| Description | Myelin basic protein, MBP (68-86) is the portion of the 68th to 86th amino acid residues in the MBP protein sequence. Myelin basic protein, MBP (68-86) can act as an autoantigen, triggering the immune system to attack its own myelin. Myelin basic protein, MBP (68-86) is used as one of the immunogensMyelin basic protein, MBP (68-86) is the portion of the 68th to 86th amino acid residues in the MBP protein sequence. Myelin basic protein, MBP (68-86) can act as an autoantigen, triggering the immune system to attack its own myelin. Myelin basic protein, MBP (68-86) is used as one of the immunogens in the experimental autoimmune encephalomyelitis (EAE) animal model to study immune responses associated with multiple sclerosis (MS)[1]... Read More | β-CGRP, human (Human β-CGRP) is one of calcitonin peptides, acts via the complex of calcitonin-receptor-like receptor (CRLR) and receptor-activity-modifying protein (RAMP), with IC50s of 1 nM and 300 nM for CRLR/RAMP1 and CRLR/RAMP2 in cells[1] | Beta-glucuronidase is an important lysosomal enzyme involved in the degradation of glucuronate-containing glycosaminoglycan[1] | Lysozyme (Muramidase) is a conserved antimicrobial protein. Lysozyme exerts its bactericidal effect by hydrolyzing bacterial cell wall peptidoglycan (PG). Lysozyme plays an important role in limiting bacterial growth on mucosal surfaces and other sites, not only controlling potential pathogens but Lysozyme (Muramidase) is a conserved antimicrobial protein. Lysozyme exerts its bactericidal effect by hydrolyzing bacterial cell wall peptidoglycan (PG). Lysozyme plays an important role in limiting bacterial growth on mucosal surfaces and other sites, not only controlling potential pathogens but also limiting overgrowth of microbiota to prevent dysbiosis. Extracellular lysozyme can also degrade polymeric PG into soluble fragments, activate NOD receptors in mucosal epithelial cells, and lead to the secretion of chemokines and activating factors by neutrophils and macrophages[1][2]... Read More | Pyruvate Kinase, Microorganism (PK) is a glycolytic enzyme that catalyzes the conversion of phosphoenolpyruvate and ADP to pyruvate and ATP[1] |