Recombinant Endoglycosidase H, expressed in E. coli and derived from Streptomyces plicatus, is widely used in biochemical research for the analysis and modification of glycoproteins. It specifically cleaves the chitobiose core of high mannose and some hybrid types of N-linked oligosaccharides from glycoproteins. This enzymatic activity is particularly valuable in the study of protein glycosylation patterns, aiding in the determination of the structure and function of glycoproteins. Researchers utilize it to deglycosylate proteins, which can simplify the analysis of protein structure by techniques such as mass spectrometry and gel electrophoresis. Additionally, Endoglycosidase H is employed in the production of therapeutic proteins, where controlling glycosylation is crucial for the efficacy and stability of biopharmaceuticals. Its ability to selectively remove certain sugar moieties without disrupting the protein backbone makes it a critical tool in both basic science and industrial applications.