MMP-14 Protein, Human (C-His)

MMP-14 protein is an endopeptidase that degrades collagen and activates progelatinase A.

MMP-14 Protein serves as a critical endopeptidase, targeting various components of the extracellular matrix, notably collagen, and playing a pivotal role in pericellular collagenolysis during development, contributing to the modeling of both skeletal and extraskeletal connective tissues. Additionally, MMP-14 activates progelatinase A, acting as a key player in the intricate regulation of the extracellular matrix. Beyond its matrix-degrading functions, MMP-14 is implicated in actin cytoskeleton reorganization by cleaving PTK7, highlighting its involvement in cellular processes beyond matrix remodeling. Furthermore, MMP-14 acts as a positive regulator of cell growth and migration through the activation of MMP15 and plays a crucial role in the formation of fibrovascular tissues in conjunction with pro-MMP2. Notably, MMP-14 cleaves ADGRB1, releasing vasculostatin-40, which exerts anti-angiogenic effects by inhibiting angiogenesis. This multifaceted functionality underscores MMP-14's significance in orchestrating diverse cellular processes and its potential as a therapeutic target in various physiological contexts.

Human

E. coli

C-10*His

P50281 (A21-G284)

4323

Partial

Approximately 31 kDa, based on SDS-PAGE under reducing conditions.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.