Recombinant Human HRASLS3 protein (Tag Free)
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Recombinant Human HRASLS3 protein (Tag Free) is a Human Fragment protein, in the 1 to 133 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.
View Alternative Names
HRASLS3, HREV107, PLA2G16, PLAAT3, Phospholipase A and acyltransferase 3, Adipose-specific phospholipase A2, Group XVI phospholipase A1/A2, H-rev 107 protein homolog, HRAS-like suppressor 1, HRAS-like suppressor 3, HREV107-3, Renal carcinoma antigen NY-REN-65, AdPLA, H-REV107, HREV107-1, HRSL3
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human HRASLS3 protein (AB86922)
ab86922 on 15% SDS-PAGE (3μg)
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
Additional notes
purified by conventional chromatography techniques.
General info
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).. (Microbial infection) Acts as a host factor for picornaviruses : required during early infection to promote viral genome release into the cytoplasm (PubMed : 28077878). May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed : 28077878). Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed : 28077878). May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed : 28077878). The lipid-modifying enzyme activity is required for this process (PubMed : 28077878).
Sequence similarities
Belongs to the H-rev107 family.
Subcellular localisation
Peroxisome membrane
Target data
Complementary Products
Product promise
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