EIF4A1 Antibodies

Eukaryotic initiation factor 4A-I (EIF4A1)

ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the present version of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs that's necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.

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Gene Information

Human
Gene Name:	EIF4A1
Uniprot:	P60842
Entrez:	1973

Family

Belongs to:
DEAD box helicase family

Alternative Names

ATP-dependent RNA helicase eIF4A-1; DDX2Aeukaryotic initiation factor 4A-I; EC 3.6.1; EC 3.6.4.13; EIF4A; EIF-4A; eIF-4A-I; eIF4A-I; eukaryotic initiation factor 4AI; eukaryotic translation initiation factor 4A; eukaryotic translation initiation factor 4A, isoform 1; eukaryotic translation initiation factor 4A1

Molecular Weight

Mass (kDA):
46.154 kDA

Genomic Context

Human
Location:	17p13.1
Sequence:	17; NC_000017.11 (7572825..7579006)

Diseases

• Malignant Neoplasms
• Neoplasms
• Neoplasm Metastasis
• Malignant Neoplasm Of Lung
• Cytomegalovirus Infections
• Dental Plaque
• Liver Regeneration Disorder
• Lung Neoplasms
• Non-small Cell Lung Carcinoma
• Stage I Non-small Cell Lung Cancer
• Neurodegenerative Disorders
• Tdp-43 Proteinopathies

• Endometrial Neoplasms
• Endometrial Polyp
• Malignant Neoplasm Of Liver
• Aneuploidy
• Malignant Tumor Of Cervix
• Carcinogenesis
• Carcinoma

Interacting Proteins

• EIF4G1
• EIF4G2
• EIF4H
• PDCD4

Pathways

• Translation
• Localization
• Methylation
• Regulation Of Translation
• Cell Adhesion
• Transport
• Cell Proliferation
• Fertilization
• Hepatocyte Proliferation
• Conjugation
• Nuclear Export
• Regeneration

• Ribosome Biogenesis
• Mrna Transcription
• Poly-a Binding
• Cell Growth
• Wound Healing
• Contact Inhibition

PTMs

• Phosphorylation

• Methylation

• Ubiquitination

Research Areas

• Core ESC-Like Genes
• mTOR Pathway
• Stem Cell Markers

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/EIF4A1

Best Uses Of The EIF4A1 Marker

Steven Boster invented his first product in 1993. This earned him the nickname "he that converts science into the lavatory." Afterward, he developed dozens of products for immunohistochemistry, including hundreds of primary antibodies. Boster was the largest antibody catalog company in China by the late 90s. PicoKine(tm), his proprietary ELISA platform, was also developed by Boster to produce high-sensitivity ELISA kit.

TGEV

The EIF4A1 marker can be used to study the progression of cancer and is an effective anti-inflammatory agent. Song Han, a piglet researcher, found this marker in the stomach. It is also useful for detecting tumor-associated immune cytokines (TAIs).

Lp-1s treatment resulted in an increase in STAT1 phosphorylation after cells were infected with TGEV. It was also positively correlated with the time following TGEV infection. In addition, the Lp-1s-infected group showed lower levels of TGEVN protein expression than the TGEV infection group at all times points. The blank control group however, had no protein expression.

Lp-1s treatment stimulated IFNb production by IPEC-J2 cell. This level reached a peak at 24-hours. Lp-1s pretreated IPEC-J2 cells with Lp-1s inducing high levels IFNb production.

The TGEV treatment increased IFN-b and JAK-STAT1, while Lp-1s reduced the expression of ZAP. Interestingly, TGEV treatment increased MX2 and IFN-b. The ZAP protein level was positively related to the PKR level, while the levels of p-PKR/PKR as well as p-PKR/b–tubulin were not significantly different among the two groups.

eIF4A1

The eIF4A1 genes encode a protein that unwinds secondary structures within the 5'-UTR mRNAs. This enzyme is vital for many biological processes, including reproduction and gene regulation. It is therefore important to determine the best way to use this gene. It is useful for developing new therapeutic strategies and can help to determine the target gene.

