• Name
  • Description
  • Cat#
  • Pricings
  • Quantity

About TIMP / Tissue Inhibitor of Metalloprotease:

TIMP, or tissue inhibitor of metalloproteinase, is a family of protease inhibitors, which regulate matrix metalloproteinases or MMPs.
There are four TIMPs, known as: TIMP-1, TIMP-2, TIMP-3, TIMP-4.

TIMP Function
TIMPS are specific protease inhibitors, which regulate and control MMPs. MMPs are zinc-dependent endopeptidases, which play an instrumental role in extracellular matrix degradation and subsequently impact multiple processes, including: Tissue repair, Cirrhosis, Wound healing, Tumour invasion and metastasis, Morphogenesis, angiogenesis.
TIMPs play a crucial role in maintaining good health, and an imbalance between TIMPs and MMPs has been linked to a host of medical issues, including: Rheumatoid and osteoarthritis, Cardiovascular disease and degradation of the aortic wall, Cancer metastasis and Endometriosis.
In addition to their inhibiting role, TIMPs can also promote cell development across a broad spectrum of cell types, and studies suggest that TIMP-1 can have anti-apoptotic effects. Apoptosis is a molecular process, which contributes to the death of cancerous cells.

Tissue Inhibitor of Metalloprotease Mechanism
The TIMP family, which comprises four members, contains three secreted proteins, TIMP-1, TIMP-2 and TIMP-4, and one membrane-bound protein, TIMP-4. TIMPs bind with MMPs, prohibiting access to the catalytic domain. As TIMP-3 is a membrane-bound protein, it can only target the extracellular matrix. TIMPs can be expressed from several different tissues, and expression is controlled by hormones and cytokines. In healthy individuals, the expression of MMPs should be minimal.

TIMP Structure
TIMPs in human beings have two key domains: an N-terminal and a C-terminal. The N-terminal comprises up to 125 amino acids, while the C-terminal comprises around 65 residues. The four TIMP family members are approximately 40% identical in sequence to each other. TIMP-2 and TIMP-4 are the most similar, sharing around 50% of the same structure.