Recombinant TIMP1 protein (His tag)

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Introducing the recombinant human Metalloproteinase inhibitor 1 (TIMP-1) fragment (residues 24-207), a high-purity protein designed to encompass the complete NTR functional domain. This product serves as an essential tool for researchers investigating metalloproteinase inhibition, cellular signaling, and erythroid differentiation, offering targeted insights into domain-specific mechanisms.

Metalloproteinase inhibitor 1 (TIMP-1) is a secreted protein that functions by forming irreversible complexes with catalytic zinc cofactors in metalloproteinases, effectively inactivating key enzymes such as MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13, and MMP16, though it does not act on MMP14. Beyond its role as a protease inhibitor, TIMP-1 acts as a growth factor, regulating cell differentiation, migration, and death through signaling pathways involving CD63 and ITGB1. It also plays a critical role in integrin signaling and exhibits species-specific erythropoietic activity, stimulating the growth and differentiation of human and murine erythroid progenitors. As a secreted protein, TIMP-1 operates extracellularly, influencing tissue remodeling and cellular communication in various physiological and pathological contexts.