Iron Regulatory Protein, Rat, Control Peptide (IRP-1)
Artikelnummer:
USB-I8670-20
Hersteller Artikelnummer:
I8670-20
Alternativnummer:
USB-I8670-20-100
Hersteller:
US Biological
Kategorie:
Molekularbiologie
Applikation:
ELISA
Control Peptide for I8615-01 (antiserum) and I8615-02 (affinity purified antibody). Synthetic peptide consisting of 20aasequence within the N-terminus of rat IRP-1. Elemental iron is required for a variety of normal cellular functions and vital for proper growth and development. However, natural iron is quite insoluble and excess iron is harmful, since it can catalyze the formation of potentially damaging reactive oxygen species. Humans also have very limited capacity to excrete iron. Therefore, cells have developed mechanisms to improve solubility of iron and to control intracellular iron levels at the point of absorption in the intestine and other tissue. Several proteins including Ferritin, transferrin (Tf), transferrin receptors (TfRs), and iron regulatory proteins (IRPs), iron transporter (NRMAP2/DMT1/DCT1) etc play a key role in iron metabolism. Some genes involved in iron-metabolism are associated with genetic disorders such as Friedreichs Ataxia (Frataxin), genetic hemochromatosis (HFE), and Sex-linked anemia (Hephaestin). Iron regulatory proteins (IRP-1 and IRP-2) are cytoplasmic mRNA-binding proteins that control intracellular iron levels by regulating the translation of ferritin, Tfrs, and other proteins congaing iron-responsive element (IRE) located at the 5-UTR. IRP binds to IREs with high affinity in situation of iron starvation. Binding of IRP to IRE of ferritin represses its transcription. However, when cells are iron replete, IRPs lose their capacity to bind IREs, allowing efficient translation of ferritin and reducing Tfr mRNA half-life. Although IRP1 and IRP-2 share significant protein sequence homology, they differ in tissue distribution and mode of regulation. IRP-1, also known as IRE-BP-1/aconitase/citrate hydrolyase/ferritin repressor protein, (mouse/rat/human 889 aa, chromosome 9, ~98kD) also posses aconitase activity and highly homologous with mitochondrial aconitase. IRP-1 is more abundant than IRP-2 and it is widely expressed. IRP-2/IRE-BP2 (rat/human 963 aa) is relatively less abundant than IRP-1 and lacks aconitase activity. It has a unique 73-aa insertion in the N-terminus. In the presence of high iron levels, IRP-2 is rapidly targeted to proteasome-mediated degradation. Although, both IRPs bind the consensus IREs, it is also shown that IRP-2 can recognize an exclusive IRE subset.
Reinheit:
Highly purified
Formulierung:
Supplied as a liquid in PBS, pH 7.2
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