Product nameRecombinant Mouse MMP9 protein
See all MMP9 proteins and peptides
Protein lengthFull length protein
Amino Acid Sequence
Our Abpromise guarantee covers the use of ab39309 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Mouse-MMP9 degrades denatured collagen (gelatin), and a range of extracellular matrix components in-vivo. Unlike MMP2, MMP9 is not constituitively produced by most normal cells, although the enzyme is often over expressed by transformed cells, tumor cells, and cells treated with the phorbol ester PMA. An endogenous inhibitor to MMP9, TIMP1, is often complexed with the enzyme in-vivo, but has been removed from this preparation.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Constituents: PBS, 50% Glycerol, 1.45% Sodium chloride
- 82 kDa matrix metalloproteinase-9
- 92 kDa gelatinase
- 92 kDa type IV collagenase
FunctionMay play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-
-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
Tissue specificityProduced by normal alveolar macrophages and granulocytes.
Involvement in diseaseIntervertebral disc disease
Metaphyseal anadysplasia 2
Sequence similaritiesBelongs to the peptidase M10A family.
Contains 3 fibronectin type-II domains.
Contains 4 hemopexin repeats.
DomainThe 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.
modificationsProcessing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.
N- and O-glycosylated.
Cellular localizationSecreted, extracellular space, extracellular matrix.
- Information by UniProt
All lanes : Anti-MMP9 antibody (ab38898) at 2 µg/ml
Lane 1 :
Natural human MMP9 protein (Proenzyme, monomer) (ab157344)
Lane 2 :
Recombinant Mouse MMP9 protein (ab39309)
Lysates/proteins at 0.1 µg per lane.
Performed under reducing conditions.
This blot was produced using a 4-12% Bis-Tris gel under the MOPS buffer system. The gel was run at 200V for 60 minutes before being transferred onto a nitrocellulose membrane at 30V for 70 minutes. The membrane was then blocked for an hour before being incubated with anti-MMP9 antibody (ab38898; 2 microgram per mL) overnight at 4°C. Antibody binding was detected using infrared labelled goat anti-rabbit (green) antibody (diluted 1:20000) for 1 hour at room temperature before imaging.
This product has been referenced in:
- Chiang HY et al. R1R2 peptide ameliorates pulmonary fibrosis in mice through fibrocyte migration and differentiation. PLoS One 12:e0185811 (2017). Read more (PubMed: 28968441) »
- Nighot P et al. Matrix metalloproteinase 9-induced increase in intestinal epithelial tight junction permeability contributes to the severity of experimental DSS colitis. Am J Physiol Gastrointest Liver Physiol 309:G988-97 (2015). Read more (PubMed: 26514773) »