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TIMP2 Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19. Interacts (via the C-terminal) with MMP2 (via the C- terminal PEX domain); the interaction inhibits the MMP2 activity. Down-regulated by TGFB1. Belongs to the protease inhibitor I35 (TIMP) family. Note: This description may include information from UniProtKB.
Protein type: Cell development/differentiation; Extracellular matrix; Inhibitor; Motility/polarity/chemotaxis; Secreted; Secreted, signal peptide
Chromosomal Location of Human Ortholog: 17q25.3
Cellular Component: extracellular matrix; extracellular region; extracellular space; proteinaceous extracellular matrix
Molecular Function: metalloendopeptidase inhibitor activity; protease binding; protein binding
Biological Process: extracellular matrix disassembly; negative regulation of membrane protein ectodomain proteolysis; neutrophil degranulation; response to cytokine stimulus; response to hormone stimulus
Reference #:  P16035 (UniProtKB)
Alt. Names/Synonyms: CSC-21K; metalloproteinase inhibitor 2; TIMP2; tissue inhibitor of metalloproteinase 2
Gene Symbols: TIMP2
Molecular weight: 24,399 Da
Basal Isoelectric point: 7.46  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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