Anti-Neutrophil Elastase/ELANE Antibody Picoband® Fluoro594 Conjugated

Neutrophil elastase is a serine protease of neutrophil and monocyte granules. Its key physiologic role is in innate host defense, but it can also participate in tissue remodeling and possesses secretagogue actions important to local inflammatory responses. Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode structurally similar proteins. The encoded preproprotein is proteolytically processed to generate the active protease. Following activation, this protease hydrolyzes proteins within specialized neutrophil lysosomes, called azurophil granules, as well as proteins of the extracellular matrix. This protein also degrades the outer membrane protein A (OmpA) of E. coli as well as the virulence factors of such bacteria as Shigella, Salmonella and Yersinia. Mutations in this gene are associated with cyclic neutropenia and severe congenital neutropenia (SCN) . This gene is present in a gene cluster on chromosome 19.

E. coli-derived mouse Elastase/ELANE/ELA2 recombinant protein (Position: S27-N265) . Mouse Elastase/ELANE/ELA2 shares 92% amino acid (aa) sequence identity with rat Elastase/ELANE/ELA2.

Calcium Signaling, Cancer, Complement, Cytoskeleton/ECM, Defensin, ECM Enzymes, ECM Proteins, Extracellular Matrix, Human Protein, Immunology, Innate Immunity, Invasion/Microenvironment, Macrophage/Inflammation, Microbiology, NK Cells, Protein, Signal Transduction, Signaling Pathway

Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity) . .

1. Ancliff, P. J., Gale, R. E., Liesner, R., Hann, I. M., Linch, D. C.Mutations in the ELA2 gene encoding neutrophil elastase are present in most patients with sporadic severe congenital neutropenia but only in some patients with the familial form of the disease. Blood 98: 2645-2650, 2001. 2. Bristow, C. L., Fiscus, S. A., Flood, P. M., Arnold, R. R. Inhibition of HIV-1 by modification of a host membrane protease. Int. Immun. 7: 239-249, 1995.