Recombinant Human HAMP(60-84) Protein, hFc Tag
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| Amount : | 50 µg |
| Content : | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8% trehalose is added as protectants before lyophilization. |
| Storage condition : | Store at -20°C to -80°C for 12 months in lyophilized form. After reconstitution, if not intended for use within a month, aliquot and store at -80°C (Avoid repeated freezing and thawing). Lyophilized proteins are shipped at ambient temperature. |
| Uniprot ID : | P81172 |
| Alternative Name : | HEPC; HFE2B; LEAP1; PLTR |
Molecular Characterization: HAMP(Asp60-Thr84) hFc(Glu99-Ala330)
Molecular weight: The protein has a predicted molecular mass of 28.9 kDa after removal of the signal peptide. The apparent molecular mass of HAMP(60-84)-hFc is approximately 25-35 kDa due to glycosylation.
Description: Recombinant Human HAMP(60-84) Protein with C-terminal human Fc tag
The product encoded by this gene 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 against bacteria and fungi. Mutations in this gene cause hemochromatosis type 2B, also known as juvenile hemochromatosis, a disease caused by severe iron overload that results in cardiomyopathy, cirrhosis, and endocrine failure.
Molecular weight: The protein has a predicted molecular mass of 28.9 kDa after removal of the signal peptide. The apparent molecular mass of HAMP(60-84)-hFc is approximately 25-35 kDa due to glycosylation.
Description: Recombinant Human HAMP(60-84) Protein with C-terminal human Fc tag
The product encoded by this gene 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 against bacteria and fungi. Mutations in this gene cause hemochromatosis type 2B, also known as juvenile hemochromatosis, a disease caused by severe iron overload that results in cardiomyopathy, cirrhosis, and endocrine failure.
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