Mouse Monoclonal EFTU1 antibody. Suitable for ELISA, WB, ICC/IF and reacts with Escherichia coli samples. Cited in 2 publications. Immunogen corresponding to Cell preparation containing eEF1A1/EF-Tu protein.
Preservative: 0.02% Sodium azide
Constituents: PBS, 0.1% BSA
| ELISA | WB | ICC/IF | |
|---|---|---|---|
| Escherichia coli | Expected | Expected | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Escherichia coli | Dilution info Use at an assay dependent concentration. | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Escherichia coli | Dilution info Use at an assay dependent concentration. | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Escherichia coli | Dilution info Use at an assay dependent concentration. | Notes - |
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This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation. Plays a stimulatory role in trans-translation; binds tmRNA. Protects glycyl-tRNA(Gly) from hydrolysis by E.coli D-aminoacyl-tRNA deacylase (dtd) (By similarity). (Microbial infection) Upon infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex. With EF-Ts may provide a stabilizing scaffold for the beta (catalytic) subunit. Helps separate the double-stranded RNA of the template and growing RNA during elongation. With the beta subunit helps form the exit tunnel for template RNA. (Microbial infection) Required for the tRNase activity of CdiA-CT from E.coli strain EC869; the toxic CT module is thought to cleave tRNA in the context of translationally active GTP EF-Tu-aa-tRNA complexes. GTP is required for tRNase activity but is not hydrolyzed. CdiA-CT is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:28223500). EF-Tu interacts with at least 2 different toxic CT domains, the 2 toxins are different and degrade tRNA at different positions (PubMed:28223500, PubMed:28973472). (Microbial infection) Required for the tRNase activity of CdiA-CT from E.coli strain NC101; the toxic CT module is thought to cleave tRNA in the context of translationally active GTP EF-Tu-aa-tRNA complexes. The toxin may remodel the EF-Tu-aa-tRNA complex to displace the 3'-end of the aa-tRNA so it can enter the toxin active site and be cleaved. GTP is required for tRNase activity but is not hydrolyzed. CdiA-CT is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:28223500). EF-Tu interacts with at least 2 different toxic CT domains, the 2 toxins are different and degrade tRNA at different positions (PubMed:28223500, PubMed:28973472).
b3339, JW3301, tufA, Elongation factor Tu 1, EF-Tu 1, Bacteriophage Q beta RNA-directed RNA polymerase subunit III, P-43
Mouse Monoclonal EFTU1 antibody. Suitable for ELISA, WB, ICC/IF and reacts with Escherichia coli samples. Cited in 2 publications. Immunogen corresponding to Cell preparation containing eEF1A1/EF-Tu protein.
Preservative: 0.02% Sodium azide
Constituents: PBS, 0.1% BSA
Does not recognise eEF1A1/EF-Tu from eukaryotes. Cross reacts with Bacteroides fragilis, Streptococcus oralis, Bacillus subtilis, Pseudomonas aeruginosa, Burkholderia cepacia and Deinococcus sp. A weak cross reaction might also be observed with Mycobacterium tuberculosis.
0.2 µm filtered antibody solution.
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EEF1A1 also known as EF-Tu in prokaryotes functions as an elongation factor in the process of protein synthesis. It facilitates the delivery of aminoacyl-tRNA to the ribosome during the elongation phase of translation. eEF1A1 exhibits a mass of approximately 50 kDa and shows high expression levels in various tissues particularly in the liver and neuronal tissues. It shares functional similarities with EF-G which plays a role in translocation during translation. Moreover eEF1A1 appears relevant in cellular processes beyond translation contributing to its importance across cellular functions.
EEF1A1 acts as an important component in the machinery of protein synthesis and takes part in the elongation factor complex. Within this complex eEF1A1 interacts with other molecules to ensure the accuracy and efficiency of codon-anticodon pairing on the ribosome. Additionally eEF1A1 associates with actin and participates in the cytoskeleton organization. This multifunctional currency of eEF1A1 suggests its involvement in diverse cellular processes beyond classic translation tasks.
The role of eEF1A1 in protein synthesis positions it within the larger context of the mTOR signaling pathway important for cellular growth proliferation and metabolism. Since its function bridges translation initiation and elongation it interacts with proteins like mTOR and S6K1. Within the MAPK pathway eEF1A1 shows interactions influencing cellular survival and apoptosis. These interactions connect eEF1A1 to essential regulatory mechanisms that maintain cellular homeostasis and adaptability.
EEF1A1 exhibits significant involvement in cancer and neurodegenerative diseases. Overexpression or mutation of eEF1A1 frequently associates with various cancers implicating its role in tumor progression and cell proliferation. Interactions with proteins such as p53 link eEF1A1 to pathways that influence tumor suppression and genomic stability. In neurodegenerative conditions like Alzheimer's disease altered eEF1A1 behavior and expression affect neuronal viability and tau protein interaction suggesting its potential contribution to the pathogenesis of these disorders.
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