Mouse/Rat MMP-2 Biotinylated 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-2

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-2 (gelatinase A), a type IV collagenase, can degrade a broad range of substrates including type IV, V, VII and X collagens as well as elastin and fibronectin. 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-2 has been shown to be associated with many connective tissue cells as well as neutrophils, macrophages and monocytes. Structurally, MMP-2 may be divided into several distinct domains: a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin-like domain thought to play a role in substrate targeting; and a carboxyl terminal (hemopexin-like) domain containing 2 N-linked glycosylation sites. The amino acid sequences of the proenzymes are identical between mouse and rat.  

Product Datasheets

Related Research Areas

• APP Cleavage and Amyloid-beta Degradation
• Cancer Biomarkers
• Collagen Modifying Enzymes
• Extracellular Matrix Remodeling and Cell Migration During EMT
• Gametes and Fertilization
• HIF Transcription Factors
• Inflammatory Mediators
• Mesenchymal Cells and EMT
• Metalloproteases and Regulators
• MMPs, TIMPs and Related Molecules
• Platelets
• Preeclampsia