Recombinant Human MMP-8 / MMP8 Protein (Catalog#10254-H08H)
Preparation
This antibody was obtained from a rabbit immunized with purified, recombinant Human MMP-8 / MMP8 (rh MMP-8 / MMP8; Catalog#10254-H08H; NP_002415.1; Met1-Gly467), and then biotinylated.
Source
Monoclonal Rabbit IgG Clone #102
Purification
Protein A
Formulation
0.2 μm filtered solution in PBS
Conjugate
Biotin
Form
Liquid
Shipping
This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Storage
This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.
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.
References
Hasty K.A., et al. ,(1990), Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases. J. Biol. Chem. 265:11421-11424.
Blaeser J., et al. , (1991), Mercurial activation of human polymorphonuclear leucocyte procollagenase.Eur. J. Biochem. 202:1223-1230.
Blaeser J., et al. ,(1991), Mercurial activation of human polymorphonuclear leucocyte procollagenase. Eur. J. Biochem. 202:1223-1230.