The copper efflux transporters ATP7A and ATP7B sequester intracellular copper into the vesicular secretory pathway for export from the cell. ATP7A functions as a transmembrane copper-translocating P-type ATPase and plays a vital role in systemic copper absorption in the gut and copper reabsorption in the kidney. Polarized epithelial cells such as Madin-Darby canine kidney cells are a physiologically relevant model for systemic copper absorption and reabsorption in vivo. Although ATP7A is not detectable in most normal tissues, it is expressed in a considerable fraction of many common tumor types. Increased expression of ATP7A renders cells resistant to cisplatin and carboplatin. Mutations in the ATP7A gene result in Menkes disease, which is fatal in early childhood. Mutations in the ATP7B gene lead to the autosomal recessive disorder, Wilson disease, characterized by neurological symptoms and hepatic damage.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of Copper-transporting ATPase 2 isoforms a and b 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 1372-1465 mapping within a C-terminal cytoplasmic domain of ATP7B of human origin
Tissue Specificity
epitope corresponding to amino acids 1372-1465 mapping within a C-terminal cytoplasmic domain of ATP7B of human origin