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anti-Mouse (Murine) Aconitase 1 Antibodies:
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Human Polyclonal Aconitase 1 Primary Antibody for IP, WB - ABIN947527
Rupani, Connell: Transferrin receptor mRNA interactions contributing to iron homeostasis. in RNA (New York, N.Y.) 2016
Arabidopsis thaliana Polyclonal Aconitase 1 Primary Antibody for WB - ABIN488534
Bernard, Cheng, Zhao, Balk: An allelic mutant series of ATM3 reveals its key role in the biogenesis of cytosolic iron-sulfur proteins in Arabidopsis. in Plant physiology 2009
Show all 4 Pubmed References
Human Monoclonal Aconitase 1 Primary Antibody for IP, ELISA - ABIN559748
Reuter, Reiermann, Wörner, Schröter, Edemir, Buck, Henning, Peter-Katalinic, Vollenbröker, Amann, Pavenstädt, Schlatter, Gabriëls: IF/TA-related metabolic changes--proteome analysis of rat renal allografts. in Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association 2010
Iron increases turnover of ACO1 in kidney cells, while increasing aconitase activity, suggesting that the apoprotein (aconitase-inactive) form is not exclusively responsible for turnover.
ACO1 gene expression in tomato leaf petioles and vascular localisation of ACO1 protein.
IL-6 likely up-regulates IRP1 and DMT1 expression and down-regulates FPN1 expression in BV2 microglial cells through JNK signaling pathways
Using whole RNA sequencing of bone marrow cells in iron-overloaded mice, it was observed that Idh1 and Aco1, enzymes involved in the TCA cycle, were elevated.
The Irp1-/- mice develop polycythemia and pulmonary hypertension, and suggesting that Irp1 plays an essential role in erythropoiesis and in the pulmonary and cardiovascular systems.
IRP1 and IRP2 mutant mice rapidly succumb to systemic infection with Salmonella Typhimurium, a pathogenic bacterium that multiplies within macrophages, with increased bacterial burdens in liver and spleen.
results uncover an unexpected protective role of IRP1 in pathological conditions associated with altered Fe-S metabolism
Aco1 KD in fully differentiated 3T3-L1 adipocytes decreased lipogenic, Idh1, Adipoq, and Glut4 gene expression.
impaired mitochondrial [Fe-S] cluster biogenesis in Mfrn1(gt/gt) cells results in elevated IRP1 RNA-binding that attenuates ALAS2 mRNA translation and protoporphyrin accumulation
Data indicate that JTR-009, a benzimidazole, operated by preventing iron-regulatory protein-1 (IRP1) from binding to the iron-responsive element (IRE) in APP mRNA.
Human ACO1 is a moonlighting protein that has both aconitase enzyme activity as well as an mRNA binding function.
Aco1 is a moonlighting protein that has aconitase activity as well as mRNA binding ability.
IRP1 is the principal regulator of HIF2alpha mRNA translation
Irp1 deletion enhanced HIF2alpha protein expression in kidneys of Irp1(-/-) mice.
These results uncover separable physiological roles of each IRP and identify IRP1 as a therapeutic target for manipulating HIF-2alpha action in hematologic, oncologic, and other disorders.
The RNA-binding and aconitase forms of IRP-1 can undergo interconversion dependent on the density of cells growing in culture.
aconitase functions as a licensing factor in ERK-dependent proliferation and differentiation, thereby providing a regulatory input for iron in EPO-dependent erythropoiesis.
A wide network of mRNAs and proteins with iron-dependent regulation, IRP-dependent regulation, or both.
Iron regulatory protein 1 outcompetes iron regulatory protein 2 in regulating cellular iron homeostasis in response to nitric oxide.
Mice lacking both IRP1 in their hepatocytes suffer from mitochondrial iron deficiency and dysfunction associated with alterations of the ISC and heme biosynthetic pathways, leading to liver failure and death.
Iron regulatory protein-1 (Irp1)/aconitase activities studied in macrophages grown under control conditions or subjected to iron starvation or supplementation show that Irp1 is activated by direct disassembly of the Fe-S cluster of cytoplasmic aconitase.
A comparative study of the roles of iron regulatory proteins 1 and 2 in regulating iron metabolism.
These results support the concept that IRP1 is an oxidative stress biosensor that mediates iron accumulation and cell death when deregulated by mitochondrial dysfunction.
Results indicate that there is a dysregulation of DMT1 + IRE in IA testes, which might due to the up-regulation of IRP1 and HIF-1A.
Evaluation of the iron regulatory protein-1 interactome has been presented.
regulatory circuit involving FBXL5 and CIA acts through both IRPs to control iron metabolism and promote optimal cell growth
Data suggest that Fe-S cluster of IRP1 plays role in sensing/regulating cellular iron homeostasis; IRP1 alternates between function as cytosolic aconitase [which contains Fe(4)-S(4) cluster in active-site cleft] and function as apoenzyme [which lacks Fe-S cluster] that binds to iron response element stem-loop structures present in several iron regulatory protein transcripts. [REVIEW]
The SNP rs7874815 in the ACO1 gene was strongly associated with survival in pancreatic cancer.
Our results confirm the observation that mitoNEET is important in transferring the iron sulfur clusters to the cytosolic aconitase in living cells and the His-87 ligand in mitoNEET plays important role in this process.
Data show that IRP1 suppressed TfR1/DMT1 (+IRE) expression, limited the cellular iron content and decreased lactate dehydrogenase (LDH) release induced by hypoxia.
These in vitro studies suggest that human GLRX3 is important for cytosolic Fe-S protein maturation.
SIRT3 overexpression decreases TfR1 expression by inhibiting IRP1 and represses proliferation in pancreatic cancer cells.
ACO1 gene expression was positively associated with adipogenic markers in subcutaneous and visceral adipose tissue.
ACO1 genetic variation is associated with neuropathic pain and pain severity in HIV-infected patients on antiretroviral therapy
MitoNEET governs a novel trafficking pathway to rebuild an Fe-S cluster into cytosolic aconitase/IRP1.
Polymer-dependent translocation of IRP-1 in Cd(2+)-exposed cells may underlie effects of Cd(2+) on iron homeostasis.
Aco1 encodes a moonlighting protein that has aconitase activity as well as mRNA binding ability.
Data indicate that silencing of Grx3 in HeLa cells decreases the activities of several cytosolic Fe/S proteins, including iron-regulatory protein 1, a major component of posttranscriptional iron regulation.
Studies indicate that several genes have been linked to iron homeostasis, including transferrin (TF), iron regulatory protein 1 (ACO1) and transferrin receptor 2 (TFR2).
Lead specifically induces dysregulation of IRP1 protein by activating the ERK1/2 signaling pathway indicating a novel role for IRP1 and the ERK/MAPK pathway in vascular endothelial functions.
Even though the base-specific RNA-binding residues are not part of the aconitase active site, their substitutions can affect the aconitase activity of holo-IRP1, positively or negatively.
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.
aconitase 1, soluble
, cytoplasmic aconitate hydratase
, iron regulatory protein 1
, aconitase 1-like
, 1-Aminocyclopropane-1-carboxylic acid oxidase
, ACC oxidase 1
, ethylene-forming enzyme
, protein pTOM 13
, IRE-BP 1
, citrate hydro-lyase
, cytoplasmic aconitase
, iron-responsive element-binding protein 1
, IRE-binding protein 1
, Iron responsive element binding protein
, aconitate hydratase, cytoplasmic
, ferritin repressor protein
, iron-responsive element binding protein 1