Host: E. coli • AA: 1-183 (full length) • Tagless • MW: 21.2 kDa
Technical Support & Resources

Visit our FAQ

Contact Us

Toll Free Phone (USA and Canada Only): (888) 526-5351
Direct Phone: (734) 975-3888

Request Technical Support

Technical Support Request

To streamline the process attach the appropriate questionnaire to your inquiry.

Download IHC QuestionnaireDownload WB Questionnaire

View Our Privacy Statement for details on how we use and protect your data. In addition, this site is protected by hCaptcha and its Privacy Policy and Terms of Service apply.

Product Categories

Product Type

Application

Ferritin Heavy Chain (human, recombinant)

Item No. 32033

Technical Information
Synonyms
  • Cell Proliferation-inducing Gene 15 Protein
  • Ferritin H Subunit
  • FTH1
Purity
≥95% estimated by SDS-PAGE
Source
Recombinant human ferritin heavy chain expressed in E. coli
Amino Acids
1-183 (full length)
MW
21.2 kDa
Lyophilized from sterile PBS, pH 7.5
UniProt Accession №
P02794
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
Recommended Products

Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

    Add

    Cayman Chemical
    Visit Our Cancer Resource Center
    Find Tools & Resources to Study the Hallmarks of Cancer
    • Cancer cell signaling & regulation
    • Cancer metabolism
    • Tumor microenvironment
    EXPLORE NOW
    Product Description

    Ferritin is a spherical protein involved in iron storage and biomineralization.1,2 It is primarily localized to the cytoplasm, but is also present in the mitochondria and nucleus, and is composed of 24 protein subunits with a tissue-specific ratio of ferritin heavy chains (FTH1s) to ferritin light chains (FTLs; Item No. 32032). FTH1 and FTL are nearly identical in overall conformation but only share approximately 50% sequence homology.3 FTH1 functions as a ferroxidase that catalyzes the oxidation of Fe(II) to Fe(III) and FTL has roles in iron nucleation and protein stability. FTH1 is overexpressed in acute myeloid leukemia and leukemic stem cells compared with normal hematopoietic stem cells.4 Elevated levels of cytoplasmic and nuclear FTH1 are associated with a favorable and poor prognosis, respectively, in patients with triple negative breast cancer.5 Point mutations in the 5’-UTR of FTH1 mRNA have been found in individuals with autosomal dominant iron overload.6 Disruption of Fth1 is embryonic lethal in mice.7 Cayman’s Ferritin Heavy Chain (human, recombinant) protein consists of 183 amino acids and has an apparent molecular mass of 21.2 kDa by SDS-PAGE under reducing conditions.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Carmona, U., Li, L., Zhang, L., et al. Ferritin light-chain subunits: Key elements for the electron transfer across the protein cage. Chem. Commun. (Camb.) 50(97), 15358 (2014).

    2. Zarjou, A., Black, L.M., McCullough, K.R., et al. Ferritin light chain confers protection against sepsis-induced inflammation and organ injury. Front. Immunol. 10(131), (2019).

    3. Baraibar, M.A., Barbeito, A.G., Muhoberac, B.B., et al. A mutant light-chain ferritin that causes neurodegeneration has enhanced propensity toward oxidative damage. Free Radic. Biol. Med. 52(9), 1692-1697 (2012).

    4. Bertoli, S., Paubelle, E., Bérard, E., et al. Ferritin heavy/light chain (FTH1/FTL) expression, serum ferritin levels, and their functional as well as prognostic roles in acute myeloid leukemia. Eur. J. Haematol. 102(2), 131-142 (2019).

    5. Liu, N.Q., De Marchi, T., Timmermans, A.M., et al. Ferritin heavy chain in triple negative breast cancer: A favorable prognostic marker that relates to a cluster of differentiation 8 positive (CD8+) effector T-cell response. Mol. Cell Proteomics 13(7), 1814-1827 (2014).

    6. Kato, J., Fujikawa, K., Kanda, M., et al. A mutation, in the iron-responsive element of H ferritin mRNA, causing autosomal dominant iron overload. Am. J. Hum. Genet. 69(1), 191-197 (2001).

    7. Ferreira, C., Bucchini, D., Martin, M.E., et al. Early embryonic lethality of H ferritin gene deletion in mice. The Journal of Biological Chemisty 275(5), 3021-3024 (2000).