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HAMP Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P81172 |
|---|
| Gene ID | 57817 |
|---|---|
| Other Names | Hepcidin, Liver-expressed antimicrobial peptide 1, LEAP-1, Putative liver tumor regressor, PLTR, Hepcidin-25, Hepc25, Hepcidin-20, Hepc20, HAMP, HEPC, LEAP1 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | HAMP (HGNC:15598) |
|---|---|
| Synonyms | HEPC, LEAP1 |
| Function | Liver-produced hormone that constitutes the main circulating regulator of iron absorption and distribution across tissues. Acts by promoting endocytosis and degradation of ferroportin/SLC40A1, leading to the retention of iron in iron-exporting cells and decreased flow of iron into plasma (PubMed:22682227, PubMed:29237594, PubMed:32814342). Controls the major flows of iron into plasma: absorption of dietary iron in the intestine, recycling of iron by macrophages, which phagocytose old erythrocytes and other cells, and mobilization of stored iron from hepatocytes (PubMed:22306005). |
| Cellular Location | Secreted. |
| Tissue Location | Highest expression in liver and to a lesser extent in heart and brain. Low levels in lung, tonsils, salivary gland, trachea, prostate gland, adrenal gland and thyroid gland. Secreted into the urine and blood (PubMed:11034317). Expressed by hepatocytes (PubMed:15124018). |
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Provided below are standard protocols that you may find useful for product applications.
Background
HAMP is involved in the maintenance of iron homeostasis, and it is necessary for the regulation of iron storage in macrophages, and for intestinal iron absorption. The preproprotein is post-translationally cleaved into mature peptides of 20, 22 and 25 amino acids, and these active peptides are rich in cysteines, which form intramolecular bonds that stabilize their beta-sheet structures. These peptides exhibit antimicrobial activity.
References
Matsumoto, M., et al. Circ. J. 74(2):301-306(2010)del Giudice, E.M., et al. J. Clin. Endocrinol. Metab. 94(12):5102-5107(2009)Kwapisz, J., et al. J Zhejiang Univ Sci B 10(11):791-795(2009)Barton, J.C., et al. Am. J. Hematol. 84(11):710-714(2009)Nemeth, E., et al. Acta Haematol. 122 (2-3), 78-86 (2009) Hunter, H.N., et al. J. Biol. Chem. 277(40):37597-37603(2002)Kluver, E., et al. J. Pept. Res. 59(6):241-248(2002)
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