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-3, MMP-10 and MMP-11 (also designated stromelysin-1, 2 and 3, respectively) activate procollagenase. MMP-3 activation of procollagenase can occur via two pathways. Direct activation by MMP-3 is slow and activation by MMP-3 in conjunction with tissue or plasma proteinases is rapid. MMP-10 is expressed in small intestine, and at lower levels in lung and heart. MMP-11 is specifically expressed in stromal cells of breast carcinomas and contributes to epithelial cell malignancies.
Anwendungen
ELISA
Verdünnungen
ELISA: 2-4 µg/ml
Reaktivität
Human
Immunogen
Recombinant fragment, corresponding to amino acids 317-327, of human MMP3 protein.
Wirt
Mouse
Klonalität
Monoclonal
Klon
1B4
Isotyp
IgG3
Leichte Ketten
lambda
Konjugat
Unconjugated
Reinigung
Protein A chromatography.
Konzentration
200 µg/ml
Molekulargewicht
57 kDa
Produktform
Liquid
Formulierung
Supplied in 10mM Phosphate Buffered Saline with 0.05% BSA and 0.05% Sodium Azide.
SDS-PAGE analysis of Anti-MMP3 Antibody [1B4] under non-reduced and reduced conditions; showing intact IgG and intact heavy and light chains, respectively. SDS-PAGE analysis confirms the integrity and purity of the antibody.
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