HRASLS3 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P53816 |
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Other Accession | NP_009000 |
Clone Names | 80109128 |
Gene ID | 11145 |
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Other Names | HRAS-like suppressor 3, HRSL3, Adipose-specific phospholipase A2, AdPLA, Group XVI phospholipase A1/A2, H-rev 107 protein homolog, HRAS-like suppressor 1, HREV107-1, HREV107-3, Renal carcinoma antigen NY-REN-65, PLA2G16, HRASLS3, HREV107 |
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 | PLAAT3 (HGNC:17825) |
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Function | Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:22923616). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N- acylphosphatidylethanolamine (NAPE), which serves as precursor for N- acylethanolamines (NAEs) (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PubMed:22825852). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity). |
Cellular Location | Cell membrane {ECO:0000250|UniProtKB:P53817}; Single-pass membrane protein. Cytoplasm. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8R3U1}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8R3U1}. Peroxisome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein. Nucleus envelope {ECO:0000250|UniProtKB:Q8R3U1}. Lysosome membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein. Note=During eye lens differentiation, recruited from the cytosol to various organelles, including mitochondria, endoplasmic reticulum, nuclear envelope and lysosomes, immediately before organelle degradation. This translocation is triggered by organelle membrane damage and requires the C-terminal transmembrane domain {ECO:0000250|UniProtKB:Q8R3U1} |
Tissue Location | Widely expressed. low expression, if any, in hematopoietic cells and thymus. In testis, confined to round spermatids. Expressed in normal ovarian epithelial cells. Down- regulated in some ovarian carcinomas and testicular germ cell tumors Highly expressed in white adipose tissue (PubMed:19136964) |
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Provided below are standard protocols that you may find useful for product applications.
Background
PLA2G16 specifically catalyzes the release of fatty acids from phospholipids in adipose tissue. It also has a weak lysophospholipase activity (By similarity). Tumor suppressor that may be involved in interferon-dependent cell death.
References
Uyama, T., et al. Biochim. Biophys. Acta 1791(12):1114-1124(2009)Duncan, R.E., et al. J. Biol. Chem. 283(37):25428-25436(2008)Nazarenko, I., et al. J. Cell. Sci. 120 (PT 8), 1393-1404 (2007) Nazarenko, I., et al. Am. J. Pathol. 169(4):1427-1439(2006)
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