PLA2G16 / HRASLS3 Antibody (N-Terminus)
Goat Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, E |
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Primary Accession | P53816 |
Reactivity | Human, Rabbit, Monkey |
Host | Goat |
Clonality | Polyclonal |
Calculated MW | 18kDa |
Dilution | ELISA (1:128000), IHC-P (5 µg/ml), |
Gene ID | 11145 |
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Other Names | HRAS-like suppressor 3, HRSL3, 3.1.1.32, 3.1.1.4, 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 |
Target/Specificity | Human PLA2G16. Reported variants represent identical protein:NP_009000.2 and NP_001121675.1). |
Reconstitution & Storage | Store at -20°C. Minimize freezing and thawing. |
Precautions | PLA2G16 / HRASLS3 Antibody (N-Terminus) is for research use only and 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:19047760, PubMed:19615464, PubMed:22605381, PubMed:22825852, 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:19047760, PubMed:19615464, PubMed:22605381, PubMed:22825852, 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:19047760, PubMed:19615464, PubMed:22605381, PubMed:22825852). 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) |
Volume | 250 µl |
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Background
Exhibits PLA1/2 activity, catalyzing the calcium- independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O- acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity.
References
Husmann K.,et al.Oncogene 17:1305-1312(1998).
Kato S.,et al.Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
Siegrist S.,et al.Oncogene 20:5155-5163(2001).
Uyama T.,et al.Biochim. Biophys. Acta 1791:1114-1124(2009).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
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