Human MMP-8 Alexa Fluor® 350-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: MMP-8

Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP‑8 (neutrophil collagenase) is expressed in neutrophils, where it is stored in specific granules. MMP‑8 release from the neutrophils is stimulated by various factors such as interleukins 1 and 8, TNF-alpha and GM-CSF. MMP‑8 is capable of cleaving types I, II and III triple-helical collagen, gelatin peptides, fibronectin, proteoglycans, aggrecan, serpins, beta -casein and peptides such as angiotensin and substance P. In addition to its function in phagocytosis,
MMP‑8 has a high capacity for infiltrating connective tissue, and is implicated in the breakdown of the extracellular matrix in diseases such as rheumatoid arthritis. Structurally, MMP‑8 consists of several domains: a pro-domain that is cleaved upon activation, a catalytic domain containing the zinc-binding site, a short hinge region and a hemopexin-like domain. MMP‑8 is heavily glycosylated.

Product Datasheets

Related Research Areas

• Cancer Biomarkers
• Collagen Modifying Enzymes
• Metalloproteases and Regulators
• Microglia Development
• MMPs, TIMPs and Related Molecules
• Search Bioprocessing Enzymes