Eukaryotic Translation Initiation Factor 5A (EIF5A) (N-Term) Peptide
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- Target See all EIF5A products
- EIF5A (Eukaryotic Translation Initiation Factor 5A (EIF5A))
- Protein Region
- N-Term
- Origin
- Human
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Source
- Synthetic
- Application
- Blocking Peptide (BP), Western Blotting (WB)
- Sequence
- LKGRPCKIVE MSTSKTGKHG HAKVHLVGID IFTGKKYEDI CPSTHNMDVP
- Characteristics
- This is a synthetic peptide designed for use in combination with anti-EIF5A Antibody. It may block above mentioned antibody from binding to its target protein in western blot and/or immunohistochecmistry under proper experimental settings. There is no guarantee for its use in other applications.
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- Add 100 μL of sterile PBS. Final peptide concentration is 1 mg/mL in PBS.
- Storage
- -20 °C
- Storage Comment
- For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
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- Target
- EIF5A (Eukaryotic Translation Initiation Factor 5A (EIF5A))
- Background
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EIF5A is a mRNA-binding protein involved in translation elongation. It has an important function at the level of mRNA turnover, probably acting downstream of decapping. It is involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. With syntenin SDCBP, EIF5A functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis. EIF5A regulates also TNF-alpha-mediated apoptosis and mediates effects of polyamines on neuronal process extension and survival. It may play an important role in brain development and function, and in skeletal muscle stem cell differentiation. EIF5A is also described as a cellular cofactor of human T-cell leukemia virus type I (HTLV-1) Rex protein and of human immunodeficiency virus type 1 (HIV-1) Rev protein, essential for mRNA export of retroviral transcripts.
Protein Size: 184 - Gene ID
- 1984
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