Matrix metalloproteinases are a family of zinc- and calcium-dependant endopeptidases, which degrade extracellular matrix proteins. MMP-9 is secreted as a 92kD zymogen. Cleavage of pro-MMP-9 results in the active enzyme with a molecular weight of ~82kD. MMP-9 has a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells, and is involved in inflammatory responses, tissue remodelling, wound healing, tumor growth and metastasis.
Source:
Recombinant corresponding to aa20-707 from pro form of human Pro-MMP-9 minus the signal peptide, fused to 6x His-tag at N-terminal, expressed in E. coli.
Applications:
Suitable for use in Western Blot as a control. Other applications not tested.
Recommended Dilution:
Optimal dilutions to be determined by the researcher.
Storage and Stability:
May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.