| 特异性 | 不与大鼠ApoAI,BMP1,BMP2,BMP3,BMP4,BMP7,CRP,HGF,HSP27,IL-1α,IL-1RI,IL-1β,IL1RA,IL-2,IL-4,IL-5,IL-6,IL-10,IL-12,IL-13,IL-15,IL-17C,IL-21,IL-23,IFN ,MMP-2,sIL-2R,sIL-6R,PDGF,PLA2G7,prolactin,TGFβ1,TGFβ2,TGFβ3,TLR1,TLR2,TLR3等反应。 |
| 背景说明 | As the first member of membrane type (MT) MMPs, MMP-14, also known as MT1-MMP, plays an important role in extracellular matrix (ECM) remodeling by being able to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules such as CD44 and integrin alpha V. MMP-14 is therefore a key enzyme in many physiological and pathological processes such as angiogenesis and tumor invasion. Structurally, MMP-14 consists of the following domains: a pro domain containing the furin cleavage site, a catalytic domain containing the zinc-binding site, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplamasic tail. Recombinant Human MMP-14 consists of the pro and catalytic domains, which can be activated by treatment with furin as described in the Activity Assay Protocol. |