ANXA7 antibody - N-terminal region (ARP36584_T100)
- Known as:
- ANXA7 (anti-) - N-terminal region (ARP36584_T100)
- Catalog number:
- arp36584_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- ANXA7 antibody - N-terminal region (ARP36584_T100)
Related genes to: ANXA7 antibody - N-terminal region (ARP36584_T100)
- Gene:
- ANXA7 NIH gene
- Name:
- annexin A7
- Previous symbol:
- ANX7
- Synonyms:
- -
- Chromosome:
- 10q22.2
- Locus Type:
- gene with protein product
- Date approved:
- 1994-07-20
- Date modifiied:
- 2014-11-19
Related products to: ANXA7 antibody - N-terminal region (ARP36584_T100)
Related articles to: ANXA7 antibody - N-terminal region (ARP36584_T100)
- Despite significant advancements in CRISPR/Cas-based genome editing technology over the past decade, achieving simultaneous homozygous gene editing at multiple targets in primary cells remains a major challenge. In this study, we developed and constructed a CRISPR multi-gene targeting system that integrates episomal vectors with tRNA-sgRNA array technology. This approach leverages scaffold/matrix attachment region (S/MAR) sequences to enable sustained episomal expression of both Cas9 and single-guide RNAs (sgRNAs) without genomic integration, thereby enhancing gene editing efficiency. For simultaneous editing of multiple loci, we used the tRNA-sgRNA architecture to process multiple sgRNAs from a single vector. Using this system in porcine fetal fibroblasts, we achieved concurrent editing of six genes, namely , , , , , and , in individual cells. These edited cells supported normal development following somatic cell nuclear transfer, yielding blastocysts with unaltered developmental competence. Collectively, our findings establish a framework for the application of CRISPR/Cas9 in gene-edited pigs, facilitating the generation of multi-gene-edited animals for biomedical and agricultural applications. - Source: PubMed
Publication date: 2026/05/08
Jiang ChaoqianYang DongyanSun ChengboRen XingruiLi TianzeWu JiayanTian JianFeng MingjieYao YuchangSong JunWeng XiaogangMu Yanshuang - This study aimed to investigate the roles of ANXA7 and its upstream regulator RNF168 in Crohn's disease (CD) progression, focusing on their interaction with inflammation and intestinal mucosal barrier disruption. Colon tissues from CD patients, including inflamed and uninflamed tissues, were analyzed to assess ANXA7 expression. The biological functions of ANXA7 were studied in vitro using LPS/ATP-stimulated NCM460 cells, employing ANXA7 knockdown and overexpression experiments. Protein-protein interactions were examined using co-immunoprecipitation (Co-IP) and mass spectrometry. The regulatory role of RNF168 in ANXA7 degradation was explored through Co-IP and ubiquitination assays. The effects of RNF168 and ANXA7 on autophagy and NLRP3 inflammasome-induced pyroptosis were assessed. In vivo experiments were conducted using IL-10 knockout (KO) mice, RNF168 mice with TNBS-induced colitis, and organoids to investigate the therapeutic potential of RNF168 and ANXA7 manipulation. ANXA7 expression was significantly reduced in inflamed tissues and correlated with CD-related inflammatory markers. RNF168 promoted the ubiquitination and degradation of ANXA7, thereby suppressing autophagy and inducing NLRP3 inflammasome-mediated pyroptosis. The in vitro and in vivo biological functions of sh-RNF168 were rescued by sh-ANXA7. ELK1 was identified as a key transcription factor regulating RNF168 expression, linking transcriptional regulation with inflammation and disease progression. Our findings suggest a mechanistic model where ELK1 upregulates RNF168, leading to ANXA7 degradation, suppression of autophagy, and enhanced pyroptosis, thereby promoting CD progression and intestinal barrier disruption. Targeting the RNF168-ANXA7 axis offers a potential therapeutic strategy for CD. - Source: PubMed
Publication date: 2026/01/10
Wang HonggangLiu YujunJiang WenliangJi YunCheng ShaoqiCheng ChaoXu ZiweiZhang ChangheSun JingZhao Jie - Directed axonal trafficking of mRNA via ribonucleoprotein (RNP) complexes is essential for neuronal function and survival. However, mechanisms governing retrograde RNP transport remain poorly understood. Here, we reveal that Annexin A7 (ANXA7) promotes the recruitment of aggregation-prone T-cell intracellular antigen 1 (TIA1)-containing RNPs to cytoplasmic dynein, enabling their retrograde trafficking to the soma for degradation. Both persistent and transient Ca²⁺ elevation disrupted this function of ANXA7, leading to the detachment of TIA1 granules from dynein, impairing their transport, and subsequently triggering pathological TIA1 aggregation within axons. Similarly, ANXA7 knockdown decouples TIA1 granules from dynein, preventing their transport and inducing pathological aggregation of TIA1, which culminates in axonopathy and neurodegeneration both in vitro and in vivo. Conversely, ANXA7 overexpression reinforces trafficking and counteracts aberrant aggregation of TIA1-containing RNPs in axons. We describe here a Ca -regulated mechanism which modulates retrograde axonal trafficking of RNPs and prevents the formation of pathological aggregates in axons. - Source: PubMed
Publication date: 2025/11/03
Feng YuLuan TongshuZhang ZhendaWang WeiChu YuanyuanWan SijiaPan XiaorongLi JieLiu YifanXu YaqianDou KunWang Tong - Cardiovascular diseases, particularly coronary atherosclerosis, pose a major health burden, with plaque rupture and erosion contributing to acute coronary syndrome (ACS). Platelet adhesion and aggregation are key in thrombosis, making them critical therapeutic targets. This study aimed to elucidate the regulatory role of annexin A7 (ANXA7) in the progression of coronary atherosclerosis. - Source: PubMed
Publication date: 2025/06/23
Lin YueYe LifangQian LinglingDing KunZhu HangyaoWang Lihong - Spinal cord injury is characterized by high incidence and high disability, and the specific targets and drugs have not yet been explored. Lipid droplet is a type of organelles that regulates lipid metabolism and oxidative stress. And the regulatory mechanisms of lipid droplets on spinal cord injury remain unclear. Herein, it is found that GTPase activation of Annexin A7 (ANXA7) promotes the up-regulation of genes related to lipid droplet formation. ANXA7 can interact with peroxisome proliferator-activated receptor gamma (PPARγ) to enhance the stability of PPARγ, and promote lipid droplet formation and interaction with mitochondria through promoting Perilipin 5 expression. Then, oxidative stress and lipid peroxidation are inhibited due to the promotion of nuclear factor erythroid 2-related factor 2 (NRF2) nuclear translocation and expression of glutathione peroxidase 4 (GPX4). ANXA7 activation promotes lipid droplet formation and mitochondria-lipid droplet interaction by enhancing nuclear translocation of PPARγ, which contributes to inhibiting lipid peroxidation and neuron damage. Furthermore, activation of PPARγ can promote neural function recovery and spinal cord repair in mice. The focus of this study is to investigate the effects of lipid droplets regulated by ANXA7/PPARγ, providing new targets and strategies for spinal cord injury. - Source: PubMed
Publication date: 2025/02/25
Chen LuLiu HaoranJiang LinlinWang ZihangChang YongLi NaFeng Shiqing