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- Table of Contents
Facts about Translation initiation factor eIF-2B subunit alpha.
Human | |
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Gene Name: | EIF2B1 |
Uniprot: | Q14232 |
Entrez: | 1967 |
Belongs to: |
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eIF-2B alpha/beta/delta subunits family |
eIF-2B GDP-GTP exchange factor subunit alpha; EIF2B; EIF-2B; EIF-2Balpha; EIF2BAMGC117409; eukaryotic translation initiation factor 2B, subunit 1 (alpha, 26kD); eukaryotic translation initiation factor 2B, subunit 1 alpha, 26kDa; MGC125868; MGC125869; translation initiation factor eIF-2B subunit alpha
Mass (kDA):
33.712 kDA
Human | |
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Location: | 12q24.31 |
Sequence: | 12; NC_000012.12 (123620406..123633686, complement) |
The human EIF2B1 protein is expressed in E.coli with His-Tag. The corresponding sequence domain is 1-305 aa. It is suitable for applications involving SDS-PAGE, and is suitable for storage at a temperature range of -2degC to +8degC for one week. However, it should not undergo repeated freeze-thai cycles. As the human EIF2B1 protein is not validated in other species, special samples, or applications, it is not appropriate for all research.
High-affinity primary antibodies recognizing eIF2B1 are available for use with other eIF2B markers. This antibody recognizes eIF2B1 in small and medium bodies. The lower the concentration of SA, the greater the recovery. Lower concentrations of SA resulted in increased localization of eIF2Bd, suggesting that DBM is associated with a decreased shuttling capacity.
The preparation process for these antibodies is straightforward: 6.7 x 105 cells were seeded in T75 flasks and cultured for 3 min at 95degC. After 4 min, the sample was blocked with 5% nonfat milk or 1% BSA. The membranes were then incubated for 1 h with appropriate LiCor primary antibodies diluted in TBST. After the incubation period, the membranes were visualized on a LiCor Odyssey Scanner using Image Studio Lite software.
In addition to the EIF2B1 protein, this antibody recognizes the protein's G-protein partner. The eIF2B subunits form distinct bodies, depending on their size. Large bodies contain all eIF2B subunits, while medium bodies contain primarily catalytic subunits. The protein is also found in various types of tissues, including the liver, kidney, and pancreas.
The 18010-1-AP antibody targets the EIF2B1 protein in WB, IP, and IF. The eIF2Ba and eIF2Bb subunits maintain their stoichiometry by mutual stabilization of their individual subunits. The eIF2B protein is highly conserved in the body and is a valuable marker for studies of cancer, inflammation, and aging.
The eIF2Bb homologous complex is another protein whose structure is ambiguous. It is not an homodimer, but instead a dimer of eIF2B. The energy values of this eIF2Ba and eIF2Bb are in good agreement with experimental data. This means that high-affinity antibodies targeting eIF2B1 proteins should be useful for a variety of biological applications.
The structure of eIF2B remains elusive, with the apparent molecular mass typically in the range of 250 to 350 kDa. In the past, the protein was thought to be a heteropentamer, with five subunits. Mass spectrometry data confirm that these subunits are in equimolar amounts. Models based on distantly related enzymes have been proposed for the eIF2Bge subcomplex.
The eIF2B1 gene provides instructions for five parts of the eIF2B protein. EIF2B regulates overall protein synthesis in the cell. This marker helps increase protein synthesis by recycling GTP, which carries energy from the nucleus to the initiation factor. On the other hand, eIF2B slows down protein synthesis by binding tightly to the initiation factor. It prevents GTP from recycling.
Molecular and cellular studies show that eIF2B1 is a potential therapeutic target for cancer cells with aberrant Wnt signaling. Cancer stem cells that express aberrant Wnt signaling are known to target eIF2B. The EIF2B1 marker is expressed in intestinal cells containing multiple driver mutations and a hypomorphic eIF2B1 mutation.
The expression levels of eIF2B are regulated by the presence of a tumor suppressor protein, APC. This tumor suppressor is essential for the growth of small intestinal epithelial cells. Intestinal adenomas show markedly elevated levels of eIF2B. This marker is a potential diagnostic tool for early detection of intestinal adenomas. While the exact function of eIF2B is not understood, it has important roles in cancer cell biology.
eIF2B1 expression is required for sustained growth of intestinal epithelial cells in organoids. Intestinal eIF2B expression is lethal in yeast cells, but maintains its effects on intestinal epithelium. Intestinal epithelial cells, which are the most common human cancer cells, express eIF2B. Moreover, the gene is essential for growth and survival of organoids.
The indel mutations in CRISPR/Cas9-treated mice result in lethality. This suggests that eIF2B has a housekeeping function in the cell. Furthermore, a second "hit" could be due to an increase in metabolic load during development. This is important, because it may contribute to the severity of VWM disease. As a consequence, premature death is likely a result of indel formation.
eIF2B mutations do not correlate with the severity of VWM. However, they do not reduce the level of protein synthesis in beta-cells. In addition, these mutations do not compromise the cell viability in VWM patients. However, in some cases, patients with these mutations may be diagnosed with ataxia, lower weight, and other morphological changes. eIF2Bho mice exhibit small crypts.
The eIF2B1 protein is required for translation and functions as a key regulator of ER stress. Its role in gene regulation has been identified as being crucial for the development of Alzheimer's disease, Parkinson's disease, and a variety of other neurodegenerative diseases. Despite its importance, however, it is still poorly understood. Here, we will discuss the clinical applications of the EIF2B1 marker.
The decreased asialotransferrin/transferrin ratio in CSF is an inexpensive and highly sensitive diagnostic tool for eIF2B-related diseases. It also identifies patients for further mutation analysis. The EIF2B1 gene is a component of several proteins and enzymes, including hepatic sclerosis, Alzheimer's disease, and multiple sclerosis.
This protein is also associated with childhood ataxia with central nervous system hypomyelination, a disease that is related to mutations in eIF2B genes. eIF2B is a critical component of the protein synthesis process in all cells, and regulates its activity under stress. Leukoencephalopathy with vanishing white matter has been associated with ovarian failure.
The VWM mouse model mimics the features of VWM in human disease. In this model, EIF2B1 is expressed in mice with homozygous mutations in the Eif2b5 and eif2b4 genes, which cause astrocytic and myelin abnormalities. The EIF2B1 marker is important in the field of neurodegeneration because it provides objective disease markers for evaluating treatment efficacy in VWM mice.
PMID: 11835386 by van der Knaap M.S., et al. Mutations in each of the five subunits of translation initiation factor eIF2B can cause leukoencephalopathy with vanishing white matter.
PMID: 15776425 by Ohlenbusch A., et al. Identification of ten novel mutations in patients with eIF2B-related disorders.