AIMP2 Protein, Human (His)
AIMP2 Protein, Human (His) plays a primary role in the initiation of α-synuclein (aSyn) aggregation.
- Species: Human
- Source: E. coli
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Biological Activity
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Product Properties
- Documentation
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Biological Activity
AIMP2 Protein, Human (His) plays a primary role in the initiation of α-synuclein (aSyn) aggregation.
Aminoacyl-tRNA synthetase complex interacting multifunctional protein-2 (AIMP2), which has been reported to cause selective and age-dependent degeneration of dopaminergic neurons, plays an essential role in the initiation of aSyn fibrillization and LB formation. AIMP2 first self-assembles to form amyloid-like aggregates, which interact with monomeric aSyn and induce its fibrillization in vitro as well as the formation of aSyn fibrils and LB-like inclusions in various well-established cellular and animal models of synucleinopathies. AIMP2 is part of the multiaminoacyl-tRNA synthetase complex, where it acts as a scaffold subunit to stabilize the whole complex. This complex plays a pivotal role in protein biosynthesis by catalyzing the esterification of amino acids with their corresponding tRNA. In this regard, its function suggests that it possess multiple protein-protein interaction surfaces[1].
Technical Parameters
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Species Human
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Source E. coli
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Tag N-His
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Accession
Q13155 (M1-K320)
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Molecular Construction
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N-term
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His
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AIMP2 (M1-K320)
Accession # Q13155 -
C-term
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Protein Length
Full Length
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Synonyms
AIMP2; JTV-1; Aminoacyl TRNA Synthetase Complex Interacting Multifunctional Protein 2; P38; JTV1; Multisynthetase Complex Auxiliary Component P38; Aminoacyl TRNA Synthase Complex-Interacting Multifunctional Protein 2; PRO0992; Multisynthase Complex Auxili
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AA Sequence
MPMYQVKPYHGGGAPLRVELPTCMYRLPNVHGRSYGPAPGAGHVQEESNLSLQALESRQDDILKRLYELKAAVDGLSKMIQTPDADLDVTNIIQADEPTTLTTNALDLNSVLGKDYGALKDIVINANPASPPLSLLVLHRLLCEHFRVLSTVHTHSSVKSVPENLLKCFGEQNKKQPRQDYQLGFTLIWKNVPKTQMKFSIQTMCPIEGEGNIARFLFSLFGQKHNAVNATLIDSWVDIAIFQLKEGSSKEKAAVFRSMNSALGKSPWLAGNELTVADVVLWSVLQQIGGCSVTVPANVQRWMRSCENLAPFNTALKLLK
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Predicted Molecular Mass
39.3 kDa
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Purity
≥ 90%, as determined by reducing SDS-PAGE.
Documentation
References
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
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