The matrix metalloproteinases (MMPs) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, Fibronectin, Laminin and proteoglycan. MMP catalysis requires both calcium and zinc. Membrane-type matrix metalloproteinases are type I membrane proteins that function to activate other MMPs. MT-MMP activation appears to be mediated by members of the proprotein convertase family, suggesting that a proprotein convertase/MT-MMP/MMP cascade may be involved in the regulation of ECM turnover. MT-MMP-6 (also known as MMP-25, MT6-MMP or Leukolysin) is the second GPI-anchored proteinase in the MMP family. Similar to MMP-3, MT-MMP-6 is able to cleave type IV collagen, Fibronectin, fibrin and gelatin. However, MT-MMP-6 cannot cleave Laminin-1 or activate progelatinase B. MT-MMP 6 is expressed in leukocytes, lung and spleen.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of MT-MMP-6 of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including canine, bovine and porcine
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 341-400 of MT-MMP-6 of human origin
Tissue Specificity
epitope corresponding to amino acids 341-400 of MT-MMP-6 of human origin
Western blot analysis of MT-MMP-6 expression in HL-60 whole cell lysate.
Application Notes
recommended for detection of MT-MMP-6 of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including canine, bovine and porcine
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.