| Product Name | TIMP1, 24-207aa, Human (Denatured) |
|---|---|
| Description | TIMP1 also known as metalloproteinase inhibitor 1. The matrix metalloproteinases are inhibited by specific endogenous tissue inhibitors of metalloproteinases (TIMPs), which comprise a family of four protease inhibitors: TIMP1, TIMP2, TIMP3 and TIMP4. Overall, all MMPs are inhibited by TIMPs once they are activated but the gelatinases (MMP-2 and MMP-9) can form complexes with TIMPs when the enzymes are in the latent form. The complex of latent MMP-2 (pro-MMP-2) with TIMP-2 serves to facilitate the activation of pro-MMP-2 at the cell surface by MT1-MMP (MMP-14), a membrane-anchored MMP. The role of the pro-MMP-9/TIMP-1 complex is still unknown. Recombinant human TIMP1, fused to His-tag at N-terminus, was expressed in E.coli. |
| Synonyms | Metalloproteinase inhibitor 1, EPA, EPO, HCI, CLGI, TIMP |
| Host | E. coli |
| Molecular Weight | 19.7kDa (184aa) confirmed by MALDI-TOF |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MCTCVPPHPQ TAFCNSDLVI RAKFVGTPEV NQTTLYQRYE IKMTKMYKGF QALGDAADIR FVYTPAMESV CGYFHRSHNR SEEFLIAGKL QDGLLHITTC SFVAPWNSLS LAQRRGFTKT YTVGCEECTV FPCLSIPCKL QSGTHCLWTD QLLQGSEKGF QSRHLACLPR EPGLCTWQSL RSQIA |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, Liquid, in Phosphate buffered saline (pH7.4) containing 30% glycerol, 1mM DTT, 1mM EDTA, 0.1mM PMSF |
| Concentration | 0.25mg/ml (determined by Bradford assay) |
| Purity | > 90% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Brew K., et al. (2000) Biochim Biophys Acta 1477 (1-2): 267-83. |
| Background | TIMP1 also known as metalloproteinase inhibitor 1. The matrix metalloproteinases are inhibited by specific endogenous tissue inhibitors of metalloproteinases (TIMPs), which comprise a family of four protease inhibitors: TIMP1, TIMP2, TIMP3 and TIMP4. Overall, all MMPs are inhibited by TIMPs once they are activated but the gelatinases (MMP-2 and MMP-9) can form complexes with TIMPs when the enzymes are in the latent form. The complex of latent MMP-2 (pro-MMP-2) with TIMP-2 serves to facilitate the activation of pro-MMP-2 at the cell surface by MT1-MMP (MMP-14), a membrane-anchored MMP. The role of the pro-MMP-9/TIMP-1 complex is still unknown. Recombinant human TIMP1, fused to His-tag at N-terminus, was expressed in E.coli. |
| Supplier | ARP |
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