PDAP1 Antibody
- Known as:
- PDAP1 Antibody
- Catalog number:
- XW-7944
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- PDAP1 Antibody
Related genes to: PDAP1 Antibody
- Gene:
- PDAP1 NIH gene
- Name:
- PDGFA associated protein 1
- Previous symbol:
- -
- Synonyms:
- PAP1, PAP, HASPP28
- Chromosome:
- 7q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-02-15
- Date modifiied:
- 2016-10-05
Related products to: PDAP1 Antibody
Related articles to: PDAP1 Antibody
- Hepatocellular carcinoma (HCC) exhibits aberrant lipid metabolism, notably increased de novo fatty acid synthesis and reduced fatty acid oxidation. PDAP1, a cancer-associated RNA-binding protein, is overexpressed in multiple malignancies, yet its specific contribution to fatty acid metabolic reprogramming and HCC progression remains undefined. - Source: PubMed
Publication date: 2026/03/14
Li JiazhengKong XiangxuSun HuaibinGuo XiuwenZhou HuaxinGuan ZhengyaoLu KangpingYin ZhaoqingLi YixinDu GangZhang HaoJin Bin - Platelet-derived growth factor associated protein 1 (PDAP1) is implicated in various biological processes, including tumorigenesis and the apoptosis of mature B lymphocytes. However, its functions in organismal development and homeostasis remain poorly understood. To address this gap, we generated Pdap1 knockout mice to elucidate the physiological functions of PDAP1 in vivo. Notably, our findings indicate that the absence of Pdap1 results in early embryonic lethality by embryonic day 11.5, accompanied by a spectrum of developmental abnormalities, including growth retardation, enlarged pericardium, hemorrhage within the pericardial cavity, and impaired vascularization of the yolk sac and placental labyrinth. Analysis of PDAP1 expression during embryogenesis revealed its presence in both embryonic and extra-embryonic tissues, a spatial pattern that may underlie the vascular defects observed in the yolk sac and placenta. Comparative proteomic profiling further identified nidogen-1 (NID1) as a key PDAP1-repressed target. Mechanistically, loss-of-function and gain-of-function experiments demonstrated that NID1, at least in part, mediates PDAP1-modulated endothelial cell migration, invasion, and tube formation-critical processes in vascular morphogenesis. - Source: PubMed
Yang TingWang Shi-JieChao Zhu-JunTian Ruo-FeiFu XinFan Xin-YuChen Zhi-NanLi LingCui Hong-Yong - Gliomas are the most aggressive primary malignancies of the central nervous system (CNS) and exhibit marked heterogeneity that is closely associated with metabolic reprogramming. Emerging evidence underscores the pivotal role of lactylation modifications in shaping the tumor microenvironment (TME) and facilitating glioma progression. This study aimed to systematically identify key lactylation-related genes (LRGs), elucidate their functional roles and associated pathways, and explore their potential as novel therapeutic targets using multi-omics data. - Source: PubMed
Wang ShundaTang FanChen HongPang JingyueZhang YingYang JianjingZhang Yue - Identifying factors affecting lifespan, including genes or proteins, enables effective interventions. We prioritized potential drug targets and provided insights into biological pathways for healthy longevity by integrating Mendelian randomization, cohort, and experimental studies. We identified causal effects of tissue-specific genetic transcripts and serum protein levels on three longevity outcomes: the parental lifespan, the top 1% and 10% extreme longevity, utilizing Mendelian randomization and multi-traits colocalization, combining the latest genetics data of gene expression (eQTLGen and GTEx) and proteomics (4746 proteins from five studies). We then evaluated associations of these potential genetic targets with mortality risk and life expectancy in the UK Biobank cohort. We performed in vitro cellular senescence experiments to confirm their effects. Fourteen plasma proteins and nine transcripts in whole blood had independent causal effects on longevity, where a cascading effect of both the tissue-specific transcripts and plasma proteins of LPA, PDAP1, DNAJA4, and TMEM106B showed negative effects on longevity. PDAP1 (PDGFA-associated protein 1) with the strongest genetic evidence might reduce lifespan by modifying sex hormones, adiposity, and epigenetic aging acceleration. In the prospective cohort, blood PDAP1 levels were significantly associated with higher all-cause mortality and more years of loss. In vitro, cellular senescence is accompanied by upregulation of PDAP1 expression. Exogenous PDAP1 stimulation accelerates cellular senescence while the deficiency of PDAP1 attenuates replicative senescence. This study facilitates the discovery of potential drug targets and provides a broader understanding of the biological processes of longevity, where PDAP1 emerged as a star for modifying human lifespan. - Source: PubMed
Publication date: 2025/04/10
Hou TianzhichaoSha ZimoWang QiZhu YuanyueZhu ZhengDai HuajieZhu YijieWang TiangeLi MianZhao ZhiyunXu YuLu JieliZheng JieYe JingWang WeiqingNing GuangBi YufangHu WeiguoXu Min - The overexpression and misfolding of viral proteins in the endoplasmic reticulum (ER) may cause cellular stress, thereby inducing a cytoprotective, proteostatic host response involving phosphorylation of eukaryotic translation initiation factor 2 subunit alpha (eIF2α). Here, we show that hepatitis A virus, a positive-strand RNA virus responsible for infectious hepatitis, adopts a stress-resistant, eIF2α-independent mechanism of translation to ensure the synthesis of viral proteins within the infected liver. Cap-independent translation directed by the hepatovirus internal ribosome entry site and productive hepatovirus infection of mice both require platelet-derived growth factor subunit A (PDGFA)-associated protein 1 (PDAP1), a small phosphoprotein of unknown function with eIF4E-binding activity. PDAP1 also interacts with eIF1A and is essential for translating stress-resistant host messenger RNAs that evade the proteostatic response to ER stress and that encode proteins promoting the survival of stressed cells. - Source: PubMed
Publication date: 2024/11/20
Shirasaki TakayoshiLenarcic ErikMisumi IchiroXie LingFusco William GYonish BryanDas AnshumanKim HyejeongCameron Craig ELéger-Abraham MélissaChen XianCullen John MWhitmire Jason KLi YouDuncan Joseph AMoorman Nathaniel JLemon Stanley M