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AB101821

Recombinant Human AUH protein

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Recombinant Human AUH protein is a Human Full Length protein, in the 68 to 339 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

3-MG-CoA hydratase, AU-specific RNA-binding enoyl-CoA hydratase, Itaconyl-CoA hydratase, AU-binding protein/enoyl-CoA hydratase, AUH

1 Images
SDS-PAGE - Recombinant Human AUH protein (AB101821)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human AUH protein (AB101821)

SDS-PAGE of ab101821 (3µg) under reducing condition and visualized by coomassie blue stain.

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

Q13825

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMSSEMKTEDELRVRHLEEENRGIVVLGINRAYGKNSLSKNLIKMLSKAVDALKSDKKVRTIIIRSEVPGIFCAGADLKERAKMSSSEVGPFVSKIRAVINDIANLPVPTIAAIDGLALGGGLELALACDIRVAASSAKMGLVETKLAIIPGGGGTQRLPRAIGMSLAKELIFSARVLDGKEAKAVGLISHVLEQNQEGDAAYRKALDLAREFLPQGPVAMRVAKLAINQGMEVDLVTGLAIEEACYAQTIPTKDRLEGLLAFKEKRPPRYKGE","proteinLength":"Full Length","predictedMolecularWeight":"31.4 kDa","actualMolecularWeight":null,"aminoAcidEnd":339,"aminoAcidStart":68,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q13825","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

AUH also known as AU-specific RNA binding protein/enoyl-CoA hydratase is a bifunctional protein with a molecular mass of approximately 39 kDa. It plays an important role in RNA binding and hydratase activities. AUH is expressed in many tissues including liver brain and heart providing its multiple functional capacities within cells. It binds to AU-rich elements present in mRNA which has significant influence on mRNA stability and turnover. The protein also acts as an enoyl-CoA hydratase involved in the leucine catabolic process.
Biological function summary

The AUH protein is involved in regulating the stability of mRNA by binding to AU-rich elements. This activity is critical for controlling genes expression as it modulates the decay rate of various mRNAs involved in cellular responses. While AUH functions largely independently it may interact with other proteins transiently to exert its RNA binding activity although it is not a part of a stable protein complex. Its hydratase function contributes to the breaking down of leucine an essential amino acid further highlighting its multifaceted biological roles.

Pathways

AUH is interwoven with essential metabolic and gene expression pathways. The protein aligns heavily within the leucine catabolism pathway contributing to the conversion of leucine to acetoacetate and acetyl-CoA which are key intermediates in energy production. AUH's involvement in mRNA decay processes connects it to pathways regulating apoptosis and proliferation where precise control of mRNA turnover by AUH and its related proteins like HuR is essential for cellular outcome.

AUH is linked to a rare genetic disorder known as 3-Methylglutaconic aciduria type 1 (MGA-1) characterized by metabolic anomalies manifesting due to defective leucine catabolism. Mutations in the AUH gene disrupt normal protein function leading to accumulation of metabolic intermediates. Furthermore AUH's role in mRNA regulation implies a connection to cancer where altered expression or mutation might contribute to disruptions in gene expression control. Associated proteins in these contexts include components of the mRNA decay pathway and enzymes involved in amino acid metabolism.
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Specifications

Form

Liquid

Additional notes

ab101821 was purified using conventional chromatography.

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General info

Function

Catalyzes the fifth step in the leucine degradation pathway, the reversible hydration of 3-methylglutaconyl-CoA (3-MG-CoA) to 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) (PubMed : 11738050, PubMed : 12434311, PubMed : 12655555, PubMed : 16640564). Can catalyze the reverse reaction but at a much lower rate in vitro (PubMed : 16640564). HMG-CoA is then quickly degraded by another enzyme (such as HMG-CoA lyase) to give acetyl-CoA and acetoacetate (PubMed : 16640564). Uses other substrates such as (2E)-glutaconyl-CoA efficiently in vitro, and to a lesser extent 3-methylcrotonyl-CoA (3-methyl-(2E)-butenoyl-CoA), crotonyl-CoA ((2E)-butenoyl-CoA) and 3-hydroxybutanoyl-CoA (the missing carboxylate reduces affinity to the active site) (PubMed : 16640564). Originally it was identified as an RNA-binding protein as it binds to AU-rich elements (AREs) in vitro (PubMed : 7892223). AREs direct rapid RNA degradation and mRNA deadenylation (PubMed : 7892223). Might have itaconyl-CoA hydratase activity, converting itaconyl-CoA into citramalyl-CoA in the C5-dicarboxylate catabolism pathway (PubMed : 29056341). The C5-dicarboxylate catabolism pathway is required to detoxify itaconate, an antimicrobial metabolite and immunomodulator produced by macrophages during certain infections, that can act as a vitamin B12-poisoning metabolite (PubMed : 29056341).

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Subcellular localisation

Mitochondrion

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Product protocols

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Target data

Catalyzes the fifth step in the leucine degradation pathway, the reversible hydration of 3-methylglutaconyl-CoA (3-MG-CoA) to 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) (PubMed : 11738050, PubMed : 12434311, PubMed : 12655555, PubMed : 16640564). Can catalyze the reverse reaction but at a much lower rate in vitro (PubMed : 16640564). HMG-CoA is then quickly degraded by another enzyme (such as HMG-CoA lyase) to give acetyl-CoA and acetoacetate (PubMed : 16640564). Uses other substrates such as (2E)-glutaconyl-CoA efficiently in vitro, and to a lesser extent 3-methylcrotonyl-CoA (3-methyl-(2E)-butenoyl-CoA), crotonyl-CoA ((2E)-butenoyl-CoA) and 3-hydroxybutanoyl-CoA (the missing carboxylate reduces affinity to the active site) (PubMed : 16640564). Originally it was identified as an RNA-binding protein as it binds to AU-rich elements (AREs) in vitro (PubMed : 7892223). AREs direct rapid RNA degradation and mRNA deadenylation (PubMed : 7892223). Might have itaconyl-CoA hydratase activity, converting itaconyl-CoA into citramalyl-CoA in the C5-dicarboxylate catabolism pathway (PubMed : 29056341). The C5-dicarboxylate catabolism pathway is required to detoxify itaconate, an antimicrobial metabolite and immunomodulator produced by macrophages during certain infections, that can act as a vitamin B12-poisoning metabolite (PubMed : 29056341).
See full target information Methylglutaconyl-CoA hydratase, mitochondrial
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