Key features and details
- Expression system: Escherichia coli
- Purity: >= 98% SDS-PAGE
- Endotoxin level: < 1.000 Eu/µg
- Active: Yes
- Suitable for: HPLC, SDS-PAGE
Product nameRecombinant human MMP2 protein (Active)
See all MMP2 proteins and peptides
MMP2 activity was measured by its ability to cleave a chromogenic peptide MMP2 substrate at room temperature.
At an MMP2 concentration of 2.5 µg/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes.
Purity>= 98 % SDS-PAGE.
>= 98% HPLC.
Endotoxin level< 1.000 Eu/µg
Expression systemEscherichia coli
Protein lengthFull length protein
SequenceMYNFFPRKPK WDKNQITYRI IGYTPDLDPE TVDDAFARAF QVWSDVTPLR FSRIHDGEAD IMINFGRWEH GDGYPFDGKD GLLAHAFAPG TGVGGDSHFD DDELWTLGEG QVVRVKYGNA DGEYCKFPFL FNGKEYNSCT DTGRSDGFLW CSTTYNFEKD GKYGFCPHEA LFTMGGNAEG QPCKFPFRFQ GTSYDSCTTE GRTDGYRWCG TTEDYDRDKK YGFCPETAMS TVGGNSEGAP CVFPFTFLGN KYESCTSAGR SDGKMWCATT ANYDDDRKWG FCPDQGYSLF LVAAHEFGHA MGLEHSQDPG ALMAPIYTYT KNFRLSQDDI KGIQELYGAS PDIDLGTGPT PTLGPVTPEI CKQDIVFDGI AQIRGEIFFF KDRFIWRTVT PRDKPMGPLL VATFWPELPE KIDAVYEAPQ EEKAVFFAGN EYWIYSASTL ERGYPKPLTS LGLPPDVQRV DAAFNWSKNK KTYIFAGDKF WRYNEVKKKM DPGFPKLIAD AWNAIPDNLD AVVDLQGGGH SYFFKGAYYL KLENQSLKSV KFGSIKSDWL GC
Predicted molecular weight62 kDa
Amino acids109 to 660
Additional sequence informationab81550 contains the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).
Our Abpromise guarantee covers the use of ab81550 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
ReconstitutionReconstitute in water to a concentration of 0.1 mg/ml. Please note that if you receive this product in liquid form, it has already been reconstituted as described and no further reconstitution is necessary.
- 72 kDa gelatinase
- 72kD type IV collagenase
- CLG 4
FunctionUbiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-
-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro.
PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.
Tissue specificityProduced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate.
Involvement in diseaseDefects in MMP2 are the cause of Torg-Winchester syndrome (TWS) [MIM:259600]; also known as multicentric osteolysis nodulosis and arthropathy (MONA). TWS is an autosomal recessive osteolysis syndrome. It is severe with generalized osteolysis and osteopenia. Subcutaneous nodules are usually absent. Torg-Winchester syndrome has been associated with a number of additional features including coarse face, corneal opacities, patches of thickened, hyperpigmented skin, hypertrichosis and gum hypertrophy. However, these features are not always present and have occasionally been observed in other osteolysis syndromes.
Sequence similaritiesBelongs to the peptidase M10A family.
Contains 3 fibronectin type-II domains.
Contains 4 hemopexin-like domains.
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.
modificationsPhosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro.
The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be facilitated by binding integrinv/beta3.
Cellular localizationSecreted > extracellular space > extracellular matrix. Membrane. Nucleus. Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab81550 has been referenced in 3 publications.
- Sarker H et al. Identification of fibrinogen as a natural inhibitor of MMP-2. Sci Rep 9:4340 (2019). PubMed: 30867536
- Del Ben M et al. Overexpression of the Vitronectin V10 Subunit in Patients with Nonalcoholic Steatohepatitis: Implications for Noninvasive Diagnosis of NASH. Int J Mol Sci 19:N/A (2018). PubMed: 29463024
- De Cunto G et al. Middermal Elastolysis: Dermal Fibroblasts Cooperate with Inflammatory Cells to the Elastolytic Disorder. Mediators Inflamm 2017:9524594 (2017). PubMed: 29097850