PEX7 antibody Polyclonal Antibodies Primary antibodies
- Known as:
- PEX7 (anti-) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb36183
- Product Quantity:
- 5
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- PEX7 antibody Polyclonal Antibodies Primary antibodies
Related genes to: PEX7 antibody Polyclonal Antibodies Primary antibodies
- Gene:
- PEX7 NIH gene
- Name:
- peroxisomal biogenesis factor 7
- Previous symbol:
- -
- Synonyms:
- PTS2R, RD
- Chromosome:
- 6q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-05-22
- Date modifiied:
- 2016-10-05
Related products to: PEX7 antibody Polyclonal Antibodies Primary antibodies
Related articles to: PEX7 antibody Polyclonal Antibodies Primary antibodies
- Neurogenesis is characterized by dynamic structural changes and functional remodeling of multiple organelles, which interact to form an intricate network that precisely modulates processes including neural progenitor cell self-renewal, neurogenesis, and terminal neuronal development. However, the spatiotemporal dynamics of peroxisomes and their functional contributions within this regulatory network remain incompletely defined during mammalian cortical development. Here, we found that radial glial cells (RGCs) exhibit enriched peroxisome abundance, whereas neural differentiation is associated with reduced peroxisome numbers and increased pexophagy, accompanied by the remodeling of lipid metabolic programs. Acute disruption of peroxisomes by PLAAT3-PEX11 impaired neural differentiation in the embryonic mouse cortex, while knockout compromised neurogenic progression in human cortical organoids, supporting a conserved requirement for peroxisomal function during cortical development. Lipidomic and imaging analyses revealed that peroxisome-derived ether lipids were essential for driving neural differentiation and were specifically enriched in mitochondria. Consistently, knockdown of , which catalyzes the initial step of ether lipid biosynthesis, reduced neural differentiation, and disrupted mitochondrial structure and function, while batyl alcohol supplementation partially restored these defects. Mechanistically, the ether lipids maintain the structural integrity of mitochondrial cristae and thereby support respiratory chain activity, which in turn promotes oxidative phosphorylation and activates the NAD associated signaling. Collectively, this work highlights the precise spatiotemporal regulation of neurogenesis through peroxisomal dynamics and interorganelle crosstalk and identifies ether lipids as a potential therapeutic target for neurodevelopmental disorders. - Source: PubMed
Publication date: 2026/07/22
Li LinZou WenzhengLv YuqingLu YingfeiLiang JiaqiZhang ShukuiHu BaoyangJiao Jianwei - During infection, exists primarily as an intracellular pathogen of phagocytes, where it overcomes host defense mechanisms and replicates within the phagosome. This intracellular proliferation of yeasts requires the function of the fungal peroxisome for multiple, incompletely defined roles, with early pathogenesis functions dependent on the proper trafficking of peroxisomal matrix proteins carrying a type 1 peroxisome-targeting signal (PTS1). To better understand the potential roles of peroxisomes during infection, we identified the constituents of the peroxisomal proteome of pathogenic-phase yeasts through proximity labeling using a peroxisome-targeted TurboID biotin ligase. Comparative proteomics using peroxisome- or cytosol-localized TurboID identified 90 high-confidence peroxisomal proteins. To validate the peroxisomal proteome, a subset of nine putative peroxisomal proteins was localized to the peroxisome using fluorescent protein fusions. Comparison of peroxisomal proteomes for yeasts lacking the Pex5 or Pex7 cytosolic PTS1 or PTS2 receptors assigned proteins to either the PTS1- or PTS2-dependent peroxisomal import pathways, and refined the Histoplasma PTS1 tripeptide consensus sequence. The peroxisomal proteome of yeast during macrophage infection was ultimately determined to provide relevance to 's primary pathogenic niche. The identities of the proteins comprising the peroxisomal proteome include several enzymes for canonical peroxisome-localized biochemical pathways (e.g., fatty acid utilization and siderophore biosynthesis), but also represent several potential novel functions for the organelle. The defined peroxisomal proteome of pathogenic-phase yeasts, particularly the set of proteins imported via the PTS1 import pathway, thus establishes the important foundation for understanding how peroxisomes promote intracellular pathogenesis. - Source: PubMed
Publication date: 2026/06/09
Brechting Peter JRappleye Chad A - - Source: PubMed
Publication date: 2026/05/22
A RoshwanthVellingiri BalachandarPeer SameerWander Arvinder - Peroxisomes are single-membrane organelles present in most eukaryotic cells and play important roles in various biological activities. PEX5 and PEX7 are peroxisomal receptors that import matrix proteins containing peroxisomal targeting signals into the peroxisome. However, the specific contributions of CgPEX5 and CgPEX7 in the growth, nutritional utilization, conidial development, and pathogenicity of Colletotrichum gloeosporioides remain to be elucidated. Our results demonstrated that deletion of Cgpex5 or Cgpex7 severely inhibited vegetative growth of C. gloeosporioides. However, compared to the ΔCgpex7 strain, the ΔCgpex5 exhibited reduced capacity for carbon and nitrogen sources utilization, lower conidial production, aberrant conidial morphology and downregulated expression of CgBrlA, CgAbaA and CgWetA in C. gloeosporioides. Transcriptome analysis further indicated that Cgpex5 deletion triggered a reprogramming of crucial metabolic pathways, resulting in altered expression of multiple key metabolism-related genes. In addition, the ΔCgpex5 strain exhibited reduced penetration ability, induced smaller lesions on the host, and led to lower levels of host-derived reactive oxygen species (ROS) during infection compared to the ΔCgpex7 strain. Taken together, our results demonstrate that Cgpex5 gene is essential for growth, nutritional utilization, conidial development, and pathogenesis in C. gloeosporioides, whereas Cgpex7 plays a comparatively minor role. These findings indicated that Cgpex5-mediated peroxisomal import pathway represents a promising target for developing novel fungicidal strategies to control postharvest diseases. - Source: PubMed
Publication date: 2026/03/14
Han ZhanhongRen DandanZhu PinkuanGong DiZhang ZhengkePan Yonggui - Rhizomelic chondrodysplasia punctata type 1 (RCDP1) is a peroxisomal disorder characterized by skeletal shortening, intellectual disability, seizures, cataracts, and reduced lifespans. RCDP1 is caused by biallelic loss-of-function variants in , which encodes a protein required for importing select enzymes into the peroxisome matrix, including those essential for ether lipid synthesis (e.g., plasmalogens) and the branched-chain fatty acid catabolism. Plasmalogen deficiency is a hallmark of RCDP1 and other peroxisomal disorders, including RCDP types 2-5 (RCDP2-5) and Zellweger spectrum disorders (ZSD). Here, we performed comprehensive metabolomic profiling of clinical samples from RCDP patients and -deficient mouse models. We identified profound neurometabolic disturbances in the cerebral cortex and cerebellum of -deficient mice involving multiple lipid classes, including phosphatidylethanolamines (PEs), phosphatidylcholines (PCs), acylcarnitines, and sphingomyelins. Notably, many of these neurometabolic alterations were absent in patient and -deficient mouse plasma, indicating that plasma-based profiling can underrepresent the extent of CNS lipid remodeling. Overall, these findings reveal novel insights into neurometabolic adaptations to plasmalogen deficiency and suggest the potential involvement of additional pathways that may contribute to neurological dysfunction in RCDP. - Source: PubMed
Publication date: 2025/12/19
Sankhe RiyaWilliams Meredith IFallatah WedadMackay LauraBrown Mary LayneBhagwat PranjaliElsea Sarah HBraverman NancyWangler Michael F