GPAA1 Antibody (N-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O43292 |
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Clone Names | 91013043 |
Gene ID | 8733 |
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Other Names | Glycosylphosphatidylinositol anchor attachment 1 protein, GPI anchor attachment protein 1, GAA1 protein homolog, hGAA1, GPAA1, GAA1 |
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 | GPAA1 |
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Synonyms | GAA1 |
Function | Component of the GPI transamidase complex, necessary for transfer of GPI to proteins (PubMed:34576938). Essential for GPI- anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate. |
Cellular Location | Endoplasmic reticulum membrane; Multi-pass membrane protein |
Tissue Location | Ubiquitously expressed in fetal and adult tissues. Expressed at higher levels in fetal tissues than adult tissues |
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Provided below are standard protocols that you may find useful for product applications.
Background
Posttranslational glycosylphosphatidylinositol (GPI)anchor attachment serves as a general mechanism for linkingproteins to the cell surface membrane. The protein encoded by thisgene presumably functions in GPI anchoring at the GPI transferstep. The mRNA transcript is ubiquitously expressed in both fetaland adult tissues. The anchor attachment protein 1 contains anN-terminal signal sequence, 1 cAMP- and cGMP-dependent proteinkinase phosphorylation site, 1 leucine zipper pattern, 2 potentialN-glycosylation sites, and 8 putative transmembrane domains.
References
Jiang, W.W., et al. Mol. Cancer 6, 74 (2007) :Olsen, J.V., et al. Cell 127(3):635-648(2006)Ho, J.C., et al. Int. J. Cancer 119(6):1330-1337(2006)Vainauskas, S., et al. J. Biol. Chem. 280(16):16402-16409(2005)Vainauskas, S., et al. J. Biol. Chem. 279(8):6540-6545(2004)
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