TIMP-4, Recombinant, Mouse, aa1-224 (Tissue Inhibitors of Metalloproteinases)

Tissue inhibitors of metalloproteinases (TIMPs) are a family of secreted proteins that regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases (MMPs). There are four known members of the family, TIMP-1, -2, -3, and -4. TIMP-4 is produced by a wide range of tissues, particularly brain, heart, ovary and skeletal muscle (1, 2). Limited studies have shown that TIMP-4 has a tumor suppressive effect against WilmпїЅs tumor, exhibits negative correlation with glioma maligancy and is found in breast carcinoma cells (3, 5). TIMP-4 inhibits MMP-mediated proteolysis by forming a noncovalent binary complex with the MMP active site through its N-terminal domain. In addition, it binds to the hemopexin-like domain of proMMP-2 through its C-terminal domain in a manner similar to TIMP-2 (6). However, unlike TIMP-2, TIMP-4 does not promote proMMP-2 activation by MT1-MMP (MMP-14) (7). Although TIMP-4 is a potent inhibitor of most MMPs, it is not an effective inhibitor of ADAMs, such as TACE (8, 9).\n\nSource:\nRecombinant protein corresponding to aa1-224 from mouse TIMP-4, NS0-derived.\n\nMolecular Weight: \n~25-26kD\n\nEndotoxin:\n<0.10EU/1ug (LAL method).\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

145843

Size

10ug

Form

Supplied as a liquid in Tris, NaCl.

Purity

~95% (SDS-PAGE)

References

1. Greene et al. (1996) J. Biol. Chem. 271:30375. 2. Leco et al. (1997) FEBS Lett. 401:213. 3. Geliker et al. (2001) Oncogene 20:4337. 4. Hernandez-Barrantes et al. (2001) Biochem. Biophys. Res. Comm. 281:126. 5. Amour et al. (1998) FEBS Lett. 435:39. 6. Groft et al.(2001) Br. J. Cancer 85:55. 7. Hurst et al. (2001) Biochem. Biophys. Res. Comm. 281:166. 8. Bigg et al. (1997) J. Biol. Chem. 272:15496.