SRP54 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P61011 |
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Clone Names | 100528323 |
Gene ID | 6729 |
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Other Names | Signal recognition particle 54 kDa protein, SRP54, SRP54 |
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 | SRP54 (HGNC:11301) |
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Function | Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:34020957). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane (PubMed:34020957). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes (PubMed:34020957). Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA (PubMed:28972538, PubMed:34020957). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA (PubMed:34020957). SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER (PubMed:34020957). Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA (By similarity). Plays a role in proliferation and differentiation of granulocytic cells, neutrophils migration capacity and exocrine pancreas development (PubMed:28972538, PubMed:29914977). |
Cellular Location | Nucleus speckle. Cytoplasm Endoplasmic reticulum |
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Provided below are standard protocols that you may find useful for product applications.
Background
SRP54 binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein).
References
Rose, J. Phd, et al. Mol. Med. (2010) In press :Yoshida, M., et al. Mol. Pharmacol. 73(3):987-994(2008)Sakashita, E., et al. Mol. Cell. Biol. 24(3):1174-1187(2004)Kuglstatter, A., et al. Nat. Struct. Biol. 9(10):740-744(2002)Yin, J., et al. RNA 7(10):1389-1396(2001)
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