SLU7 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O95391 |
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Clone Names | 110717187 |
Gene ID | 10569 |
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Other Names | Pre-mRNA-splicing factor SLU7, hSlu7, SLU7 |
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 | SLU7 |
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Function | Required for pre-mRNA splicing as component of the spliceosome (PubMed:10197984, PubMed:28502770, PubMed:30705154). Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'-splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and for correct AG identification when more than one possible AG exists in 3'-splicing site region. May be involved in the activation of proximal AG. Probably also involved in alternative splicing regulation. |
Cellular Location | Nucleus. Nucleus speckle. Cytoplasm Note=Predominantly nuclear. Shuttling between the nucleus and the cytoplasm is regulated by the CCHC-type zinc finger. Upon UV-C stress stimulus, the nuclear concentration of the protein decreases, affecting alternative splicing. Translocates from the nucleus to the cytoplasm after heat shock cell treatment. Accumulates in cytoplasmic vesicle- like organelles after heat shock treatment, which may represent stress granules. |
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Background
Pre-mRNA splicing occurs in two sequentialtransesterification steps. The protein encoded by this gene is asplicing factor that has been found to be essential during thesecond catalytic step in the pre-mRNA splicing process. Itassociates with the spliceosome and contains a zinc knuckle motifthat is found in other splicing factors and is involved inprotein-nucleic acid and protein-protein interactions. [provided byRefSeq].
References
Alberstein, M., et al. RNA 13(11):1988-1999(2007)Olsen, J.V., et al. Cell 127(3):635-648(2006)Shomron, N., et al. J. Cell. Sci. 118 (PT 6), 1151-1159 (2005) :Shomron, N., et al. Mol. Biol. Cell 15(8):3782-3795(2004)Chua, K., et al. Mol. Cell. Biol. 21(5):1509-1514(2001)
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