TRP-1

TIMP1 is an extracellular inhibitor of MMPs (see above) including MMP1, 2, 3, 7, 8, 9, 10, 11, 12, 13, and 16. It belongs to the I35 (TIMP) family of irreversible protease inhibitors that function as key modulators of extracellular matrix degradation during tissue development and remodeling. TIMP1 can also act through an MMP-independent mechanism to promote erythropoiesis by stimulating proliferation and differentiation of erythroid progenitors. Recombinant human TIMP-1 is a 20.6 kDa protein containing 184 amino acid residues.

Tissue inhibitor of metalloproteinases, Fibroblast collagenase inhibitor, Erythroid-potentiating activity

7076

P01033

NP_003245

NM_003254

Xp11.3-p11.23

Human

Human

CTCVPPHPQT AFCNSDLVIR AKFVGTPEVN QTTLYQRYEI KMTKMYKGFQ ALGDAADIRF VYTPAMESVC GYFHRSHNRS EEFLIAGKLQ DGLLHITTCS FVAPWNSLSL AQRRGFTKTY TVGCEECTVF PCLSIPCKLQ SGTHCLWTDQ LLQGSEKGFQ SRHLACLPRE PGLCTWQSLR SQIA

< 0.1 ng/µg of protein (< 1EU/µg)

> 95% by SDS-PAGE & HPLC analyses

TIMP1 activity was measured by its ability to inhibit human MMP-1 induced hydrolysis of a chromogenic peptide substrate at room temperature. Half maximal inhibition was obtained at a TIMP-1 concentration of approximately 0.5 μg/ml, when using an MMP-1 concentration of 1.6 μg/ml.

184

Lyophilized

20.6 kDa

E. coli