TIMP-1 Protein, Human (HEK293)

TIMP-1, a metalloproteinase inhibitor, operates through the formation of one-to-one complexes with target metalloproteinases, including collagenases, leading to their irreversible inactivation by binding to the catalytic zinc cofactor. Its inhibitory spectrum encompasses MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13, and MMP16, excluding MMP14. Beyond its role as an enzyme inhibitor, TIMP-1 functions as a growth factor, orchestrating cell differentiation, migration, and cell death while activating intricate cellular signaling cascades through interactions with CD63 and ITGB1. This multifaceted protein also plays a crucial role in integrin signaling and, notably, mediates erythropoiesis in vitro, exhibiting species-specific stimulation of human and murine erythroid progenitors, distinct from IL3. Moreover, TIMP-1 engages in protein-protein interactions with MMP1, MMP3, MMP10, and MMP13, demonstrating its regulatory influence on these metalloproteinases. It forms a complex with CD63 and ITGB1, further emphasizing its involvement in complex cellular signaling networks.

TIMP-1 (12.5-400 ng/mL; 20 min) increases the the phosphorylation level of AKT and ERK1/2 in THP-1 monocytic cells. Moreover, TIMP-1 (100 ng/mL) also promotes the activation of serine/threonine kinases in THP-1 cells^[1].
TIMP-1 also can stimulates THP cells to mediate cell migration and CD74 internalization (50-200 ng/mL; 1 h), with an optimal concentration of 100 ng/mL^[1].