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The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
MMP15 (matrix metallopeptidase 15), also known as MT2-MMP, is a member of the membrane-type matrix metalloproteinases characterized by their ability to degrade components of the extracellular matrix. It is encoded by the MMP15 gene, located on chromosome 16q12.2. Structurally, this enzyme is a type I transmembrane protein, composed of a signal peptide, a propeptide, a catalytic domain, a hemopexin-like domain, a transmembrane domain, and a cytoplasmic tail. The cleavage of the propeptide is crucial for its activation to degrade various substrates. The specific cleavage at Tyr132 is significant for its regulatory mechanisms in different physiological and pathological processes, including tissue remodeling, cancer progression, and metastasis. MMP15 has been implicated in cancer, where its expression levels correspond with the disease state and can influence cancer cell invasion and angiogenesis by modifying the extracellular environment and cellular interactions.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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