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| | MMP9 ANTIBODY Chemical Properties |
| | MMP9 ANTIBODY Usage And Synthesis |
| Source | Rabbit | | Reactivity | Human | | Background | The matrix metalloproteinases are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors, and adhesion molecules. Among the family members, MMP-2, MMP-3, MMP-7, and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis. Research studies have shown that MMP activity correlates with cancer development. One mechanism of MMP regulation is transcriptional. Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full-length protein. | | References | [1] McCawley, L.J. and Matrisian, L.M. (2001) Curr Opin Cell Biol 13, 534-40.
[2] Coussens, L.M. et al. (2002) Science 295, 2387-92.
[3] Sternlicht, M.D. et al. (1999) Cell 98, 137-46.
[4] Vu, T.H. et al. (1998) Cell 93, 411-22.
[5] Nagase, H. et al. (1990) Biochemistry 29, 5783-9. |
| | MMP9 ANTIBODY Preparation Products And Raw materials |
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