Recombinant Proteins
Product List
EIF4A3 Human
Eukaryotic Translation Initiation Factor 4A3 Human Recombinant
EIF4A3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
EIF4E Human
Eukaryotic Translation Initiation Factor 4E Human Recombinant
EIF4E Mouse
Eukaryotic Translation Initiation Factor 4E Recombinant Mouse
EIF4E Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 241 amino acids (1-217 a.a) and having a molecular mass of 27.6kDa. EIF4E is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
EIF4EBP1 Human
Eukaryotic translation initiation factor 4E-binding protein 1 Human Recombinant
The EIF4EBP1 is purified by proprietary chromatographic techniques.
EIF4EBP2 Human
Eukaryotic Translation Initiation Factor 4E-Binding Protein 2 Human Recombinant
EIF4EBP2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
EIF4EBP3 Human
Eukaryotic Translation Initiation Factor 4E-Binding Protein 3 Human Recombinant
EIF4EBP3 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
EIF4H Human
Eukaryotic Translation Initiation Factor 4H Human Recombinant
EIF4H is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
EIF5A Human
Eukaryotic Translation Initiation Factor 5A Human Recombinant
EIF5A2 Human
Eukaryotic Translation Initiation Factor 5A2 Human Recombinant
Introduction
Eukaryotic Translation Initiation Factors (eIFs) are proteins or protein complexes that play a crucial role in the initiation phase of eukaryotic translation. They help stabilize the formation of ribosomal preinitiation complexes around the start codon and are essential for post-transcription gene regulation . There are at least twelve eukaryotic initiation factors, each composed of multiple polypeptides, reflecting the complexity of eukaryotic translation .
Key Biological Properties: eIFs are involved in the formation of the 43S preinitiation complex (PIC), which includes the small 40S ribosomal subunit and Met-tRNAiMet . They also participate in the recruitment of the 43S PIC to the mRNA’s 5’ cap structure, facilitating the scanning process to locate the start codon .
Expression Patterns and Tissue Distribution: The expression of eIFs varies across different tissues and developmental stages. For instance, eIF2 is ubiquitously expressed and plays a critical role in delivering the initiator tRNA to the ribosome . The expression levels of eIFs can be influenced by various physiological and pathological conditions, including stress and cancer .
Primary Biological Functions: eIFs are fundamental for the translation of mRNA into proteins. They regulate the initiation phase of translation, which is the rate-limiting step of protein synthesis .
Role in Immune Responses and Pathogen Recognition: eIFs are involved in the immune response by regulating the translation of proteins essential for pathogen recognition and immune signaling . For example, eIF2α phosphorylation is a key regulatory mechanism during stress responses, including viral infections .
Mechanisms with Other Molecules and Cells: eIFs interact with various molecules, including ribosomal subunits, mRNA, and other initiation factors. For instance, eIF4E binds to the 5’ cap of mRNA, while eIF4G acts as a scaffold for the assembly of the translation initiation complex .
Binding Partners and Downstream Signaling Cascades: eIFs are regulated by several signaling pathways, such as the mTOR and MAPK pathways, which influence their activity and availability . These interactions are crucial for the proper initiation of translation and subsequent protein synthesis.
Transcriptional Regulation: The expression of eIFs is controlled at the transcriptional level by various transcription factors and signaling pathways .
Post-Translational Modifications: eIFs undergo several post-translational modifications, including phosphorylation, which can alter their activity and interactions. For example, phosphorylation of eIF2α inhibits its function, leading to a reduction in global protein synthesis during stress conditions .
Biomedical Research: eIFs are studied extensively in cancer research due to their role in regulating protein synthesis and cell growth .
Diagnostic Tools: Abnormal expression or activity of eIFs can serve as biomarkers for various diseases, including cancer and neurodevelopmental disorders .
Therapeutic Strategies: Targeting eIFs with specific inhibitors or modulators is a promising approach for developing new cancer therapies .
Development to Aging and Disease: eIFs play a critical role throughout the life cycle, from embryonic development to aging. They are involved in various cellular processes, including cell growth, differentiation, and response to environmental stress . Dysregulation of eIFs is associated with several diseases, including cancer, neurodegenerative disorders, and metabolic diseases .
