TIMP-1 Protein, Human (HEK293, Fc)

The TIMP-1 protein forms a one-to-one complex with the target metalloprotease, irreversibly inactivating it by binding to the catalytic zinc cofactor. It inhibits multiple MMPs, activates cell signaling through CD63 and ITGB1, and interacts with MMP1, MMP3, MMP10, and MMP13. TIMP-1 Protein, Human (HEK293, Fc) is the recombinant human-derived TIMP-1 protein, expressed by HEK293 , with N-hFc labeled tag. The total length of TIMP-1 Protein, Human (HEK293, Fc) is 184 a.a., with molecular weight of ~49.1 kDa.

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.

Human

HEK293

N-hFc

P01033 (C24-A207)

7076  [NCBI]

Approximately 49.1 kDa

Greater than 85% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.