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48-602MAG
Buffer Detection Kit for Magnetic Beads
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Anti-PNPLA3, clone 11C5, Cat. No. MABS2174, is a mouse monoclonal antibody that detects Phospholipase domain-containing protein 3 (PNPLA3) and has been tested for use in Western Blotting.
More>>Anti-PNPLA3, clone 11C5, Cat. No. MABS2174, is a mouse monoclonal antibody that detects Phospholipase domain-containing protein 3 (PNPLA3) and has been tested for use in Western Blotting. Less<<
Patatin-like phospholipase domain-containing protein 3
Background Information
1-acylglycerol-3-phosphate O-acyltransferase PNPLA3 (UniProt: Q9NST1; also known as EC:2.3.1.51, Acylglycerol transacylase, Adiponutrin, ADPN, Calcium-independent phospholipase A2-epsilon, iPLA2-epsilon, Lysophosphatidic acid acyltransferase, Patatin-like phospholipase domain-containing protein 3) is encoded by the PNPLA3 (also known as ASPN1, C22orf20) gene (Gene ID: 80339) in human. PNPLA3 is a single-pass type II membrane protein that specifically catalyzes coenzyme A (CoA)-dependent acylation of 1-acyl-sn-glycerol 3-phosphate (2-lysophosphatidic acid/LPA) to generate phosphatidic acid (PA), which is an important metabolic intermediate and precursor for both triglycerides and glycerophospholipids. It does not esterify other lysophospholipids. It possesses low triacylglycerol lipase and CoA-independent acylglycerol transacylase activities and thus may play a role in acyl-chain remodeling of triglycerides. It is down-regulated following a low-calorie diet and refeeding elevates the mRNA levels. It has an N-terminal cytoplasmic domain (aa 1-41), a transmembrane domain (aa 42-62), and long C-terminal lumenal domain (aa 63-481). Mutations in PNPLA3 gene are reported to cause non-alcoholic fatty liver disease 1 that is characterized by accumulation of triglycerides in the liver, insulin resistance, and dyslipidemia. A sequence variant (I148M) in PNPLA3 is shown to be a major genetic risk factor for nonalcoholic fatty liver disease. This substitution causes a major reduction in triglyceride hydrolase activity of the enzyme. (Ref.: BasuRay, S., et al. (2019). Proc. Natl. Acad. Sci. USA 116(19); 9521-9526).
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal antibody IgG2a in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Applications
Application
Anti-PNPLA3, clone 11C5, Cat. No. MABS2174, is a mouse monoclonal antibody that detects Phospholipase domain-containing protein 3 (PNPLA3) and has been tested for use in Western Blotting.
Key Applications
Western Blotting
Application Notes
Western Blotting Analysis: A representative lot detected PNPLA3 in Western Blotting applications (BasuRay, S., et. al. (2019). Proc. Natl. Acad. Sci. USA. 116(19):9521-9526).
Biological Information
Immunogen
Recombinant fusion protein of human PNPLA3 and Trigger Factor.
Clone
11C5
Concentration
Please refer to lot specific datasheet.
Host
Mouse
Specificity
Clone 11C5 is a mouse monoclonal antibody that detects human Patatin-like phospholipase domain-containing protein 3 (PNPLA3).
~54 kDa observed; 52.86 kDa calculated. Uncharacterized bands may be observed in some lysate(s).
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blotting in HepG2 cell lysate.
Western Blotting Analysis: 1 µg/mL of this antibody detected PNPLA3 in HepG2 cell lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Accumulation of PNPLA3 on lipid droplets is the basis of associated hepatic steatosis. BasuRay, S; Wang, Y; Smagris, E; Cohen, JC; Hobbs, HH Proc Natl Acad Sci U S A
116
9521-9526
2019
Fatty liver disease (FLD) is a disorder in which accumulation of triglycerides (TGs) in the liver can lead to inflammation, fibrosis, and cirrhosis. Previously, we identified a variant (I148M) in patatin-like phospholipase domain-containing protein 3 (PNPLA3) that is strongly associated with FLD, but the mechanistic basis for the association remains elusive. Although PNPLA3 has TG hydrolase activity in vitro, inactivation or overexpression of the WT protein in mice does not cause steatosis. In contrast, expression of two catalytically defective forms of PNPLA3 (I148M or S47A) in sucrose-fed mice causes accumulation of both PNPLA3 and TGs on hepatic lipid droplets (LDs). To determine if amassing PNPLA3 on LDs is a cause or consequence of steatosis, we engineered a synthetic isoform of PNPLA3 that uncouples protein accumulation from loss of enzymatic activity. Expression of a ubiquitylation-resistant form of PNPLA3 in mice caused accumulation of PNPLA3 on hepatic LDs and development of FLD. Lowering PNPLA3 levels by either shRNA knockdown or proteolysis-targeting chimera (PROTAC)-mediated degradation reduced liver TG content in mice overexpressing PNPLA3(148M). Taken together, our results show that the steatosis associated with PNPLA3(148M) is caused by accumulation of PNPLA3 on LDs.
