Recombinant Proteins
Product List
AGO2 (1-200) Human
Argonaute 2 (1-200 a.a.) Human Recombinant
AGO2 (1-200) Human Recombinant is a single, non-glycosylated, polypeptide chain containing 210 amino acids (1-200 a.a) and having a molecular mass of 23.7kDa (calculated). AGO2 (1-200) is fused to a 10 a.a His tag at N-terminal.
AGO2 Human
Argonaute 2 Human Recombinant
AGO2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 1-859) containing 869 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 98.4kDa (calculated).
EEF1A1 Human
Eukaryotic Translation Elongation Factor 1 Alpha 1 Human Recombinant
EEF1B2 Human
Eukaryotic Translation Elongation Factor 1 Beta 2 Human Recombinant
EEF1B2 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 233 amino acids (1-225 a.a.) and having a molecular mass of 25.8kDa. The EEF1B2 is purified by proprietary chromatographic techniques.
EEF1D Human
Eukaryotic Translation Elongation Factor 1 Delta Human Recombinant
EEF1D Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 301 amino acids (1-281 a.a.) and having a molecular mass of 33.2kDa (Molecular weight on SDS-PAGE will appear higher). The EEF1D is purified by proprietary chromatographic techniques.
EEF1E1 Human
Eukaryotic Translation Elongation Factor 1 Epsilon 1 Human Recombinant
EEF1E1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 194 amino acids (1-174 a.a.) and having a molecular mass of 21.9kDa.
EEF1E1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
EEF1G Human
Eukaryotic Translation Elongation Factor 1 Gamma Human Recombinant
EEF1G is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
EEF2 Human
Eukaryotic Translation Elongation Factor 2 Human Recombinant
EEF2 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
EEF2K Human
Eukaryotic Elongation Factor-2 Kinase Human Recombinant
EIF1 Human
Eukaryotic Translation Initiation Factor 1 Human Recombinant
The EIF1 is fused to 37 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
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 .
