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Catalog Number | orb1958262 |
---|---|
Category | Small Molecules |
Description | MMP-8 Protein, Human, Recombinant (His) |
Purity | 98.00% |
MW | Approxiamtely 52.6 kDa |
Biological Activity | 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. |
Note | For research use only |
Expiration Date | 12 months from date of receipt. |
Unconjugated | |
The purity of the protein is greater than 85% as determined by SDS-PAGE and Coomassie blue staining. | |
The protein has a predicted molecular mass of 52.0 kDa after removal of the signal peptide. The apparent molecular mass of MMP8-His is approximately 55-70 kDa due to glycosylation. | |
Mammalian |
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