For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 10; NC_009153.2 (18929521..18930451). Location: chromosome: 10

Human spleen ferritin

Highly Purified
Highly purified

Supplied as a liquid in SDS-PAGE reducing sample buffer.

May be stored at 4 degree C for short-term only. For long-term storage, store at -20 degree C. Aliquots are stable for at least 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Small volumes of FTL protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Elemental iron is required for a variety of normal cellular functions and vital for proper growth and development. Natural iron is quite insoluble and excess iron is harmful, since it can catalyze the formation of potentially damaging reactive oxygen species. Cells have developed mechanisms to improve solubility of iron and to control intracellular iron levels. The major pool of body iron (~85%; 40-50mg/kg) is found in circulating hemoglobin and muscle myoglobin. Iron absorption occurs primarily in the intestine (duodenum) and inversely related to body iron reserve. Several proteins including Ferritin, transferrin (Tf), transferrin receptors (TfRs), and iron regulatory proteins (IRPs) etc play a key role in iron metabolism. Ferritin is the major protein involved in iron sequestration and detoxification. Ferritin is found in all living species and its three dimensional structure is conserved in all species despite very low sequence identity from bacteria to human. Mammalian liver and spleen ferritin (~450kD) consists of 24 subunits of 2 species, the heavy subunit (~2kD; FTH) and the light subunit (~ 19kD; FTL). The 2 types of apoferritin subunits were designated H and L for heart and liver, respectively. Ferritin molecules from plants and bacteria contain only H-type chains. 'H-type' is associated with the presence of centers catalyzing the oxidation of two Fe(II) atoms. FTL subunit (rich in human liver and spleen) is coded by a gene in segment 19q13.3 and FTH subunit (rich in human heart) is located on chromosome 11. Ferritin is capable of storing up to 4,500 atoms of ferric iron. The H-to-L ratio within ferritin varies in a tissue- specific manner and is also influenced by pathophysiological conditions, including inflammation and malignancy. Hyperferritinemia- cataract syndrome has a mutation in the iron response element (IRE) in the 5-prime noncoding region of the FTL gene. Synthesis of both ferritin subunits is controlled by a common cytosolic protein, iron regulatory proteins (IRPs), which binds to the iron- responsive element (IRE) in the 5'-UTR of the H-and L-ferritin mRNAs. H-chains are important for Fe(II) oxidation and L-chains assist in core formation.

Molecular Biology; MB-Serum Proteins

Western Blot (WB)

Suitable for use in Western Blot.
Dilution: Load 10ul/lane
Optimal dilution to be determined by researcher.

19,978 Da[Similar Products]

ferritin light chain; ferritin L subunit

Ferritin light chain

Ferritin L subunit??[Similar Products]

FRIL_HORSE

Function: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. 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.

Subunit structure: Oligomer of 24 subunits. There are two types of subunits: L (light) chain and H (heavy) chain. The major chain can be light or heavy, depending on the species and tissue type. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited.

Miscellaneous: In horse spleen the light chain is the major chain.

Sequence similarities: Belongs to the ferritin family.Contains 1 ferritin-like diiron domain.

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.