EIF2S2 Blocking Peptide (C-term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P20042 |
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Other Accession | P41035, Q99L45, Q5E9D0, NP_003899.2 |
Gene ID | 8894 |
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Other Names | Eukaryotic translation initiation factor 2 subunit 2, Eukaryotic translation initiation factor 2 subunit beta, eIF-2-beta, EIF2S2, EIF2B |
Target/Specificity | The synthetic peptide sequence is selected from aa 285-299 of HUMAN EIF2S2 |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | EIF2S2 |
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Synonyms | EIF2B |
Function | Component of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (PubMed:31836389). This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (By similarity). |
Cellular Location | Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56329} |
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Provided below are standard protocols that you may find useful for product applications.
Background
Eukaryotic translation initiation factor 2 (EIF-2) functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA and binding to a 40S ribosomal subunit. EIF-2 is composed of three subunits, alpha, beta, and gamma, with the protein encoded by this gene representing the beta subunit. The beta subunit catalyzes the exchange of GDP for GTP, which recycles the EIF-2 complex for another round of initiation.
References
Rajesh, K., et al. Biochem. Biophys. Res. Commun. 374(2):336-340(2008)
Sugiyama, N., et al. Mol. Cell Proteomics 6(6):1103-1109(2007)
Olsen, J.V., et al. Cell 127(3):635-648(2006)
Olsen, J.V., et al. Cell 127(3):635-648(2006)
Mikami, S., et al. Protein Expr. Purif. 46(2):348-357(2006)
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