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).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
MMP26 polyclonal antibody detects endogenous levels of MMP26 protein.
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