AdipoGen Life Sciences

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

CHF 590.00
In stock
AG-40T-0103-C05050 µgCHF 590.00
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Product Details
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
Description

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.

Product References
  1. 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)
  2. Functional characterization of the Mycobacterium tuberculosis zinc metallopeptidase Zmp1 and identification of potential substrates: A. Petrera, et al.; J. Biol. Chem. 393, 631 (2012)
  3. Novel thiazolidinedione-hydroxamates as inhibitors of Mycobacterium tuberculosis virulence factor Zmp1: V. Slachtová, et al.; Eur. J. Med. Chem. 185, 111812 (2020)
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