Storage Buffer: PBS, pH 7.4(1%BSA and 0.1% Sodium azide)
Background:
The tissue inhibitors of metalloproteinases (TIMPs) are naturally occurring proteins that specifically inhibit matrix metalloproteinases and regulate extracellular matrix turnover and tissue remodeling by forming tightbinding inhibitory complexes with the MMPs. Thus, TIMPs maintain the balance between matrix destruction and formation. An imbalance between MMPs and the associated TIMPs may play a significant role in the invasive phenotype of malignant tumors. The TIMP proteins share several structural features including six loops held in place by six disulfide bonds arranged in three knot-like structures. These proteins also contain twelve cysteine residues in conserved regions of the molecule that form six disulfide bonds, essential for the formation of native conformations, and the N terminal region that is necessary for inhibitory activities. The N terminus of each TIMP contains a consensus sequence (VIRAK) and each TIMP is translated with a 29 amino acid leader sequence that is cleaved off to produce the mature protein. The C terminal regions are divergent, which enhances the selectivity of inhibition and binding efficiency.
Alternate Names:
Metalloproteinase inhibitor 4; TIMP 4; TIMP4; TIMP metallopeptidase inhibitor 4; TIMP-4; Timp4; TIMP4_HUMAN; Tissue inhibitor of metalloproteinase 4.