Anti-Human VPS8 Antibody Pair

Product Description: VPS8 subunit of CORVET complex (VPS8) is a key subunit of the CORVET (class C core vacuole/endosome tethering) complex, which functions as a membrane tethering factor in the endolysosomal system, specifically at early and late endosomes. Structurally, VPS8 features an elbow-shaped configuration with long C-terminal alpha-helices and RING finger domains that anchor it firmly to the CORVET core, interacting primarily with Vps18 and Vps11 subunits. This anchoring not only stabilizes the complex but also facilitates the attachment of the SNARE-binding module, enhancing membrane fusion processes. VPS8 acts as an effector for Rab5 homologs, such as Vps21, mediating endosomal membrane clustering and tethering essential for vesicle trafficking and fusion. Functionally, VPS8's interactions regulate endosome maturation and trafficking pathways critical for cellular homeostasis. Disruptions in CORVET function, including VPS8 mutations or misregulation, could impair endosomal trafficking and contribute to neurodegenerative diseases and disorders involving lysosomal dysfunction, given the complex's central role in endolysosomal membrane dynamics and intracellular transport. Protein Function: Plays a role in vesicle-mediated protein trafficking of the endocytic membrane transport pathway. Believed to act as a component of the putative CORVET endosomal tethering complexes which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (PubMed:25266290). Functions predominantly in APPL1-containing endosomes (PubMed:25266290) [The Uniprot Consortium]