Antigen Preparation
A synthetic peptide corresponding to internal segment of human MMP-26
Background
"Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. It is thought that the protein encoded by this gene is cleaved at both ends to yield the active enzyme, but this processing has not been fully described. The enzyme degrades soluble and insoluble elastin. MMP-26 (matrix metallopeptidase-26), also known as Endometase or Matrilysin-2, is a 261 amino acid metalloproteinase that is secreted as an inactive protein and is activated upon cleavage by extracellular proteinases. Expressed specifically in the placenta and uterus, MMP-26 hydrolyzes (and subsequently degrades) a variety of proteins such as Fibrinogen, Fibronectin, Vitronectin and collagen type IV (COL4). MMP-26 binds zinc and calcium as cofactors and, unlike other MMP family members, lacks a conserved C-terminal domain. MMP-26 is widely expressed in a number of malignant tumor lines where it is thought to play an important role in tissue remodeling events that are associated with carcinogenesis."
Applications/Suggested Working Dilutions
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Immunoprecipitation
2-5 µg/ml
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Flow cytometry
Not tested
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