MMP-13 Protein, Human

The MMP-13 protein plays a role in the degradation of extracellular matrix proteins, especially fibrillar collagen, fibronectin, TNC, and ACAN. It cleaves triple-helical collagen, preferentially cleaves type II collagen, and can also target other collagen types. MMP-13 Protein, Human is the recombinant human-derived MMP-13 protein, expressed by E. coli , with tag free. The total length of MMP-13 Protein, Human is 172 a.a., .

MMP-13 (Matrix Metalloproteinase 13) emerges as a pivotal player in extracellular matrix modulation, wielding its influence over various proteins such as fibrillar collagen, fibronectin, TNC, and ACAN. It exhibits notable proficiency in cleaving triple helical collagens, particularly type I, type II, and type III, with the highest activity observed with soluble type II collagen. MMP-13's multifaceted role extends beyond matrix degradation; it may also act on key regulatory proteins, including TGFB1 and CCN2, thereby influencing processes such as wound healing, tissue remodeling, cartilage degradation, and bone development. Its indispensability in embryonic bone development and ossification underscores its significance, while its involvement in fracture healing through endochondral ossification highlights its dynamic contributions to physiological processes. Moreover, MMP-13 plays a role in keratinocyte migration during wound healing and is implicated in cell migration and tumor invasion, reflecting its diverse impact on cellular functions.

Human

E. coli

Tag Free

P45452 (E103-N274)

4322

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.