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EIF4A1 Monoclonal Antibody, PE-Cy5 Conjugated

Product Specifications

Background

Translation initiation in eukaryotes necessitates the assembly of an 80S ribosomal complex. Eukaryotic initiation factors (eIFs) are utilized in a sequence of reactions that leads to 80S ribosomal assembly and initiation of translation. Mammalian eukaryotic translation initiation factor 4F (eIF4F) is a protein complex that contains eIF4A, eIF4E and eIF4G, binds mRNA at a 5?cap motif and recruits the 43S ribosomal preinitiation complex to the eligible transcript. Along with eIF4B, the eIF4F complex mediates the unwinding of mRNA secondary structure to facilitate ribosome association. eIF4E specifically interacts with the 5?cap, eIF4A (I, II) are bidirectional RNA helicases, and eIF4G (I, II) are scaffolding proteins which coordinate eIF4E, eIF4A, eIF3 and the 40S ribosome. Human eIF4AI (eIF4A, DDX2A) is a 406 amino acid protein that is 92.7% homologous to mouse eIF4AI. The promoter region of human eIF4A1 contains TATA and CAAT motifs and consensus binding sites to Sp1 and AP2.

Synonyms

ATP-dependent RNA helicase eIF4A-1; DDX2; DDX2A; eIF 4A I; eIF-4A-I; EIF4A; eIF4A I; eIF4A-I; EIF4A1; Eukaryotic initiation factor 4A-I; Eukaryotic initiation factor 4AI; eukaryotic translation initiation factor 4A, isoform 1; Eukaryotic translation initiation factor 4A1; IF4A1_HUMAN.

Gene ID

1973

Swiss Prot

P60842

Cellular Locus

Cytoplasm, Extracellular matrix

Host

Mouse

Cross Reactivity

Human, Mouse, Rat

Target

EIF4A1

Clonality

Monoclonal

Isotype

IgG

Clone

1B8

Conjugation

PE-Cy5

Source

KLH conjugated synthetic peptide derived from human eIF4A1

Applications

WB

Purification

Purified by Protein A.

Excitation Emission

488nm/670nm

Concentration

1µg/µl

Dilution

WB (1:300-5000)

Buffer

Aqueous buffered solution containing 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Modification

Unmodified

Storage Conditions

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

Gene ID URL

1973

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