TRIM2 Protein, Human
Based on 1 Customer Validation
TRIM2, an UBE2D1-dependent E3 ubiquitin-protein ligase, mediates the ubiquitination of NEFL and phosphorylated BCL2L11. Beyond its ligase role, TRIM2 has neuroprotective functions and aids neuronal rapid ischemic tolerance. It crucially participates in antiviral immunity, restricting New World arenavirus infection. This highlights TRIM2's multifaceted involvement in cellular processes beyond ubiquitin-mediated protein degradation. TRIM2 Protein, Human is the recombinant human-derived TRIM2 protein, expressed by E. coli , with tag free.
- Species: Human
- Source: E. coli
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Storage:Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.
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Biological Activity
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Technical Parameters
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Product Properties
- Documentation
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Biological Activity
Description
TRIM2, an UBE2D1-dependent E3 ubiquitin-protein ligase, mediates the ubiquitination of NEFL and phosphorylated BCL2L11. Beyond its ligase role, TRIM2 has neuroprotective functions and aids neuronal rapid ischemic tolerance. It crucially participates in antiviral immunity, restricting New World arenavirus infection. This highlights TRIM2's multifaceted involvement in cellular processes beyond ubiquitin-mediated protein degradation. TRIM2 Protein, Human is the recombinant human-derived TRIM2 protein, expressed by E. coli , with tag free.
Background
TRIM2, an UBE2D1-dependent E3 ubiquitin-protein ligase, serves as a mediator for the ubiquitination of NEFL and phosphorylated BCL2L11. Beyond its role in ubiquitin ligase activity, TRIM2 exhibits a neuroprotective function and may contribute to neuronal rapid ischemic tolerance. Furthermore, it plays a crucial role in antiviral immunity and acts as a restrictor of New World arenavirus infection, emphasizing its multifaceted involvement in cellular processes beyond ubiquitin-mediated protein degradation.
Verified Bioactivity
The ubiquitin conjugating activity of TRIM2 was validated through its ability to catalyse the generation of polyubiquitin chains in the presence of the E1 activating enzyme UBE1, the E2 conjugating enzyme Ubch5b and Bodipyubiquitin. Incubation of TRIM2 for 60 minutes at 37°C in the presence of Bodipy-ubiquitin, UBE1, Ubch5b and ATP was compared alongside two control reactions with either TRIM2 or TRIM2 &ATP excluded from the reaction. Ubiquitin conjugates were identified by the migration of the Bodipy-ubiquitin band and these were observed only in the presence of ATP and TRIM2.
Technical Parameters
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Species Human
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Source E. coli
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Tag Tag Free
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Accession
Q9C040 (A2-Q744)
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Gene ID23321
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Molecular Construction
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N-term
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TRIM2 (A2-Q744)
Accession # Q9C040 -
C-term
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Protein Length
Full Length
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Synonyms
TRIM2; KIAA0517; RNF86; Tripartite motif-containing protein 2; EC 2.3.2.27; E3 ubiquitin-protein ligase TRIM2; RING finger protein 86; RING-type E3 ubiquitin transferase TRIM2; Tripartite Motif-Containing 2; Tripartite Motif Protein TRIM2; RING-Type E3 Ubiquitin Transferase; Charcot-Marie-Tooth Disease, Type 2R; CMT2R; Tripartite Motif Containing 2
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AA Sequence
ASEGTNIPSPVVRQIDKQFLICSICLERYKNPKVLPCLHTFCERCLQNYIPAHSLTLSCPVCRQTSILPEKGVAALQNNFFITNLMDVLQRTPGSNAEESSILETVTAVAAGKPLSCPNHDGNVMEFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQLDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQDFPLHPRENDQLDFIVETEGLKKSIHNLGTILTTNAVASETVATGEGLRQTIIGQPMSVTITTKDKDGELCKTGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLSLRLYDQHIRGSPFKLKVIRSADVSPTTEGVKRRVKSPGSGHVKQKAVKRPASMYSTGKRKENPIEDDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ
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Molecular Weight
Approximately 82 kDa, based on SDS-PAGE under reducing conditions.
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Purity
≥ 85%, as determined by reducing SDS-PAGE.
Product Properties
Solution.
Supplied as a 0.22 μm filtered solution of 50 mM Tris-HCl, pH 7.5, 200 mM NaCl, 20% glycerol, 1 mM DTT.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.
<1 EU/μg, determined by LAL method.
Please use rapid thawing with running water to thaw the protein.
Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.
Shipping with dry ice.
Documentation
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
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