Recombinant Proteins

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EEF1E1 Human

Eukaryotic Translation Elongation Factor 1 Epsilon 1 Human Recombinant

EEF1E1, as produced in E. coli, is a single polypeptide chain that is not glycosylated. It contains 194 amino acids (specifically, amino acids 1 through 174) and has a molecular weight of 21.9 kDa.
A 20 amino acid His-tag is fused to the N-terminus of EEF1E1. Purification is achieved using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT3744
Source
Escherichia Coli.
Appearance
A colorless solution that has been sterile filtered.

EEF1G Human

Eukaryotic Translation Elongation Factor 1 Gamma Human Recombinant

EEF1G Human Recombinant, produced in E.coli, is a single, non-glycosylated polypeptide chain consisting of 460 amino acids (1-437) and possessing a molecular mass of 52.5 kDa. A 23 amino acid His-Tag is fused to the N-terminus of EEF1G, and the protein is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT3801
Source
E.coli.
Appearance
A clear, sterile-filtered solution.

EEF2 Human

Eukaryotic Translation Elongation Factor 2 Human Recombinant

Recombinant human EEF2, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 308 amino acids (residues 574-858) with a molecular weight of 34.3 kDa. This EEF2 variant is fused to a 23 amino acid His-Tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3874
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

EIF3J Human

Eukaryotic Translation Initiation Factor 3J Human Recombinant

This product is a highly purified form of the human EIF3J protein. It has been produced in a laboratory setting using E. coli bacteria. The protein is a single chain of 210 amino acids and includes a His-tag, which is a short sequence of amino acids that allows for easy purification. The protein is provided in a solution that is suitable for storage and use in various research applications.
Shipped with Ice Packs
Cat. No.
BT4701
Source
Escherichia Coli.
Appearance
Clear and colorless solution that has been sterilized by filtration.

EIF4EBP1 Human

Eukaryotic translation initiation factor 4E-binding protein 1 Human Recombinant

Recombinant human EIF4EBP1, expressed in E. coli, is engineered with a 20-amino acid His tag at the N-terminus. This non-glycosylated polypeptide consists of 138 amino acids, including the 118 amino acids of the EIF4EBP1 sequence. It has a molecular mass of 14.7 kDa, though it appears larger on SDS-PAGE. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5097
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterilized by filtration.

EIF4EBP2 Human

Eukaryotic Translation Initiation Factor 4E-Binding Protein 2 Human Recombinant

This product consists of a single, non-glycosylated polypeptide chain of EIF4EBP2, comprising 140 amino acids (1-120a.a.) with a molecular weight of 15.1 kDa. Produced in E. coli, the EIF4EBP2 protein is fused to a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5175
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized through filtration.

EIF4EBP3 Human

Eukaryotic Translation Initiation Factor 4E-Binding Protein 3 Human Recombinant

Recombinant human EIF4EBP3 protein was produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 123 amino acids (amino acids 1-100 of the EIF4EBP3 sequence plus a 23 amino acid His-tag at the N-terminus) and has a molecular mass of 13.3 kDa. The protein was purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5238
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.

EIF4H Human

Eukaryotic Translation Initiation Factor 4H Human Recombinant

This product consists of a recombinant human EIF4H protein produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 272 amino acids, including a 24-amino acid His-tag fused to the N-terminus. With a molecular weight of 29.9 kDa, the protein is purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT5304
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

EIF5A Human

Eukaryotic Translation Initiation Factor 5A Human Recombinant

Produced in E. coli, our EIF5A is a single, non-glycosylated polypeptide chain composed of 154 amino acids with a molecular weight of 16.8 kDa. It undergoes rigorous purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5401
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
Definition and Classification

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 .

Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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.

Regulatory Mechanisms

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 .

Applications

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 .

Role in the Life Cycle

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 .

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