Recombinant Proteins

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AGO2 (1-200) Human

Argonaute 2 (1-200 a.a.) Human Recombinant

This product consists of a single, non-glycosylated polypeptide chain comprising amino acids 1-200 of the human AGO2 protein. It has a molecular weight of 23.7kDa (calculated) and is not glycosylated. A 10 amino acid His tag is fused to the N-terminus of the protein.

Shipped with Ice Packs
Cat. No.
BT3364
Source
Escherichia Coli.
Appearance
White, lyophilized powder.

AGO2 Human

Argonaute 2 Human Recombinant

This product consists of a recombinant human AGO2 protein produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 869 amino acids, including a 10-amino acid N-terminal His tag. The calculated molecular mass of the protein is 98.4 kDa.

Shipped with Ice Packs
Cat. No.
BT3431
Source
Escherichia Coli.
Appearance

The product appears as a clear, colorless solution after filtration.

EEF1A1 Human

Eukaryotic Translation Elongation Factor 1 Alpha 1 Human Recombinant

Recombinant human EEF1A1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 462 amino acids (amino acids 1-462). It has a molecular weight of 50 kDa.
Shipped with Ice Packs
Cat. No.
BT3500
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

EEF1B2 Human

Eukaryotic Translation Elongation Factor 1 Beta 2 Human Recombinant

Recombinant human EEF1B2 protein, with an 8-amino acid His tag at the C-terminus, was expressed in E. coli. This non-glycosylated polypeptide chain consists of 233 amino acids (residues 1-225) and has a molecular weight of 25.8 kDa. Purification of EEF1B2 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3544
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless, and filtered solution.

EIF3K Human

Eukaryotic Translation Initiation Factor 3K Human Recombinant

Produced in E. coli, EIF3K is a single, non-glycosylated polypeptide chain comprising 238 amino acids (1-218a.a.) with a molecular weight of 27.2 kDa. This 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.
BT4765
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

EIF4A3 Human

Eukaryotic Translation Initiation Factor 4A3 Human Recombinant

Recombinant human EIF4A3, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 435 amino acids (amino acids 1-411) with a molecular weight of 49.4 kDa. The protein includes a 24-amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4838
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

EIF4E Human

Eukaryotic Translation Initiation Factor 4E Human Recombinant

Recombinant human EIF4E, expressed in E. coli, is a purified protein with a molecular weight of 27.2 kDa. It consists of a single polypeptide chain of 237 amino acids (residues 1-217), excluding any glycosylation modifications. A 20-amino acid Histidine tag is fused to the N-terminus to facilitate purification, which is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT4932
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized through filtration.

EIF4E Mouse

Eukaryotic Translation Initiation Factor 4E Recombinant Mouse

Recombinant EIF4E from mouse, expressed in E. coli, is a non-glycosylated polypeptide chain containing 241 amino acids (residues 1-217) with a molecular weight of 27.6 kDa. The protein includes a 24-amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT5024
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized through filtration.

EEF2K Human

Eukaryotic Elongation Factor-2 Kinase Human Recombinant

Recombinant Human EEF2K, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 748 amino acids (specifically, amino acids 1 to 725). It possesses a molecular mass of 84.6 kDa. This EEF2K protein is fused to a 23 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT3949
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

EIF1 Human

Eukaryotic Translation Initiation Factor 1 Human Recombinant

Recombinant Human EIF1 protein expressed in E. coli. This non-glycosylated protein consists of 150 amino acids (residues 1-113), resulting in a molecular weight of 16.9 kDa. For purification purposes, a 37 amino acid His-tag is fused to the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4055
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.
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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