Recombinant Proteins

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EIF1AX Human

Eukaryotic Translation Initiation Factor 1 X-linked Human Recombinant

EIF1AX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-144a.a.) and having a molecular wieght of 18.6kDa. EIF1AX is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4126
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

EIF1AY Human

Eukaryotic Translation Initiation Factor 1A Y-linked Recombinant Human

EIF1AY produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-144.a.a) and having a molecular mass of 18.8kDa.
EIF1AY is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4199
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

EIF1B Human

Eukaryotic Translation Initiation Factor 1B Human Recombinant

EIF1B 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 133 amino acids (1-113 a.a.) and having a molecular mass of 15kDa. The EIF1B is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4255
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

EIF2B1 Human

Eukaryotic Translation Initiation Factor 2B Subunit 1 Alpha Human Recombinant

EIF2B1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 325 amino acids (1-305 a.a.) and having a molecular mass of 35.8kDa.
EIF2B1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4327
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

EIF2S1 Human

Eukaryotic Translation Initiation Factor 2 Subunit 1 Alpha Human Recombinant

EIF2S1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-315 a.a.) and having a molecular mass of
38.2 kDa. The EIF2S1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4400
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

EIF3F Human

Eukaryotic Translation Initiation Factor 3F Human Recombinant

EIF3F Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-357 a.a) and having a molecular mass of 40kDa.
EIF3F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4482
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

EIF3I Human

Eukaryotic Translation Initiation Factor 3I Human Recombinant

EIF3I Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-325aa) and having a molecular mass of 38.9kDa.
EIF3I is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4541
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

EIF3I Human, Sf9

Eukaryotic Translation Initiation Factor 3I Human Recombinant, Sf9

EIF3I Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 331 amino acids (1-325 a.a) and having a molecular mass of 37.3kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).
EIF3I is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT4613
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

EIF3J Human

Eukaryotic Translation Initiation Factor 3J Human Recombinant

EIF3J Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (70-258) and having a molecular mass of 24kDa (Molecular weight on SDS-PAGE will appear higher).
EIF3J is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4701
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

EIF3K Human

Eukaryotic Translation Initiation Factor 3K Human Recombinant

EIF3K produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (1-218a.a.) and having a molecular mass of 27.2 kDa.
EIF3K is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4765
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.
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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