ACO1 Blocking Peptide (N-Term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P21399 |
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Other Accession | Q01059, Q63270 |
Gene ID | 48 |
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Other Names | Cytoplasmic aconitate hydratase, Aconitase, 4.2.1.3, Citrate hydro-lyase, Ferritin repressor protein, Iron regulatory protein 1, IRP1, Iron-responsive element-binding protein 1, IRE-BP 1, ACO1, IREB1 |
Target/Specificity | The synthetic peptide sequence is selected from aa 144-155 of HUMAN ACO1 |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | ACO1 |
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Synonyms | IREB1 |
Function | Bifunctional iron sensor that switches between 2 activities depending on iron availability (PubMed:1946430, PubMed:1281544, PubMed:8041788). Iron deprivation, promotes its mRNA binding activity through which it regulates the expression of genes involved in iron uptake, sequestration and utilization (PubMed:1946430, PubMed:1281544, PubMed:8041788, PubMed:23891004). Binds to iron-responsive elements (IRES) in the untranslated region of target mRNAs preventing for instance the translation of ferritin and aminolevulinic acid synthase and stabilizing the transferrin receptor mRNA (PubMed:1946430, PubMed:1281544, PubMed:8041788, PubMed:23891004). |
Cellular Location | Cytoplasm, cytosol. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding.
References
Hirling H.,et al.Nucleic Acids Res. 20:33-39(1992).
Humphray S.J.,et al.Nature 429:369-374(2004).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Rouault T.A.,et al.Proc. Natl. Acad. Sci. U.S.A. 87:7958-7962(1990).
Hentze M.W.,et al.Nucleic Acids Res. 19:1739-1740(1991).
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