Anti-EEF1A1 antibody (325-338 aa) [R04-3H4] (STJA0012354)

SPECIFICATIONS
ClonalityMonoclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
ImmunogenA synthetic peptide of human eEF1A1/EF-Tu
STJA0012354-100
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General Information

Short DescriptionRabbit monoclonal anti-Elongation Factor 1A1 (325-338 aa) for use in WB, IHC-F, IHC-P, ICC and IF in Human and Rat samples. Datasheet included with dilution recommendations, and related reagents.
ApplicationsWB/IHC-F/IHC-P/ICC/IF
HostRabbit
ReactivityHuman/Rat
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

ClonalityMonoclonal
Clone IDR04-3H4
IsotypeIgG
ConjugationUnconjugated
Concentration0.3 mg/mL
PurificationAffinity Purified
Dilution RangeWB 1:500-1:1000
IHC 1:50-1:100
IF 1:50-1:200
Formulation50mM Tris-Glycine (pH7.4) , 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
Storage InstructionStore at 4°C short term. Aliquot and store at-20°C long term. Avoid freeze/thaw cycles.

Target Information

Gene SymbolEEF1A1
Gene ID1915
Uniprot IDEF1A1_HUMAN
ImmunogenA synthetic peptide of human eEF1A1/EF-Tu
Immunogen Region325-338 aa

Additional Info

Post Translational Modifications ISGylated. Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2. Phosphorylation by TGFBR1 inhibits translation elongation. Trimethylated at Lys-79 by EEF1AKMT1. Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation. Trimethylated at Lys-318 by EEF1AKMT2. Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4.trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs. Trimethylated at Gly-2 by METTL13. Mono- and dimethylated at Lys-55 by METTL13.dimethylated form is predominant. Ubiquitinated at Lys-385 by RNF14 in response to ribosome collisions (ribosome stalling), leading to its degradation by the proteasome and rescue of stalled ribosomes.
Function Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis. Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome. The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation. Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1. Also plays a role in cytoskeleton organization by promoting actin bundling. (Microbial infection) Required for the translation of viral proteins and viral replication during human coronavirus SARS-CoV-2 infection.
Protein Name Elongation Factor 1-Alpha 1
Ef-1-Alpha-1
Elongation Factor Tu
Ef-Tu
Eukaryotic Elongation Factor 1 A-1
Eef1a-1
Leukocyte Receptor Cluster Member 7
Database Links Reactome: R-HSA-156842
Reactome: R-HSA-156902
Reactome: R-HSA-3371511
Reactome: R-HSA-6798695
Reactome: R-HSA-8876725
Reactome: R-HSA-9613829
Reactome: R-HSA-9735869
Cellular Localisation Cytoplasm
Nucleus
Nucleolus
Cell Membrane
Colocalizes With Dlc1 At Actin-Rich Regions In The Cell Periphery
Translocates Together With Zpr1 From The Cytoplasm To The Nucleus And Nucleolus After Treatment With Mitogens
Localization At The Cell Membrane Depends On Eef1a1 Phosphorylation Status And The Presence Of Ppp1r16b
Alternative Antibody Names Anti-Elongation Factor 1-Alpha 1 antibody
Anti-Ef-1-Alpha-1 antibody
Anti-Elongation Factor Tu antibody
Anti-Ef-Tu antibody
Anti-Eukaryotic Elongation Factor 1 A-1 antibody
Anti-Eef1a-1 antibody
Anti-Leukocyte Receptor Cluster Member 7 antibody
Anti-EEF1A1 antibody
Anti-EEF1A antibody
Anti-EF1A antibody
Anti-LENG7 antibody

Information sourced from Uniprot.org

Citations

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