Overview
Introducing Human MMP-8, a highly purified neutrophil collagenase crucial for your research and diagnostic applications. As a part of the matrix metalloproteinase family, MMP-8 plays a pivotal role in the degradation of extracellular matrix components. Isolated from stimulated human neutrophil granulocytes, this full-length pro-enzyme is ideal for studying tissue remodeling, inflammation, and various physiological processes.
Key Features
- Full-length pro-enzyme derived from human neutrophils
- Can be activated by incubating with 1 mM APMA at 37°C for 1 hour
- Activity can be measured using FRET-based enzymatic assays
- Essential for research in inflammation and tissue remodeling
- Available in a convenient 100 µL format
Specifications
| Product Name | Human MMP-8 |
|---|---|
| Volume | 100 µL |
| Source | Human neutrophil granulocytes |
| Activation Method | 1 mM APMA, 37°C for 1 hr |
FAQ
What is the optimal storage condition for Human MMP-8?
Store Human MMP-8 at -80°C to preserve its activity and stability. Avoid repeated freeze-thaw cycles to maintain integrity.
How is the enzymatic activity of MMP-8 measured?
The activity of MMP-8 can be accurately measured using FRET-based enzymatic assays that allow for precise quantification in various experimental setups.
Can Human MMP-8 be used in in vivo studies?
While Human MMP-8 is primarily designed for in vitro studies, its role in inflammation makes it a valuable tool for understanding pathological processes related to tissue remodeling.
Enhance your research capabilities with our Human MMP-8, available now for purchase. This assay kit is perfect for scientists focused on the intricacies of collagen degradation and inflammation. Interested in further applications? Explore our selection of other proteins such as recombinant mouse MOG (1-125) or recombinant human MOG (1-125) to complement your experiments. For studying other proteins involved in neurological disorders, consider our EndoClear™ Plus human recombinant a-Synuclein protein. Shop now and advance your studies with our catalog of recombinant proteins, including various catalog recombinant products.




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