Anti-MMP9 Antibody Picoband® Fluoro488 Conjugated

Matrix metallopeptidase 9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), is an enzyme that in humans is encoded by the MMP9 gene. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.

Matrix metalloproteinase-9; MMP-9;3.4.24.35;92 kDa gelatinase;92 kDa type IV collagenase; Gelatinase B; GELB;67 kDa matrix metalloproteinase-9;82 kDa matrix metalloproteinase-9; MMP9; CLG4B

A synthetic peptide corresponding to a sequence at the C-terminus of human MMP-9, different from the related mouse sequence by fourteen amino acids, and from the related rat sequence by sixteen amino acids.

Angiogenesis, Atherosclerosis, Cancer, Cardiovascular, Cell Biology, Cytoskeleton/ECM, ECM Enzymes, Extracellular Matrix, Invasion/Microenvironment, Metalloprotease, Proteolysis/Ubiquitin, Proteolytic Enzymes, Signal Transduction, Tumor Biomarkers

May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide. .

1. Template:, 92kDa type IV collagenase) . 2. Yuichiro Hirose et al. (May 2008) . A Functional Polymorphism in THBS2 that Affects Alternative Splicing and MMP Binding Is Associated with Lumbar-Disc Herniation.