Our transfection experiment was performed on pIECs using a six-well plate. We used the optimal siRNA targeting EIF4A1, which was GGAGACTATATGGGAGCAA-3'. Transfection was done according to the manufacturer's instructions using Lipofecatmine (tm) 3000. We used three siRNAs (20 nanoM each) and an intern standard, the bactin gene. The Reed and Muench method was used to measure the TCID50. We used mock-treated cells as controls.

Essential for cell replication is the eIF4A1 Protein. A study of the protein identified seven cellular proteins as partners of TGEV M protein. Seven cellular proteins interact with the TGEV M protein, ranging in their roles in gene transcription, protein folding, and metabolism. This allows us to understand how this virus infects piglets, and what we can do to stop it.

eIF4A unwinds RNA secondary structures

The rate at which eIF4A unwinds a molecule of RNA is closely related to its ATP hydrolysis rate. This is because eIF4A interacts via conformational cycling with the RNA. Two RNAs of different lengths will unwind at different rates. This means that eIF4A could undergo either a productive cycle or a futile one, depending on which is faster.

eIF4A is a canonical helicase with a core made up of two RecA domains. The enzyme exhibits both basic ATPase and RNA-stimulated ATPase functions. Biochemical experiments show that eIF4A acts as a minimal helicase module. However, the exact role of the ATP-dependent activity of eIF4A in translation initiation is still unclear.

eIF4A is capable of catalyzing three types of reactions. Three distinct sets of elements are required for each of the three reactions. The strand b strand and strand s2 are the two most important elements in NS3 helicase construction. The b strand is an addition to the undefined region in electron density around GG motif. The TAT motif can be found in the hinge region between domains II and I.

eIF4A is not necessary for the unwinding RNA second structures in yeast cells but it has been shown how to reduce CDS reactivity. eIF4A also inhibits ribosome occupation, which is crucial for RNA secondary structure. Moreover, ribosome activity has been linked to strong correlation between DMS reactivity, RNA secondary structure, and ribosome occupancy, suggesting that eIF4A may be involved.

This rapid phase is seen in RNAs with a shorter 5'-singlestranded excess. eIF4A in RNAs that have this 5'-single stranded extrahang is in a close conformation. This conformational cycling is characterized by a biphasic pattern. This behavior is most likely caused by qualitative differences between RNA, eIF4A.

Translational initiation requires eIF4A1.

The eIF4F protein is a component. It unwinds the secondary structures of mRNAs, such as the 5'-UTR. It also displays weaker activities than otherRNA helicases. Some reports suggest that eIF4A has both ATPase-dependent and helicase-independent roles during translational initiation.

eIF4A1 also forms part of the eIF4F complex cap-binding complex. This recruits the 40S ribosomal component. It also recruits a scaffolding protein called eIF4G. The scaffolding protein unwinds secondary structures in the 5'-UTR and eIF4A1 initiates transcription by binding RNA.

We performed paired end sequencing using Illumina TruSeqRNA Sample Preparation Kit v2 and SBS Chemistry Version 3. The knockdown samples in total unfractionated DNA were represented by the first four rows and the control samples by the last four rows. The matrices were rearranged to optimize space and identify eIF4A1 siRNAs as well as the corresponding controls for polysomal RNA.

eIF4F1 is a component of eIF4F. However, it also plays a crucial role in malignant progression and transformation. It has been linked to cervical cancer, colorectal carcinoma, and gastric cancer. In these types of cancer, eIF4A1 expression has been associated with poor prognosis. eIF4A1 has also been linked to several KEGG categories, including malignant cell types such as hepatocellular carcinoma, kidney cell cancer, and ovarian carcinoma.

eIF4A1 not only plays a critical role in translational initiation but also plays a pivotal roll in the unwinding the hairpins at mRNA and DNA. The unwinding of hairpins requires a specific subunit, called DHX29. This subunit is capable of unwinding hairpin structures that are more stable, such as those found at the cap. eIF4A can also unwind DNA. It also promotes the formation a polysaccharide ribosomal cleosome.