Recombinant Human Eukaryotic Translation Initiation Factor 3 Subunit E (EIF3E) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-09193P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Eukaryotic Translation Initiation Factor 3 Subunit E (EIF3E) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-09193P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Human Eukaryotic Translation Initiation Factor 3 Subunit E (EIF3E) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P60228
Target Symbol EIF3E
Synonyms eIF-3 p48; eIF3e; EIF3E_HUMAN; EIF3S6; eIFe; Eukaryotic translation initiation factor 3 subunit 6; Eukaryotic translation initiation factor 3 subunit E; eukaryotic translation initiation factor 3; subunit 6 (48kD); INT6; mammary tumor-associated protein INT6; murine mammary tumor integration site 6 (oncogene homolog); Viral integration site protein INT-6 homolog
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence MAEYDLTTRIAHFLDRHLVFPLLEFLSVKEIYNEKELLQGKLDLLSDTNMVDFAMDVYKNLYSDDIPHALREKRTTVVAQLKQLQAETEPIVKMFEDPETTRQMQSTRDGRMLFDYLADKHGFRQEYLDTLYRYAKFQYECGNYSGAAEYLYFFRVLVPATDRNALSSLWGKLASEILMQNWDAAMEDLTRLKETIDNNSVSSPLQSLQQRTWLIHWSLFVFFNHPKGRDNIIDLFLYQPQYLNAIQTMCPHILRYLTTAVITNKDVRKRRQVLKDLVKVIQQESYTYKDPITEFVECLYVNFDFDGAQKKLRECESVLVNDFFLVACLEDFIENARLFIFETFCRIHQCISINMLADKLNMTPEEAERWIVNLIRNARLDAKIDSKLGHVVMGNNAVSPYQQVIEKTKSLSFRSQMLAMNIEKKLNQNSRSEAPNWATQDSGFY
Expression Range 1-445aa
Protein Length Full Length
Mol. Weight 79.1kDa
Research Area Epigenetics And Nuclear Signaling
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway. May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins.
Subcellular Location Cytoplasm. Nucleus, PML body.
Protein Families EIF-3 subunit E family
Database References
Tissue Specificity Ubiquitously expressed. Expressed at highest levels in appendix, lymph, pancreas, skeletal muscle, spleen and thymus.

Gene Functions References

  1. These data suggest that eIF3e downregulation may be involved in epithelial-mesenchymal transition in endometriosis, possibly through preferential translation of Snail. PMID: 28438065
  2. A transcript-specific eIF3 complex mediates global translational control of energy metabolism. PMID: 27477275
  3. INT6 protects against breast cancer by showing how it functions in DSB repair, with potential clinical implications for cancer therapy. PMID: 27550454
  4. eIF3e is an angiogenesis suppressor. Silencing of eIF3e promotes blood perfusion recovery after limb ischemia through stabilization of hypoxia-inducible factor 2alpha activity. PMID: 25758454
  5. High eIF3e expression may contribute to tumor progression and predict poor prognosis in colon cancer. PMID: 25400724
  6. Int6/eIF3e is essential for proliferation and survival of human glioblastoma cells. PMID: 24481065
  7. 40S ribosome loading imparts a phosphorylation mark on the cap-binding eIF4F complex that regulates selective mRNA translation and is synchronized by a specific eIF3 subunit PMID: 24736843
  8. Our findings indicate that Int6 act as a hypoxia-independent master switch of angiogenesis in neuronal cells PMID: 22960363
  9. eukaryotic initiation factor 4G (eIF4G) protein binds to eIF3c, -d, and -e to promote mRNA recruitment to the ribosome. PMID: 24092755
  10. novel role of eIF3e/Int6 in the regulation of EMT in breast epithelial cells PMID: 22907435
  11. IL-6 and IL-8 are HIF2alpha controlled cytokines for angiogenesis particularly in endothelial cells. PMID: 23478175
  12. HTLV-1Tax binds both INT6 and UPF1. The analysis of Tax mutants indicated that the Tax-INT6 association is necessary for nonsense-mediated mRNA decay inhibition, and data suggest that Tax sequesters INT6 out of reach from UPF1. PMID: 22553336
  13. INT6 and MIF4GD were observed to colocalize in cytoplasmic foci. It was concluded that INT6, by establishing interactions with MIF4GD and SLBP, plays an important role in translation of poly(A) minus histone mRNAs. PMID: 22532700
  14. findings reveal unexpected and striking connections of INT6 with ATM and BRCA1 PMID: 22508697
  15. Int6 depletion blocks ubiquitin-dependent proteolysis by decreasing both ubiquitin levels and the assembly of functional proteasome machinery, leading to accumulation of oncoproteins, such as SRC3. PMID: 20890303
  16. data suggest that eIF3e has a positive role in breast cancer progression. It regulates the translation, and in some cases abundance, of mRNAs involved in key aspects of cancer cell biology PMID: 20453879
  17. Int-6 protein can bind the three complexes /eIF3, COP9 signalosome and 26S proteasome/, possibly exerting a regulatory activity in both protein translation and degradation PMID: 12220626
  18. EIF3e/INT6 is localized in part to the nucleus, while other eIF3 components are cytoplasmic. Primary human fibroblasts showed reduced nuclear INT6 staining in early S phase. PMID: 15030549
  19. Reducing Int-6 expression by RNA interference in HeLa cells markedly alters mitosis progression and defects in spindle formation, chromosome segregation and cytokinesis are observed. PMID: 15558017
  20. Results suggest that Int6 expression, evaluated by quantitative real-time PCR, may represent a new prognostic factor in patients with stage I non-small cell lung cancers. PMID: 15867213
  21. eIF3e binds to eIF4G during the process of cap-dependent translation initiation PMID: 16766523
  22. INT6 stabilizes chromatin-bound MCM7 and alteration of this effect is associated with replication deficiency. PMID: 17310990
  23. INT6 knockdown by RNA interference strongly inhibits nonsense-mediated messenger RNA decay (NMD), which triggers degradation of mRNAs with premature stop codons. PMID: 17468741

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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