZRANB2-2D (both ZF domains), were isolated in the apo form and shown to bind Zn(II) via UV-visible-monitored competitive titrations with Co(II) as a spectroscopic probe. Zn binding to each construct led to the adoption of a limited secondary structure of each domain, as measured by circular dichroism (CD). Hydrogen-deuterium exchange coupled with mass spectrometry (HDX-MS) of the two-domain construct, ZRANB2-2D, revealed that both ZF domains adopt a more rigid structure upon Zn binding. Zn binding to the first ZF domain resulted in a greater decrease in the conformational dynamics than Zn binding to the second ZF domain. RNA binding to TRA2B pre-mRNA, a physiological splicing target, was measured by fluorescence anisotropy (FA), and high-affinity RNA binding was found to require Zn coordination to both domains. HDX-MS of ZRANB2-2D with TRA2B RNA as well as two optimized RNA sequences that contain a single and double AGGUAA hexamer revealed additional protection from H/D exchange for ZRANB2 in the presence of RNA. Here, greater protection was observed for the second ZF of ZRANB2-2D, suggesting a larger effect on conformational dynamics. A model for zinc-mediated RNA binding of ZRANB2 is proposed. - Source: PubMed
Publication date: 2024/12/16
Hursey Matthew SReitz Abigail DKihn Kyle CDeredge Daniel JMichel Sarah L J - Targeting and manipulating endogenous RNAs in a sequence-specific manner is essential for both understanding RNA biology and developing RNA-targeting therapeutics. RNA-binding zinc fingers (ZnFs) are excellent candidates as designer proteins to expand the RNA-targeting toolbox, due to their compact size and modular sequence recognition. Currently, little is known about how the sequence of RNA-binding ZnF domains governs their binding site specificity. Here, we systematically introduced mutations at the RNA-contacting residues of a well-characterized RNA-binding ZnF protein, ZRANB2, and measured RNA binding of mutant ZnFs using a modified RNA bind-n-seq assay. We identified mutant ZnFs with an altered sequence specificity, preferring to bind a GGG motif instead of the GGU preferred by wild-type ZRANB2. Further, through a series of all-atom molecular dynamics simulations with ZRANB2 and RNA, we characterized changes in the hydrogen-bond network between the protein and RNA that underlie the observed sequence specificity changes. Our analysis of ZRANB2-RNA interactions both in vitro and in silico expands the understanding of ZnF-RNA recognition rules and serves as a foundation for eventual use of RNA-binding ZnFs for programmable RNA targeting. - Source: PubMed
Publication date: 2025/01/22
Liang QishanXiang Joy SYeo Gene WCorbett Kevin D