Overview
- Peptide (C)ESVSEPRKSFMYSR, corresponding to amino acid residues 251-264 of mouse ZIP6 (Accession Q8C145). Extracellular, N-terminus.
- Mouse and rat brain lysates, human SH-SY5Y and K562 cell lysates (1:200-1:2000).
- Western blot analysis of mouse (lanes 1 and 3) and rat (lanes 2 and 4) brain lysates:1,2. Anti-ZIP6/SLC39A6 (extracellular) Antibody (#AZT-006), (1:200).
3,4. Anti-ZIP6/SLC39A6 (extracellular) Antibody, preincubated with ZIP6/SLC39A6 (extracellular) Blocking Peptide (#BLP-ZT006).
- Rat brain sections (1:200).
- Human Jurkat T-cell leukemia cells (5 µg).
ZIP6 (SLC39A6) is a zinc (Zn) transporter located on the cell membrane.
Zn is an essential heavy metal, part of numerous biological processes as an enzymatic co-factor, and also as an intracellular signaling mediator that recruits extracellular stimuli and determines the final outputs of various physiological pathways. Intracellular and extracellular Zn levels regulate many cellular processes such as autophagy, cell growth and death, and cell migration1,2.
Movement of Zn in and out of cells, across membranes, is regulated by zinc transporters. Zn transporter protein 6 (ZIP6) is a member of the ZIP family of Zinc transporters and of the LIV-1 sub-family. ZIP transporters contain 8 transmembrane domains with a cytoplasmic region between TM3 and TM4. LIV-1 subfamily members contain the HEXXH motif within TM5. They also exhibit diverse lengths of the N-terminal extracellular domain3.
The gene encoding this transporter has been shown to take part in estrogen receptor‐positive breast cancer and serves as a reliable marker of this disease. Overexpression of ZIP6 protein is also observed in prostate and kidney tumor cells4.
ZIP6 is also strongly upregulated during T-cell activation5. ZIP6 heteromerizes with ZIP10 for oocyte-to-egg transition and epithelial to mesenchymal transition in fetus development6,7.