Aconitate Hydratase 1 (ACO1) Peptide
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Description
Aconitate Hydratase 1 (ACO1) Peptide is a synthetic peptide. This peptide is used in the production of
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Aconitate Hydratase 1 (ACO1) |
| Host | Synthetic |
| Assay Type | Activity: Not tested. Sequence Fragment: Internal region: C-QVDFNRRADSLQKNQ |
| Recommended Dilution | BL (predicted): 0.5 mg/ml. Optimal dilutions/concentrations should be determined by the end user. |
| Conjugation | Unconjugated |
| Size 1 | 100 µg |
| Form | Lyophilized |
| Tested Applications | P-ELISA |
| Buffer | Prior to lyophilization: Deionized water. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20 °C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| Gene ID | 48, 11428, 50655 |
| NCBI Accession | NP_002188.1 |
| Alias | IRP1,ACONS,HEL60,IREB1,IREBP,IREBP1 |
| Background | Protein ACO1 |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. Reconstitute in deionized water. |
Descripción
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The protein encoded by this gene is a bifunctional, cytosolic protein that functions as an essential enzyme in the TCA cycle and interacts with mRNA to control the levels of iron inside cells. When cellular iron levels are high, this protein binds to a 4Fe-4S cluster and functions as an aconitase. Aconitases are iron-sulfur proteins that function to catalyze the conversion of citrate to isocitrate. When cellular iron levels are low, the protein binds to iron-responsive elements (IREs), which are stem-loop structures found in the 5' UTR of ferritin mRNA, and in the 3' UTR of transferrin receptor mRNA. When the protein binds to IRE, it results in repression of translation of ferritin mRNA, and inhibition of degradation of the otherwise rapidly degraded transferrin receptor mRNA. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Alternative splicing results in multiple transcript variants
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