Recombinant Human Lysozyme protein (GST tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Lysozyme also known as muramidase is a protein with enzymatic activity that breaks down bacterial cell walls by hydrolyzing the glycosidic bonds of peptidoglycan. The molecular weight of lysozyme is approximately 14 kDa. This protein is expressed in various tissues and body fluids including egg whites human saliva tears and milk. Lysozyme acts as an antimicrobial agent and plays a significant role in the innate immune system.

Biological function summary

Lysozyme contributes to host defense by targeting bacteria. It is not part of a complex but functions as a single enzyme. By compromising the integrity of bacterial cell walls it clears pathogens swiftly from the body. Lysozyme activity assays measure its ability to hydrolyze bacterial peptidoglycan reflecting its role in immune defense. Many cells such as neutrophils and macrophages express lysozyme during the immune response aiding in pathogen clearance.

Pathways

Lysozyme is chiefly involved in the antibacterial humoral response pathway. Its action aligns with other antimicrobial proteins such as lactoferrin. Both lysozyme and lactoferrin are integral to the body’s first line of defense against bacterial invasion. In addition lysozyme is relevant in the pathway managing mucosal immunity working in conjunction with proteins that enhance pathogen clearance like defensins.

Lysozyme has links to conditions such as sarcoidosis and hereditary renal amyloidosis. In sarcoidosis altered expression patterns of lysozyme may serve as a marker for disease activity. In hereditary renal amyloidosis mutations in the lysozyme gene result in amyloid fibril formation leading to renal dysfunction. Understanding these connections helps in the diagnosis and treatment of related conditions.