Human Recombinant FTH1 protein (V2LY-0526-LY4046)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Protein Construction
This product is Human Recombinant FTH1 protein consist of Amino Acid: 1-183 and predicts a molecular mass of 21.2 kDa.
Molecule Mass
21.2 kDa
Sequence
Amino Acid: 1-183
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>95% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Ferritin Heavy Chain 1
Function
Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
Biological Process
Cellular iron ion homeostasis Source: ProtInc
Immune response Source: UniProtKB
Intracellular sequestering of iron ion Source: UniProtKB
Iron ion transport Source: GO_Central
Negative regulation of cell population proliferation Source: UniProtKB
Negative regulation of fibroblast proliferation Source: UniProtKB
Cellular Location
Cytosol; Extracellular exosome; Extracellular region; Autolysosome; Nucleus; Cytoplasm; Ficolin-1-rich granule lumen; Intracellular ferritin complex; Tertiary granule lumen
Involvement in disease
The disease is caused by variants affecting the gene represented in this entry. In a Japanese family affected by HFE5, a single point mutation has been detected in the iron-responsive element (IRE) in the 5'-UTR of FTH1 mRNA. This mutation leads to an increased binding affinity for iron regulatory protein and thereby to the efficient suppression of mRNA translation. A disorder of iron metabolism characterized by iron overload. Excess iron is deposited in a variety of organs leading to their failure, and resulting in serious illnesses including cirrhosis, hepatomas, diabetes, cardiomyopathy, arthritis, and hypogonadotropic hypogonadism. Severe effects of the disease usually do not appear until after decades of progressive iron loading.

Yang, G., Pan, Q., Lu, Y., Zhu, J., & Gou, X. (2023). miR-29a-5p modulates ferroptosis by targeting ferritin heavy chain FTH1 in prostate cancer. Biochemical and Biophysical Research Communications.

Muhammad, J. S., ElGhazali, G., Shafarin, J., Mohammad, M. G., Abu-Qiyas, A., & Hamad, M. (2022). SARS-CoV-2-induced hypomethylation of the ferritin heavy chain (FTH1) gene underlies serum hyperferritinemia in severe COVID-19 patients. Biochemical and Biophysical Research Communications, 631, 138-145.

Ali, A., Shafarin, J., Abu Jabal, R., Aljabi, N., Hamad, M., Sualeh Muhammad, J., ... & Hamad, M. (2021). Ferritin heavy chain (FTH1) exerts significant antigrowth effects in breast cancer cells by inhibiting the expression of c‐MYC. FEBS Open bio, 11(11), 3101-3114.

Li, X., Si, W., Li, Z., Tian, Y., Liu, X., Ye, S., ... & Zhu, M. (2021). miR‑335 promotes ferroptosis by targeting ferritin heavy chain 1 in in vivo and in vitro models of Parkinson's disease. International Journal of Molecular Medicine, 47(4), 1-12.

Bertoli, S., Paubelle, E., Bérard, E., Saland, E., Thomas, X., Tavitian, S., ... & Récher, C. (2019). Ferritin heavy/light chain (FTH1/FTL) expression, serum ferritin levels, and their functional as well as prognostic roles in acute myeloid leukemia. European journal of haematology, 102(2), 131-142.

Ravi, V., Madhankumar, A. B., Abraham, T., Slagle-Webb, B., & Connor, J. R. (2019). Liposomal delivery of ferritin heavy chain 1 (FTH1) siRNA in patient xenograft derived glioblastoma initiating cells suggests different sensitivities to radiation and distinct survival mechanisms. PLoS One, 14(9), e0221952.

Huang, H., Qiu, Y., Huang, G., Zhou, X., Zhou, X., & Luo, W. (2019). Value of ferritin heavy chain (FTH1) expression in diagnosis and prognosis of renal cell carcinoma. Medical science monitor: international medical journal of experimental and clinical research, 25, 3700.

Balaratnam, S., West, N., & Basu, S. (2018). A piRNA utilizes HILI and HIWI2 mediated pathway to down-regulate ferritin heavy chain 1 mRNA in human somatic cells. Nucleic Acids Research, 46(20), 10635-10648.

Jin, P., Kang, J., Lee, M. K., & Park, J. W. (2018). Ferritin heavy chain controls the HIF-driven hypoxic response by activating the asparaginyl hydroxylase FIH. Biochemical and biophysical research communications, 499(3), 475-481.

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For research use only. Not intended for any clinical use.

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