ANXA7 Antibody
- Known as:
- ANXA7 Antibody
- Catalog number:
- XW-7989
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- ANXA7 Antibody
Related genes to: ANXA7 Antibody
- 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
Related articles to: ANXA7 Antibody
- 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 - Ischemic stroke causes acute brain calcium phosphate (CaP) deposition, a process involving primarily the injured neurons. Whereas the adverse impact of CaP deposition on the brain structure and function has been recognized, the underlying mechanisms remain poorly understood. This investigation demonstrated that the neuron-expressed, plasma membrane-associated Ca2+-binding proteins annexin (Anx) A2, AnxA5, AnxA6, and AnxA7 contributed to neuronal CaP deposition in the mouse model of ischemic stroke. These Anxs were released from the degraded plasma membrane of the ischemic neurons and were able to form Anx/CaP complexes, a nanostructure capable of binding to the β actin filaments via Anx-actin interaction to cause neuronal CaP deposition prior to brain infarction. Anx administration to the healthy mouse brain caused brain CaP deposition and infarction. Monomeric β actin was able to block competitively Anx binding to β actin filaments and prevent ischemic stroke- and Anx administration-induced brain CaP deposition and infarction. Administration of siRNAs specific to the four Anx mRNAs alleviated brain CaP deposition and infarction. These observations support the role of Anxs in CaP formation and deposition in ischemic neurons. - Source: PubMed
Publication date: 2025/01/16
Liu Shu QTroy John BGoldman JeremyGuillory Roger J