FTL / ferritin, light polypeptide Protein (His Tag)

Ferritin, light polypeptide Protein Datasheet

FTL / Ferritin, light polypeptide Protein Product Information

• Synonym: MGC71996, NBIA3
• Protein Construction: A DNA sequence encoding the human FTL (P02792) (Met 1-Asp 175) was expressed, with a polyhistidine tag at the N-terminus.
• Source: Human
• Expression Host: E.coli

FTL / Ferritin, light polypeptide Protein QC Testing

• Purity: > 95 % as determined by SDS-PAGE.
• Endotoxin: Please contact us for more information.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Met
• Molecular Mass: The recombinant human FTL consisting of 191 amino acids and has a calculated molecular mass of 22.1 KDa. It migrates as an approximately 23KDa band in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from sterile 50mM Tris, 20%glycerol, pH 9.5
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: FTL / Ferritin, light polypeptide protein

FTL / Ferritin, light polypeptide Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

FTL / Ferritin, light polypeptide Protein Description

Ferritin, light polypeptide (FTL) is the light subunit of the ferritin protein. Ferritin is the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Storage of iron in the tissues occurs in the form of ferritin and hemosiderin. The latter originates from ferritin that has undergone intracellular digestion of its protein shell, leaving the iron core. Ferritin and hemosiderin are components of a continuum. Ferritin has been identified in all types of living organisms: animals, plants, molds, and bacteria. Whithin the protein shell of ferritin, iron is first oxidized to the ferric state for storage as ferric oxyhdroxide. Thus, ferritin removes excess iron from the cell sap where it could otherwise participate in peroxidation mechanisms.

References

1. Munro HN. et al., 1988, Ann N Y Acad Sci. 526: 113-23.
2. Zhang Y. et al., 2008, Proteomics. 8 (20): 4344-56.
3. Lebo RV. et al., 1986, Hum Genet. 71 (4): 325-8.