The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-8 (also designated neutrophil collagenase, PMNL collagenase or collagenase-2) degrades fibrillar collagen types I, II and III. Unlike other members of the MMP family, MMP-8 is expressed exclusively in inflammatory conditions. MMP-8 is highly expressed in the postpartum uterus, and it is thought to be involved in the postpartum involution of the uterus. MMP-8 is also the predominant collagenase expressed in ulcers and healing wounds.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
IHC: 1:50~1:200
Application Notes:
MMP-8 (F445) polyclonal antibody detects endogenous levels of MMP-8 protein.
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