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.
Applications
ELISA
Dilutions
ELISA: 2-4 µg/ml
Reactivity
Human
Immunogen
Recombinant fragment, corresponding to amino acids 317-327, of human MMP3 protein.
Host
Mouse
Clonality
Monoclonal
Clone ID
1B4
Isotype
IgG3
Light Chains
lambda
Conjugate
Unconjugated
Purification
Protein A chromatography.
Concentration
200 µg/ml
Molecular Weight
57 kDa
Product Form
Liquid
Formulation
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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