Reactivity | RtSpecies Glossary |
Applications | Enzyme Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 (Catalog # ES001). The specific activity is >710 pmol/min/μg, as measured under the described conditions. |
Source | Mouse myeloma cell line, NS0-derived rat MMP-9 protein Leu35-Pro708, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Leu35 |
Structure / Form | Pro form |
Protein/Peptide Type | Recombinant Enzymes |
Gene | Mmp9 |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 75 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 94 kDa, reducing conditions |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Supplied as a 0.2 μm filtered solution in MES, NaCl, CaCl2 and Glycerol. |
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Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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Assay Procedure |
*Adjusted for Substrate Blank |
Matrix metalloproteinases are a family of zinc- and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 may be divided into five distinct domains: a pro-domain which is cleaved upon activation, a catalytic domain containing the zinc binding site, a gelatin-binding domain consisting of three contiguous fibronectin type II units, a proline-rich linker region, and four carboxyl terminal hemopexin-like domains.
Images | Ratings | Applications | Species | Date | Details | ||||||||
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reviewed by:
Verified Customer |
Zymograph positive control | 04/06/2018 |
Summary
Comments
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Verified Customer 04/06/2018 |
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Application: | Zymograph positive control | |
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