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

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

Cat no: M2425-02R


Supplier: United States Biological
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Matrix metalloproteinases are a family of zinc and calcium-dependent 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. Recombinant protein corresponding to aa113-450 at the catalytic domain of human MMP-9, fused to a N-terminal, 6x His-tag, expressed in E. coli. Applications: Suitable for use a control in Western Blot. Other applications not tested. Recommended Dilutions: 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. Aliquots are stable for 6 months 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: M2425-02R
Applications: Western Blot
Size: 10ug
Form: Supplied as a liquid in 25mM Tris-HCl, pH 6.8, 50mM DTT, 1% SDS, 0.1% Bromophenol Blue, 2.5% glycerol.
Purity: Purified
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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