TIMP-1 Protein, Mouse (HEK293, His)

TIMP-1, a metalloproteinase inhibitor, exerts its regulatory function by forming one-to-one complexes with target metalloproteinases, such as collagenases, leading to the irreversible inactivation of these enzymes by binding to their catalytic zinc cofactor. This inhibitory action encompasses a spectrum of metalloproteinases, including MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13, and MMP16, with no observed effect on MMP14. Beyond its role as an enzyme inhibitor, TIMP-1 serves as a growth factor, influencing diverse cellular processes like differentiation, migration, and cell death. It activates signaling cascades through interactions with CD63 and ITGB1, implicating its involvement in integrin signaling. TIMP-1 also engages in protein-protein interactions with MMP1, MMP3, MMP10, and MMP13, demonstrating its regulatory influence on these metalloproteinases. Furthermore, it forms a complex with CD63 and ITGB1, indicating its participation in intricate cellular signaling networks.