Rab5a, 1_215aa, Human, Recombinant, E.coli
- Known as:
- Rab5a, 1_215aa, Human, Recombinant, E.coli
- Catalog number:
- RAB0701
- Product Quantity:
- 0.5mg
- Category:
- -
- Supplier:
- ATGen
- Gene target:
- Rab5a 1_215aa Human Recombinant .coli
Related genes to: Rab5a, 1_215aa, Human, Recombinant, E.coli
- Gene:
- FCN2 NIH gene
- Name:
- ficolin 2
- Previous symbol:
- -
- Synonyms:
- P35, FCNL, EBP-37, ficolin-2
- Chromosome:
- 9q34.3
- Locus Type:
- gene with protein product
- Date approved:
- 1996-07-11
- Date modifiied:
- 2016-10-05
- Gene:
- RAB5A NIH gene
- Name:
- RAB5A, member RAS oncogene family
- Previous symbol:
- RAB5
- Synonyms:
- -
- Chromosome:
- 3p24.3
- Locus Type:
- gene with protein product
- Date approved:
- 1990-01-22
- Date modifiied:
- 2015-06-29
Related products to: Rab5a, 1_215aa, Human, Recombinant, E.coli
Related articles to: Rab5a, 1_215aa, Human, Recombinant, E.coli
- Ovarian granulosa cells (GCs) play a crucial role in follicle development and hormone production. These functions require substantial energy, supported by mitochondrial activity and balanced lipid metabolism. RAB5 is known to maintain mitochondrial homeostasis; however, its role in regulating lipid metabolism via the energy-sensing AMP-activated protein kinase (AMPK) pathway remains unclear. In polycystic ovary syndrome (PCOS), a disorder often linked to metabolic and mitochondrial defects in GCs, RAB5A levels are significantly reduced in obese subtypes. In this study, we demonstrate that RAB5A deficiency disrupts lipid metabolism and impairs normal cell proliferation, characterized by increased mitochondrial stress (increased reactive oxygen species) and activation of mitophagy via AMPK. RAB5A may coordinate with MIGA2, a protein involved in regulating mitochondria-lipid droplet interactions, to modulate lipid metabolism via AMPK activity. Notably, activating AMPK with AICAR reverses the adverse effects of RAB5A loss. Collectively, these findings identify RAB5A as a key regulator of GC function and a potential therapeutic target in obese PCOS. - Source: PubMed
Publication date: 2026/04/29
Liu Shao-HongYang PingZhu Bing-HongLi Hong-YuWang ShanWang YongLiu Xiao-Man - Diabetic kidney disease (DKD) is a common condition with few treatment options, and inflammation plays a pivotal role in its progression. Luteolin, a natural compound found in traditional Chinese herbs, is known for its anti-inflammatory properties, making it a potential treatment for DKD. But its effect and mechanisms in DKD remain incompletely elucidated. - Source: PubMed
Publication date: 2026/04/24
Deng LingchenWang YongShi ChunruWu JieYao JinShen WanjunZhang ZiyueLiu RanWang XuZhu HanyuZhang LiCai GuangyanZhou JianhuiHong QuanChen Xiangmei - TBC (Tre2/Bub2/Cdc16) domain-containing proteins constitute the widespread family of GTPase-activating proteins (GAPs). They interact with the Rab superfamily of small GTPases, stimulate GTP hydrolysis, and regulate vesicle trafficking. TBC1D17, involved in Shiga toxin trafficking, autophagy and glucose metabolism regulation, constitutes an example of GAP interacting with Rabs. Here we present the first crystal structures of the murine and human TBC domains of TBC1D17 proteins determined at 2.20 and 3.34 Å resolution, respectively. The TBC domain in both structures represents a heart-like shape. Our analyses revealed dimerization of the TBC domain through a fragment located near residues participating in GTP hydrolysis, a result we observed also in structures of closely related homologs. Furthermore, we tested Rab5a interactions with various fragments of TBC1D17. Interestingly, this protein contains an annotated, yet uncharacterized, Rab-binding domain (RBD) and our studies revealed strong interactions of Rab5a with TBC1D17 fragments containing RBD, while interactions with the TBC domain alone are much weaker. These results provide the first direct evidence for the critical role of the TBC1D17 RBD in interactions with Rab5a. - Source: PubMed
