MMP 8 Human
EC 3.4.24.34, Matrix metalloproteinase-8, MMP-8, PMNL-CL, HNC, CLG1.
Description
The MMP-8 is purified by proprietary chromatographic techniques.
Product Specs
Recombinant human neutrophil MMP-8, in its latent form, spanning the entire protein length.
Matrix metalloproteinase 8 (MMP-8) exhibits a strong preference for degrading collagen type I among interstitial collagens.
Elevated levels of full-length MMP-8 protein correlated with increased neutrophil infiltration in the skin. Neutrophils are recognized as the primary source of MMP-8.
MMP-8 is synthesized and stored within specific granules in neutrophil leukocytes. Consequently, its activity is modulated by factors like surface-bound ligands (e.g., IgG or complement components) that trigger its release through degranulation. Upon release and activation via proteolytic or oxidative mechanisms, MMP-8 plays a pivotal role in the breakdown of connective tissue, a hallmark of inflammatory responses.
The purification of MMP-8 is achieved using proprietary chromatographic methods.
Repeated freeze-thaw cycles should be avoided.
One unit of collagenolytic activity is defined as the amount of enzyme required to cleave 1 µg of collagen per minute using the solution method.
Serves as a standard for the analysis of mammalian collagenase activity.
EC 3.4.24.34, Matrix metalloproteinase-8, MMP-8, PMNL-CL, HNC, CLG1.
Product Science Overview
The MMP-8 protein is encoded by the MMP8 gene, which is located on chromosome 11q22.3 in humans . The gene is part of a cluster of MMP genes. Most MMPs are secreted as inactive proproteins and are activated when cleaved by extracellular proteinases. However, MMP-8 is unique as it is stored in secondary granules within neutrophils and is activated by autolytic cleavage .
MMP-8 primarily degrades type I, II, and III collagens, which are major components of the extracellular matrix . This activity is essential for normal tissue remodeling and repair. In disease contexts, such as cancer, the loss of MMP-8 has been associated with increased tumor growth and metastatic burden, as well as enhanced tumor vascularity and altered immune cell infiltration .
Recombinant human MMP-8 is produced using advanced biotechnological methods. It is typically expressed in a mouse myeloma cell line (NS0) and purified to high levels of purity (>90%) using SDS-PAGE under reducing conditions . The recombinant protein is available in both carrier-free and carrier-containing formulations, with the carrier-free version being recommended for applications where the presence of bovine serum albumin (BSA) could interfere .
Recombinant MMP-8 is widely used in research to study its role in various physiological and pathological processes. It is also used in assays to measure its activity, which is typically done using fluorogenic peptide substrates . The enzyme’s activity can be measured by its ability to cleave these substrates, providing insights into its function and potential therapeutic applications .
MMP-8 has been implicated in various diseases, including cancer and inflammatory conditions. In cancer, MMP-8 activity has been linked to the regulation of the innate immune system through its interaction with cytokines like IL-6 and IL-8 . Understanding the role of MMP-8 in these processes can provide valuable insights into potential therapeutic targets for treating these diseases.
