Description
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. Neutrophil collagenase, also known as Matrix metalloproteinase-8, MMP-8, and CLG1, is a member of the peptidase M1A family. MMP-8 may affect the metastatic behavior of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 in the tumor may have a protective effect against lymph node metastasis. MMP-8 may affect the metastatic behavior of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 participates in wound repair by contributing to the resolution of inflammation and open the possibility to develop new strategies for treating wound healing defects.
Form
Lyophilized from sterile 50mM Tris, 10mM CaCl2, 150mM NaCl, pH 7.5, 5 % trehalose, 5% mannitol and 0.01% Tween80.
Molecular Mass
The recombinant human MMP8 consists of 458 amino acids after removal of the signal peptide and has a predicted molecular mass of 52.6 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhMMP8 is approximately 65-75 kDa due to glycosylation.
