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Human Promatrilysin (r-ProMMP-7) (GWB-18DEB8)



0.1 mg


Concentration: About 1.0 mg/mL Activity: >= 1.400 U/mg protein Human Promatrilysin is produced by DNA recombinant procedure in E. coli. Human Promatrilysin is refolded from the inclusion body. Its amino acid sequence is the same as the native one.

Function: Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.

Catalytic Activity: Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha-2(I) > alpha-1(I).

Cofactor: Binds 2 calcium ions per subunit.

Cofactor: Binds 2 zinc ions per subunit.

Subcellular Location: Secreted, extracellular space, extracellular matrix (Probable).

Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Similarity: Belongs to the peptidase M10A family [view classification].

Additional Information

Name Human Promatrilysin (r-ProMMP-7) (GWB-18DEB8)
Availability Discontinued
Related Product Names EC; Pump-1 protease; Uterine metalloproteinase; Matrix metalloproteinase-7; MMP-7; Matrin MPSL1; PUMP1Human Promatrilysin (r-ProMMP-7)MMP7
Swissprot ID P09237
NCBI Acc Number NP_002414.1
Molecular Weight 29677
Source E. coli
Format Clear solution
Reactivity Human
Storage -80 degree C for long-term storage
Datasheets/Manuals Printable datasheet for GWB-18DEB8
Intended Use Research Use Only