Cell Signaling Technology

Product Pathways - Metabolism

FTH1 Antibody #3998

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Mk Endogenous 21 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

FTH1 Antibody detects endogenous levels of total FTH1 protein. Nonspecific bands are seen above 80 kDa.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino-terminal region of FTH1. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HT-29 and HeLa cells using FTH1 Antibody.

Background

Ferritin (FTH) is a ubiquitous and highly conserved protein which plays a major role in iron homeostasis by sequestering and storing iron in a non-toxic and bioavailable form (1). The assembled ferritin molecule, often referred to as a nanocage, can store up to 4,500 atoms of iron (2,3). It forms a holoenzyme of ~450 kDa, consisting of 24 subunits made up of two types of polypeptide chains: ferritin heavy chain and ferritin light chain, each having unique functions. Ferritin heavy chains catalyze the first step in iron storage, the oxidation of Fe(II), whereas ferritin light chains promote the nucleation of ferrihydrite, enabling storage of Fe(III) (4). In addition to iron buffering, heavy chain ferritin also enhances thymidine biosynthesis (5). Serum ferritin levels serve as an indicator of the amount of iron stored in the body. Serum ferritin is the most sensitive test for anaemia. The level of serum ferritin is markedly elevated in inflammation, malignancy, and iron overload disorders (6). Research studies have found that defects in ferritin proteins are also associated with several neurodegenerative diseases (7).

  1. Munro, H.N. et al. (1988) Ann N Y Acad Sci 526, 113-23.
  2. Theil, E.C. (2004) Annu Rev Nutr 24, 327-43.
  3. Theil, E.C. et al. (2006) J Biol Inorg Chem 11, 803-10.
  4. Treffry, A. et al. (1992) FEBS Lett 302, 108-12.
  5. Oppenheim, E.W. et al. (2001) J Biol Chem 276, 19855-61.
  6. Tarng, D.C. (2009) Nat Clin Pract Nephrol 5, 66-7.
  7. Fischer, P. et al. (1997) Life Sci 60, 2273-8.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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