The WDFY3 Polyclonal Antibody (PAC013223) is a valuable tool for researchers studying WDFY3, a protein that plays a crucial role in various cellular processes. This antibody, produced in rabbits, exhibits high reactivity with human samples and has been validated for use in Western blot applications. By targeting the WDFY3 protein, this antibody enables precise detection and analysis in different cell types, making it an excellent choice for studies in cell biology and disease research.WDFY3, also known as WD repeat and FYVE domain-containing protein 3, is involved in diverse cellular functions such as autophagy, intracellular trafficking, and receptor signaling.
Its involvement in these processes highlights its importance in various physiological and pathological conditions, including cancer, neurodegenerative diseases, and immune disorders. By elucidating the role of WDFY3, researchers can gain valuable insights into these diseases and potentially identify novel therapeutic targets for intervention.
WD repeat and FYVE domain containing 3;WDFY3;ALFY;KIAA0993;MGC16461;ZFYVE25 ;
UniProt Protein Function:
WDFY3: 2 isoforms of the human protein are produced by alternative splicing.Protein type: Lipid-binding; Nuclear envelope; Membrane protein, peripheral; TransferaseChromosomal Location of Human Ortholog: 4q21.23Cellular Component: PML body; nuclear membrane; extrinsic to membrane; cytoplasm; autophagic vacuole; nuclear envelope; inclusion bodyMolecular Function: beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; protein binding; metal ion binding; phosphatidylinositol bindingBiological Process: endosome transport; positive regulation of macroautophagy
UniProt Protein Details:
NCBI Summary:
This gene encodes a phosphatidylinositol 3-phosphate-binding protein that functions as a master conductor for aggregate clearance by autophagy. This protein shuttles from the nuclear membrane to colocalize with aggregated proteins, where it complexes with other autophagic components to achieve macroautophagy-mediated clearance of these aggregated proteins. However, it is not necessary for starvation-induced macroautophagy. [provided by RefSeq, May 2010]
