Anaspec has announced the release of three new MMP recombinant proteins: MMP-1, MMP-9 and MMP-12.
These proteins, derived from the catalytic domain of the proteins, are supplied as activated proteins.
They can be used as positive controls for the Sensolyte 520 and 490 assays, for western blot, immunoprecipitation, Elisa or zymography.
Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases, capable of digesting extracellular matrix components.
1-2 MMP-1 (collagenase-1) is involved in tumour development, metastasis and rheumatoid arthritis.
3-5 MMP-1 is proposed as a therapeutic target for these diseases and digests a range of substrates, including a-1 antitrypsin, myelin basic protein, collagen I, II, III, VII, VIII, casein and gelatin.
3-5 MMP-9 (92-kDa gelatinase, collagenase-IV) is involved in a number of diseases, such as cancer, angiogenesis, alopecia and metastasis.
6-7 MMP-9 is secreted as zymogen with prodomain, gelatin-binding domain consisting of three contiguous fibronectin type II units, catalytic domain, proline-rich linker region and C-terminal hemopexin-like domain.
It can degrade a variety of substrates, including gelatin, collagens type IV, V, XIV, a2-macroglobulin, elastin, vitronectin and proteoglycans.
1,2,6,7 MMP-12 (macrophage elastase) is involved in smoke-induced emphysema, tumor and other diseases.
8-9 MMP-12 is secreted as a 54-kDa zymogen and becomes the mature 45-kDa active form after proteolytic cleavage.
MMP-12 has a range of substrates, including a-1 proteinase inhibitor, a-2 antiplasmin, plasminogen activator inhibitor-2, collagen IV, laminin, fibronectin and elastin, but not interstitial collagens.
