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- サプライヤー
- TargteMol
- カタログNo.
- TMPY-02869
- 製品名称
- MMP-12 Protein, Human, Recombinant (catalytic domain)
- タンパク質名
- MMP-12
- Species
- Human
- HOST
- E. coli
- 20μg: -
- お問い合わせ
Overview
| Synonyms | HME, ME, MME, matrix metallopeptidase 12, MMP-12 |
|---|---|
| Characteristics | Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2. The specific activity is > 800 pmoles/min/?g. |
| Endotoxin Level | Please contact us for more information. |
| Purity | 90.60% |
| Description | Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. Macrophage Metalloelastase, also known as Matrix metalloproteinase-12, Macrophage elastase, MMP12, and MMP-12, is a secreted protein that belongs to the peptidase M1A family. MMP12 is a macrophage-secreted elastase that is highly induced in the liver and lung in response to S. mansoni eggs and contains four hemopexin-like domains. MMP12 is a proteolytic enzyme responsible for the cleavage of plasminogen to angiotensin, which has an angiostatic effect. It may be involved in tissue injury and remodeling and has significant elastolytic activity. It may be related to prognosis in breast cancer patients. MMP12 promotes fibrosis by limiting the expression of specific ECM-degrading MMPs. Like MMP12, MMP13 expression is highly dependent on IL-13 and type I I-IL-4 receptor signaling. MMP12 is a potent proinflammatory and oncogenic molecule. MMP12 up-regulation plays a critical role in emphysema to lung cancer transition that is facilitated by inflammation. |
| Reference | Ota T.,et al.,(2004), Complete sequencing and characterization of 21,243 full-length human cDNAs.Nat. Genet. 36:40-45.,Gronski T.J. Jr.,et al., (1997), Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase.J. Biol. Chem. 272:12189-12194.,Shapiro S.D.,et al.,(1993), Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. J. Biol. Chem. 268:23824-23829. |
| URL | https://www.targetmol.com/recombinant-protein/mmp12_protein_human_recombinant_catalytic_domain_ |
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