Overview
- Peptide (C)EGTHLMGVKDSNIHE, corresponding to amino acid residues 261-275 of human Ferroportin (Accession Q9NP59). 2nd intracellular loop.
Note: the structure of Ferroportin is still controversial and there is no defined topology yet. 
Western blot analysis of rat spleen (lanes 1 and 5), rat small intestine (lanes 2 and 6), rat liver (lanes 3 and 7) and mouse liver (lanes 4 and 8) lysates.1-4. Anti-Ferroportin (SLC40A1) Antibody (#AIT-001), (1:500).
5-8. Anti-Ferroportin (SLC40A1) Antibody, preincubated with Ferroportin/SLC40A1 Blocking Peptide (#BLP-IT001).
Expression of Ferroportin in mouse brainImmunohistochemical staining of mouse cerebellum and forebrain using Anti-Ferroportin (SLC40A1) Antibody (#AIT-001). A. In the cerebellum, Ferroportin staining (green) appears in cerebellar purkinje cells (horizontal arrows) and their dendrites (vertical arrows). B. In the forebrain, intense Ferroportin staining appears (green) in oligodendrocytes (horizontal arrows) and moderate staining is detected in neurons (vertical arrow). In both panels (A and B) DAPI is used as the counterstain.
Expression of Ferroportin in mouse brainImmunohistochemical staining of perfusion-fixed frozen mouse substantia nigra pars compacta (SNC) sections using Anti-Ferroportin (SLC40A1) Antibody (#AIT-001). A. Ferroportin staining (green) appears in several cells in the SNC. B. Tyrosine hydroxylase (red) stains dopaminergic neurons. C. Merge of A and B demonstrates Ferroportin in dopaminergic and non-dopaminergic neurons. Cell nuclei are stained using DAPI (blue).
- Donovan, A. et al. (2005) Cell Metab. 1, 191.
- Ward, D.M. and Kaplan, J. (2012) Biochim. Biophysi. Acta 1823, 1426.
- Ganz, T. et al. (2005) Cell Metab. 1, 155.
- Liu, X.B. et al. (2005) Blood Cells Mol. Dis. 35, 33.
- Wallace, D.F. et al. (2010) Am. J. Physiol. 298, C75.
Ferroportin (SLC40A1) is an iron transporter suggested to play roles in intestinal iron absorption and cellular iron release. To date, Ferroportin is the only known mammalian iron exporter and is essential for transport of iron from one cell type to another1.
Ferroportin has 9-12 transmembrane domains. The topology of the transporter has not been defined with precision and the number of transmembrane domains is still under scrutiny. Studies indicate that the amino terminus of Ferroportin is cytosolic. The location of the carboxyl-terminal, however, is unclear. A second controversial issue regarding Ferroportin structure is whether Ferroportin is a monomer or dimer. Many reports using similar approaches including chromatography, cross-linking and physical techniques such as birefringence, have led to contrasting results2.
Ferroportin is found in all the tissues where major iron flows are regulated, including duodenal enterocytes, placental trophoblast, macrophages, and hepatocytes3.
Mutations that result in defective Ferroportin transport activity will lead to the phenotype of “classic” Ferroportin disease, which is macrophage iron loading and normal to low transferrin saturation2. Expression of mutant Ferroportin in some cultured cell types results in defects in Ferroportin trafficking where the mutant protein never reaches the cell surface4. In other cell types, the mutant Ferroportin was shown to accumulate at the cell surface but had defective transport activity5.
Alomone Labs is pleased to offer a highly specific antibody directed against an epitope of human Ferroportin-1. Anti-Ferroportin (SLC40A1) Antibody (#AIT-001) can be used in western blot and immunohistochemistry applications. It has been designed to recognize Ferroportin-1 from human, rat, and mouse samples.
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