Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

EIF1AX Human

Eukaryotic Translation Initiation Factor 1 X-linked Human Recombinant

Recombinant human EIF1AX, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 150 amino acids (residues 1-144a.a.) with a molecular weight of 18.6 kDa. A 20a.a. His-Tag is fused to the N-terminus of EIF1AX, which is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT4126
Source
Escherichia Coli.
Appearance
A clear, sterile solution without any color.

EIF1AY Human

Eukaryotic Translation Initiation Factor 1A Y-linked Recombinant Human

Produced in E.Coli, EIF1AY is a single, non-glycosylated polypeptide chain consisting of 167 amino acids (1-144.a.a) with a molecular weight of 18.8kDa. It includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4199
Source
Escherichia Coli.
Appearance
Clear, sterile solution after filtration.

EIF1B Human

Eukaryotic Translation Initiation Factor 1B Human Recombinant

Recombinant human EIF1B protein, expressed in E. coli, is fused with a 20 amino acid His tag at its N-terminus. This single, non-glycosylated polypeptide chain consists of 133 amino acids (residues 1-113) and has a molecular weight of 15 kDa. Purification of EIF1B is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4255
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

EIF2B1 Human

Eukaryotic Translation Initiation Factor 2B Subunit 1 Alpha Human Recombinant

The EIF2B1 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 325 amino acids (specifically, residues 1 to 305). It has a molecular weight of 35.8 kDa. The protein includes a 20 amino acid His-tag fused to its N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT4327
Source
Escherichia Coli.
Appearance
A sterile, colorless solution that has been filtered.

EIF2S1 Human

Eukaryotic Translation Initiation Factor 2 Subunit 1 Alpha Human Recombinant

Recombinant Human EIF2S1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 335 amino acids (specifically, amino acids 1 to 315). Its molecular weight is approximately 38.2 kDa. A 20 amino acid His-Tag is fused to the N-terminus of EIF2S1. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4400
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

EIF3F Human

Eukaryotic Translation Initiation Factor 3F Human Recombinant

This product consists of the human EIF3F protein recombinantly produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 380 amino acids, with the first 357 amino acids representing the EIF3F sequence and a 23 amino acid His-tag fused at the N-terminus. The molecular weight of the recombinant protein is 40kDa, and it undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4482
Source
Escherichia Coli.
Appearance
The product appears as a clear, colorless solution that has been sterilized by filtration.

EIF3I Human

Eukaryotic Translation Initiation Factor 3I Human Recombinant

This product consists of EIF3I Human Recombinant, produced in E. coli. It is a single, non-glycosylated polypeptide chain with 348 amino acids (1-325aa) and a molecular weight of 38.9kDa. A 23 amino acid His-tag is fused to the N-terminus of the EIF3I protein. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4541
Source
Escherichia Coli.
Appearance
The product appears as a clear solution that has undergone sterile filtration.

EIF3I Human, Sf9

Eukaryotic Translation Initiation Factor 3I Human Recombinant, Sf9

EIF3I Human Recombinant, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain consisting of 331 amino acids (with a sequence spanning from amino acid 1 to 325) and possessing a molecular weight of 37.3kDa. On SDS-PAGE under reducing conditions, it migrates at a range of 40-57kDa. This recombinant protein is engineered with a 6-amino acid His-tag fused at the C-terminus and is purified through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4613
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

EIF5A2 Human

Eukaryotic Translation Initiation Factor 5A2 Human Recombinant

Recombinant EIF5A2, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 173 amino acids (residues 1-153). With a molecular weight of 18.9 kDa, this EIF5A2 protein is fused to a 20 amino acid His-Tag at its N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT5466
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

EEF1D Human

Eukaryotic Translation Elongation Factor 1 Delta Human Recombinant

Recombinant human EEF1D, expressed in E. coli, is fused to a 20 amino acid His tag at its N-terminus. This non-glycosylated polypeptide chain comprises 301 amino acids (1-281 a.a.) with a molecular mass of 33.2kDa. Note: The molecular weight observed on SDS-PAGE may be higher. Purification of EEF1D is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT3622
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 .

© Copyright 2024 Thebiotek. All Rights Reserved.