MMP12 Protein

MMP12 Protein Overview

MMP12 reagents

The matrix metalloproteases (MMPs) are a family of related matrix-degrading enzymes that are important in tissue remodeling and repair during development and inflammation. Abnormal expression is associated with various diseases such as tumor invasiveness, arthritis, and atherosclerosis. MMP activity may also be related to cigarette-induced pulmonary emphysema. Shapiro et al. (1993) cloned a cDNA for a metalloproteinase produced by human alveolar macrophages, which are known to have the capacity to degrade elastin (130160), by screening an alveolar macrophage cDNA library and a genomic library with the previously cloned mouse gene (Shapiro et al., 1992). The human gene, which they designated HME (human macrophage metalloelastase), produces a 1.8-kb transcript encoding a 470-amino acid protein that is 64% identical to the mouse protein. Both the mRNA and protein were detected in alveolar macrophages. As in the mouse, the predicted human 54-kD protein is processed by loss of both N- and C-terminal residues to a 22-kD mature form. The authors showed that recombinantly expressed HME was able to degrade insoluble elastin.

MMP12 protein family

Belongs to the peptidase M10A family.

MMP12 protein name

Recommended name
Macrophage metalloelastase
Short name
MME||ME||hME||MMP-12
Aliases
HME, macrophage elastase
Alternative name
Macrophage elastase Matrix metalloproteinase-12

MMP12 Protein Sequence

Species Human MMP12 protein
Length 470
Mass (Da) 54002
Sequence Human MMP12 protein sequence
Species Mouse MMP12 protein
Length 473
Mass (Da) 54971
Sequence Mouse MMP12 protein sequence
Species Rat MMP12 protein
Length 465
Mass (Da) 53738
Sequence Rat MMP12 protein sequence

MMP12 Protein Molecular Weight & PI

Macrophage metalloelastase precursor (EC 3.4.24.65) (MME) (Macrophage elastase) (ME) (hME) (Matrix metalloproteinase-12) (MMP-12) Homo sapiens (Human).

The parameters have been computed for the following feature

FT CHAIN 106-470 Macrophage metalloelastase.

Molecular weight (Da)

42123.57

Theoretical pI

8.57

MMP12 Protein Structure

Binary enzyme-product complexes of human MMP12
Deposited
2003-03-19   Released:  2003-08-05
Deposition Author(s)
Bertini, I., Calderone, V., Fragai, M., Luchinat, C., Mangani, S., Terni, B.
Organism(s)
Homo sapiens
Expression System
Escherichia coli
Experimental Data Snapshot
Method
X-RAY DIFFRACTION
Resolution
1.8500 Å
R-Value Free
0.244
R-Value Work
0.195
1OS9 From PDB

Human MMP12 protein Secondary structure

Recombinant MMP12 Protein Feature

MMP12 Protein, Human, Recombinant (catalytic domain)

High Purity
> 90 % as determined by SDS-PAGE
Low Endotoxin
Please contact us for more information.
High Activity
Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 (AnaSpec, Catalog # 27076). The specific activity is > 800 pmoles/min/µg.

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