Recombinant Human Chid1 protein

ChID1 (Chitinase Domain-Containing Protein 1) is a conserved eukaryotic protein belonging to the glycosyl hydrolase family 18 (GH18), characterized by a chitinase-like structural domain. Despite lacking classical chitinase enzymatic activity due to mutations in catalytic residues, ChID1 retains a chitin-binding domain, suggesting potential roles in carbohydrate recognition or interactions with chitin-like glycans. First identified in *Drosophila* as a regulator of developmental signaling pathways, ChID1 homologs exist across species, including mammals (human CHID1), plants, and fungi. Its evolutionary conservation implies fundamental biological significance.

In mammals, CHID1 is ubiquitously expressed, localized to the cytoplasm and extracellular vesicles. Studies link it to immune modulation, autophagy, and lipid metabolism. For instance, CHID1 binds to glycosaminoglycans and interacts with proteins involved in vesicular trafficking, hinting at a role in cellular homeostasis or interorganelle communication. It is also implicated in inflammatory responses, with altered expression observed in autoimmune diseases and cancer. However, its precise molecular mechanisms remain unclear, making it a subject of ongoing research.

Recombinant ChID1 proteins are engineered for functional studies. Produced via heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells), these proteins retain the conserved GH18 domain, enabling structural analysis and ligand-binding assays. Tagged versions (e.g., His-tag or GFP-fusion) facilitate purification and localization tracking. Applications include elucidating ChID1’s role in disease models, screening for binding partners, and exploring therapeutic potential in disorders involving glycosylation defects or immune dysregulation. Current challenges include resolving its substrate specificity and reconciling conflicting data from different experimental models.