Product nameNatural human MMP9 protein (dimer)
See all MMP9 proteins and peptides
Protein lengthFull length protein
DescriptionNatural human MMP9 protein
Amino Acid Sequence
Molecular weight220 kDa
Amino acids1 to 707
Additional sequence informationIsolated from stimulated human neutrophil granulocytes (buffy coat). Disulfide-bridged MMP-9 homodimer.
Our Abpromise guarantee covers the use of ab168863 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
≥1’500mU/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1µmol Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0.
Purity>95% by SDS-PAGE .
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Preservative: 0.05% Sodium azide
Constituents: 0.05% Brij, 0.06% Calcium chloride, 0.001% Zinc chloride, 0.79% Tris HCl, 1.17% Sodium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- 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 [EP1254] (ab76003) at 5 µg/ml
Lane 1 :
Natural human MMP9 protein (dimer) (ab168863)
Lane 2 :
Natural human MMP9 protein (Proenzyme, monomer) (ab157344)
Lane 3 :
Recombinant Mouse MMP9 protein (ab39309)
Lysates/proteins at 0.1 µg per lane.
Lanes 1-2 : Infrared labelled goat anti-rabbit (green) antibody at 1/20000 dilution
Lane 3 : Infrared labelled goat anti-rabbit (green) a at 1/20000 dilution
Performed under reducing conditions.
This product has been referenced in:
- Rydeen AB & Waxman JS Cyp26 Enzymes Facilitate Second Heart Field Progenitor Addition and Maintenance of Ventricular Integrity. PLoS Biol 14:e2000504 (2016). Read more (PubMed: 27893754) »
- Dabo AJ et al. Matrix Metalloproteinase 9 Exerts Antiviral Activity against Respiratory Syncytial Virus. PLoS One 10:e0135970 (2015). Read more (PubMed: 26284919) »