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AB15506
Sigma-AldrichAnti-Iron Pegulatory Protein 1 Antibody
Anti-Iron Pegulatory Protein 1 Antibody detects level of Iron Pegulatory Protein 1 & has been published & validated for use in ELISA & WB.
More>>Anti-Iron Pegulatory Protein 1 Antibody detects level of Iron Pegulatory Protein 1 & has been published & validated for use in ELISA & WB. Less<<
Anti-Iron Pegulatory Protein 1 Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
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-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.
Anti-Iron Pegulatory Protein 1 Antibody detects level of Iron Pegulatory Protein 1 & has been published & validated for use in ELISA & WB.
Key Applications
ELISA
Western Blotting
Application Notes
Western blot: 1-10 µg/mL using ECL. Immunohistochemistry: Not tested. Recommended testing antibody dilution:2-20 µg/mL ELISA: 1:10,000-1:100,000 using 50-100 ng of control peptide/well. Optimal working dilutions must be determined by end user.
Biological Information
Immunogen
Synthetic peptide near the N-terminus of rat IRP-1.
Host
Rabbit
Specificity
Iron regulatory protein 1 (IRP-1). The immunogen sequence has no significant homology with IRP-2.
Species Reactivity
Rat
Species Reactivity Note
Other species have not yet been tested. The immunogen sequence is 94% conserved in mouse, and 89% in human and rabbit IRP-1.
Aconitase 1, also known as iron regulatory element binding protein 1 (IREB1), is a cytosolic protein which binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5' UTR of ferritin mRNA, and in the 3' UTR of transferrin receptor mRNA. The iron-induced binding to the IRE results in repression of translation of ferritin mRNA, and inhibition of degradation of the otherwise rapidly degrading transferrin receptor mRNA. Thus, IREB1 plays a central role in cellular iron homeostasis. It was also shown to have aconitase activity, and hence grouped with the aconitase family of enzymes.
FUNCTION: SwissProt: P21399 # This protein also expresses aconitase activity. COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity). SIZE: 889 amino acids; 98399 Da SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: SwissProt: P21399 ## Belongs to the aconitase/IPM isomerase family.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Maintain at -20°C in undiluted aliquots for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles.
α -Actinin TvACTN3 of Trichomonas vaginalis is an RNA-binding protein that could participate in its posttranscriptional iron regulatory mechanism. Calla-Choque, JS; Figueroa-Angulo, EE; Ávila-González, L; Arroyo, R BioMed research international
2014
424767
2014
Trichomonas vaginalis is a sexually transmitted flagellated protist parasite responsible for trichomoniasis. This parasite is dependent on high levels of iron, favoring its growth and multiplication. Iron also differentially regulates some trichomonad virulence properties by unknown mechanisms. However, there is evidence to support the existence of gene regulatory mechanisms at the transcriptional and posttranscriptional levels that are mediated by iron concentration in T. vaginalis. Thus, the goal of this study was to identify an RNA-binding protein in T. vaginalis that interacts with the tvcp4 RNA stem-loop structure, which may participate in a posttranscriptional iron regulatory mechanism mediated by RNA-protein interactions. We performed RNA electrophoretic mobility shift assay (REMSA) and supershift, UV cross-linking, Northwestern blot, and western blot (WB) assays using cytoplasmic protein extracts from T. vaginalis with the tvcp4 RNA hairpin structure as a probe. We identified a 135-kDa protein isolated by the UV cross-linking assays as α-actinin 3 (TvACTN3) by MALDI-TOF-MS that was confirmed by LS-MS/MS and de novo sequencing. TvACTN3 is a cytoplasmic protein that specifically binds to hairpin RNA structures from trichomonads and humans when the parasites are grown under iron-depleted conditions. Thus, TvACTN3 could participate in the regulation of gene expression by iron in T. vaginalis through a parallel posttranscriptional mechanism similar to that of the IRE/IRP system.
