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AdipoGen Life Sciences
Zmp1 (M. tuberculosis) (rec.) (His)
Product Details | |
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Synonyms | Zinc Metalloprotease 1; Endopeptidase; Rv0198c |
Product Type | Protein |
Properties | |
Source/Host | E. coli |
Sequence |
Full-length Zmp1 (Mycobacterium tuberculosis) is fused at the N-terminus to a His-tag. |
Specificity |
Prefered cleavage sequence is PxxF. |
Biological Activity |
~0.5U/mg protein. Active towards the generic fluorogenic substrate for matrix metalloproteinases MMP2/MMP7 (Lit. 1). |
MW | ~73.9kDa |
Purity | ≥98% (SDS-PAGE) |
Endotoxin Content | N/A |
Concentration | 0.5-1mg/ml (Lot specific) |
Formulation | Liquid. In 10mM TRIS-HCl, pH 8.0. |
Other Product Data |
UniProt link O53649: Zmp1 (M. tuberculosis) |
Shipping and Handling | |
Shipping | DRY ICE |
Short Term Storage | -20°C |
Long Term Storage | -80°C |
Handling Advice |
After opening, prepare aliquots and store at -80°C. Avoid freeze/thaw cycles. |
Use/Stability | Stable for at least 6 months after receipt when stored at -80°C. |
Documents | |
MSDS | Download PDF |
Product Specification Sheet | |
Datasheet | Download PDF |
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-1β into IL-1β and the consequent phagosome maturation.
- Crystal Structure of Mycobacterium tuberculosis Zinc-dependent Metalloprotease-1 (Zmp1), a Metalloprotease Involved in Pathogenicity: D.M. Ferraris, et al.; J. Biol. Chem. 286, 32475 (2011)
- Functional characterization of the Mycobacterium tuberculosis zinc metallopeptidase Zmp1 and identification of potential substrates: A. Petrera, et al.; J. Biol. Chem. 393, 631 (2012)
- Novel thiazolidinedione-hydroxamates as inhibitors of Mycobacterium tuberculosis virulence factor Zmp1: V. Slachtová, et al.; Eur. J. Med. Chem. 185, 111812 (2020)