MMP26 polyclonal antibody

Metalloproteinases (MMPs) are a family of proteins that are involved in the breakdown of the extracellular matrix during normal cellular events, including reproduction, tissue remodeling and embryonic development. 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.

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of MMP26 polyclonal antibody at 1:500 dilution Lane1:HEK293T whole cell lysate Lane2:Raw264.7 whole cell lysate Lane3:H9C2 whole cell lysate