Home  >  Products  >  Matrix Metalloproteinase 9, Pro, Recombinant, Human (Matrix Metallopeptidase 9, MMP-9, MMP9, 92kD Gelatinase, 92kD Type IV Collagenase, CLG4B, Gelatinase B, GELB, MANDP2)

Matrix Metalloproteinase 9, Pro, Recombinant, Human (Matrix Metallopeptidase 9, MMP-9, MMP9, 92kD Gelatinase, 92kD Type IV Collagenase, CLG4B, Gelatinase B, GELB, MANDP2)

Cat no: M2425-40B


Supplier: United States Biological
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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 ELISA, Western Blot, Dot Blot, Immunohistohemistry, Immunoassays, Development of Rapid tests and other immunoassay. 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.
Catalogue number: M2425-40B
Applications: ELISA, Immunohistochemistry, Western Blot
Size: 10ug
Form: Supplied as liquid.
Purity: ~95% (SDS-PAGE)
References: 1. Pourmotabbed, T et al., Biochim Biophys Acta. 1204 (1):97-107(1994). 2. Romanic, AM. et al., Stroke 29 (5): 1020-1030 (1998).

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