Nielipińska DominikaOrlikowska MartaNielipiński MaciejSekuła BartoszBłażewska Katarzyna MGendaszewska-Darmach EdytaPietrzyk-Brzezińska Agnieszka J - Seed storage proteins (SSPs) are stored in protein storage vacuoles (PSVs) within plant endosperm cells. In rice, glutelins undergo post-Golgi trafficking via dense vesicles (DVs) to protein body II (PBII). Phosphatidylinositol 3-phosphate (PI3P) regulates endosomal, autophagic, and vacuolar trafficking, yet its role in glutelin transport remains unclear. Here, we characterized the glutelin precursor accumulation14 (gpa14) mutant, which exhibits over-accumulation of 57-kDa glutelin precursors and floury, shrunken endosperm. Map-based cloning identified a single adenine insertion in Vacuolar Protein Sorting 34 (OsVPS34), resulting in a putative truncated protein lacking the PI3Ka and PI3_PI4_kinase domains. OsVPS34 encodes phosphatidylinositol 3-kinase (PI3K), which interacts with other subunits of the PI3K complex to regulate the production of PI3P. PI3P was enriched in the trans-Golgi network (TGN) and pre-vacuolar compartment (PVC), co-localized with Rab5a and GPA5, and was detected in DVs and PBIIs. In gpa14, PI3P levels were reduced, leading to mis-localization and decreased membrane association of Rab5a and GPA5, key regulators of glutelin trafficking. Our findings demonstrate that OsVPS34 is essential for synthesis of PI3P, which plays a crucial role in recruiting GPA5 and Rab5a to DVs for glutelin post-Golgi trafficking in rice endosperm. - Source: PubMed
Publication date: 2026/03/18
Xu ShanbinMa MingqingZhao HuanhuanZhou AoniLi ZiLi BoHe YuzheZhang GuipingCai HongpingGu ChuanweiYu TingYang XueZhou LeiZhang YuDuan ErchaoTeng XuanLiu XiLiu ShijiaTian YunluJiang LingRen YulongWang YihuaDong HuiWan Jianmin - Endosomes are nanoscale intracellular compartments that sort and recycle cell-surface receptors such as epidermal growth factor receptor-1 (EGFR1). Nanometer-scale interactions and coclustering of signaling proteins, cargo, and the membrane are critical to this process, yet direct 3D visualization has been hindered by the limited resolution of conventional and super-resolution microscopies. Here, we adapt expansion microscopy (ExM) to visualize and quantify nanoclusters of endosomal proteins in human retinal pigment epithelial (RPE-1) cells. We developed a 3D distortion analysis leveraging the Farneback optical-flow principle to detect anisotropies in hydrogel expansion, revealing under-expansion of cytoplasmic regions within ExM hydrogels and overestimation of size and distance measurements of small compartments such as endosomes. To calibrate ExM images of cytoplasmic regions containing endosomes, we introduced a self-assembling protein nanocage that reports the true local nanoscale expansion factor. To stimulate and visualize EGFR1 internalization and sorting, we applied a pulse-chase protocol with fluorescently tagged epidermal growth factor (EGF), fixed cells at 15 and 30 min, and subjected samples to 10-fold ExM and multiplexed 3D Airyscan microscopy to map cargo and EGFR1 relative to other endosomal proteins. A volume tracing pipeline was developed to visualize the changes in the labeled EGF and EGFR1 densities at the limiting membrane of the endosomes. These changes included enrichment of EGF and EGFR1 in the endosomal interior and accumulation of Rab5a near the limiting membrane during early endosome maturation. Together, this multiplexed 3D ExM toolkit provides a quantitative framework for visualizing and measuring small subcellular organelles at true molecular-scale resolution. - Source: PubMed
Publication date: 2026/03/16
Shakespeare TaylaSeehra Rajpinder SFlores Rodriguez NeftaliAtuanya NkolikaSheard Thomas M DKöhler RalfBose DanielWunderley LydiaWoodman PhilipCiani BarbaraJayasinghe Izzy