Zmp1 (M. tuberculosis) (rec.) (His)

AdipoGen Life Sciences

Zmp1 (M. tuberculosis) (rec.) (His)

10

Research Use Only

M13 endopeptidases are single-pass, transmembrane zinc-metallopeptidases responsible in human for the regulation of the biological activity of many hormones and peptides and are involved in many important processes such as blood pressure regulation (Neprilysin or NEP1), cardiovascular development (Endothelin Converting Enzyme-1 or ECE-12), prevention of haemolytic reaction (KELL) and phosphate homeostasis (PHEX). Zmp1 is a soluble enzyme member of the M13 endopeptidases family that plays a key role in Mycobacterium tuberculosis pathogenicity with a still unknown mechanism. Recently, it was shown to suppress inflammasome activation by inhibiting caspase-1 activation, thus preventing processing of pro-IL-1beta into IL-1beta and the consequent phagosome maturation. - Protein. Full-length Zmp1 (Mycobacterium tuberculosis) is fused at the N-terminus to a His-tag. Source: E. coli. Endotoxin content: N/A. Liquid. In 10mM TRIS-HCl, pH 8.0. Prefered cleavage sequence is PxxF. Purity: >98% (SDS-PAGE). M13 endopeptidases are single-pass, transmembrane zinc-metallopeptidases responsible in human for the regulation of the biological activity of many hormones and peptides and are involved in many important processes such as blood pressure regulation (Neprilysin or NEP1), cardiovascular development (Endothelin Converting Enzyme-1 or ECE-12), prevention of haemolytic reaction (KELL) and phosphate homeostasis (PHEX). Zmp1 is a soluble enzyme member of the M13 endopeptidases family that plays a key role in Mycobacterium tuberculosis pathogenicity with a still unknown mechanism. Recently, it was shown to suppress inflammasome activation by inhibiting caspase-1 activation, thus preventing processing of pro-IL-1beta into IL-1beta and the consequent phagosome maturation.

-20°C,-80°C

41116133