DATA SHEET for RP1MMP 8

RP1MMP8 is a Rabbit antibody to the Matrix Metalloproteinase, Neutrophil Collagenase, made with a synthetic peptide based on the hinge region of the Human sequence. The antibody binds to MMP-8, but does not cross react with the other MMP family members (MMP-1, MMP-2, MMP-3, MMP-9, etc.). The antibody has been peptide-affinity purified, concentrated to 1mg/ml, with the addition of Sodium Azide as preservative and 50% glycerol as cryoprotectant

MMP-8, first described in neutrophils, is a classical type-I collagenase; like MMP-1 it is able to cleave intact type-I collagen at the same site in all three strands. The sequence for MMP-8 is very similar to MMP-1, but until recently it was thought to be produced exclusively by neutrophils. MMP-8 has recently been detected in other cell types. MMP-8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms. RP1MMP8 Anti-MMP-8 works well for Western Blotting applications, and when used against the reduced protein identifies bands at 64 Kd, 58 Kd, and a series of further cleaved active forms. RP1MMP8 will also bind to the non-reduced protein, and thus has application for immunoprecipitation, immunohistochemistry, and ELISA. MMP-8 is not produced by most cell types; it has been found in PMNL neutrophils, arthritic chondrocytes and gingival fibroblasts. MMP-8 levels in quiescent cells and tissues are minimal, and mitogen stimulation or protein concentration is often needed to visualize the bands. In addition, cell types differ greatly in the quantity of MMP-8 produced. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for non-human samples.