商品编号


AG-40T-0103-C050



品牌


Adipogen



公司


Adipogen



公司分类


Proteins



Size

50 ?g


商品信息


More Information



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.



BIOLOG
ical 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

0.5mg/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/St
ABI
lity

Stable for at least 6 months after receipt when stored at -80°C.



Documents



MSD
S


Download PDF



Product Specification Sheet



Datasheet


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M13 endopeptidases are single-pass, transmembrane zinc-metallopeptidases respons
IBL
e in human for the regulation of the
BIOLOG
ical 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

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)