epitope corresponding to amino acids 471-580 mapping near the C-terminus of MT-MMP-4 of human origin
Modification Notes
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 (1). MMP catalysis requires both calcium and zinc (2). MT-MMP 4 (also known as MMP-17 or MT4-MMP) is a glycosylphosphatidylinositol (GPI)-anchored proteinase. The zinc-dependent MMP has a unique specificity among synthetic substrates and the capability to degrade gelatin and activate progelatinase A (3,4). MT-MMP 4 is mainly expressed in the brain, leukocytes, colon, ovary and testis. In addition, MMP-4 is expressed in all breast carcinomas (5). The human MT-MMP 5 (also known as MMP-24 or MT5-MMP) gene maps to chromosome 20q11.2, a region frequently amplified in tumors. MMP-5 is predominantly expressed in brain, kidney, pancreas and lung. MT-MMP 5 is also expressed at high levels in brain tumors compared to normal brain tissue (6). MT-MMP 6 (also known as MMP-25, MT6-MMP or Leukolysin) is the second GPI-anchored proteinase in the MMP family (7). A C-terminal-truncated MMP-6 protein is expressed as a strong gelatinolytic species that is derived from a cell-associated proenzyme. MT-MMP 6 is expressed in leukocytes, lung and spleen (8).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of MT-MMP-4 of mouse, rat and human origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 471-580 mapping near the C-terminus of MT-MMP-4 of human origin
Tissue Specificity
epitope corresponding to amino acids 471-580 mapping near the C-terminus of MT-MMP-4 of human origin