Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
PNPLA2 encodes an enzyme which catalyzes the first step in the hydrolysis of triglycerides in adipose tissue.
Showing 10 out of 186 products:
Human Monoclonal PNPLA2 Primary Antibody for CyTOF, FACS - ABIN4899287
He, Wu, Gong, Luo, Zhang, Li, Lu, Wei, Yang: Enhanced efficacy of combination therapy with adeno‑associated virus-delivered pigment epithelium-derived factor and cisplatin in a mouse model of Lewis lung carcinoma. in Molecular medicine reports 2014
Polyclonal PNPLA2 Primary Antibody for WB - ABIN540337
Haemmerle, Lass, Zimmermann, Gorkiewicz, Meyer, Rozman, Heldmaier, Maier, Theussl, Eder, Kratky, Wagner, Klingenspor, Hoefler, Zechner: Defective lipolysis and altered energy metabolism in mice lacking adipose triglyceride lipase. in Science (New York, N.Y.) 2006
Human Polyclonal PNPLA2 Primary Antibody for IHC (p), IHC - ABIN252920
Schoenborn, Heid, Vollmert, Lingenhel, Adams, Hopkins, Illig, Zimmermann, Zechner, Hunt, Kronenberg: The ATGL gene is associated with free fatty acids, triglycerides, and type 2 diabetes. in Diabetes 2006
Human Polyclonal PNPLA2 Primary Antibody for ELISA, WB - ABIN314328
Steinberg, Kemp, Watt: Adipocyte triglyceride lipase expression in human obesity. in American journal of physiology. Endocrinology and metabolism 2007
Human Monoclonal PNPLA2 Primary Antibody for ELISA, IHC - ABIN449788
Mason, Meex, Russell, Canny, Watt: Cellular localization and associations of the major lipolytic proteins in human skeletal muscle at rest and during exercise. in PLoS ONE 2014
No difference in the genotype frequency of rs7925131 or rs7942159 in PNPLA2 between the normal free fatty acids (FFA) group and the high FFA group in a Chinese Han population.
Non-cardiac ATGL-mediated modulation of the cardiac lipidome may play an important role in the pathogenesis of chronic heart failure.
Although we found evidence for moderate association between PNPLA2 tagSNPs and anthropometric and metabolic parameters in our cohort, no evidence for association between polymorphisms in the PNPLA2 gene and the presence and severity of non-alcoholic fatty liver disease was identified.
Study reports the derivation of iPSCs from fibroblasts of two Neutral Lipid Storage Disease with Myopathy (NLSDM)patients carrying different ATGL mutations. These iPSCs exhibited defects in neutral lipid metabolism similar to those of NLSDM fibroblasts. NLSDM-iPSCs were able to undergo directed differentiation into cardiomyocytes.
Thus, ATGL in leucocytes may be an important biomarker for the diagnosis of TGCV and our assay may provide insights into pathophysiology and elucidate the underlying mechanism of TGCV and related disorders.
The ATGL gene was frequently deleted in various forms of human cancers and was associated with poor prognosis.
a Snail1 (show SNAI1 Antibodies)-ATGL axis that regulates adipose lipolysis and fatty acid release, is reported.
ABHD5 (show ABHD5 Antibodies) possesses a PNPLA2-independent function in regulating autophagy and tumorigenesis.
Oxidative stress decreased the levels of PNPLA2 transcripts with no effect on ALOX5 (show ALOX5 Antibodies) expression. Exogenous additions of P1 peptide or overexpression of the PNPLA2 gene decreased both LTB4 (show PTGR1 Antibodies) levels and death of RPE (show RPE Antibodies) cells undergoing oxidative stress.
Results suggest that increased adipose triglyceride lipase (ATGL) expression is associated with increased adiposity and stromal proliferation in patients with pancreatic ductal adenocarcinoma (PDAC).
ATGL in brown adipose tissue is not a prerequisite for cold-induced thermogenesis in vivo.
this study shows that long non-coding steroid receptor (show ESR2 Antibodies) RNA activator promotes hepatic steatosis through repressing the expression of ATGL
ATGL deficiency results in male infertility in mice.
Loss of ATGL induces spontaneous development of pulmonary neoplasia in knockout mouse model.
ATGL acts as an important upstream signaling node that, via SIRT1 (show SIRT1 Antibodies), increases autophagy/lipophagy as a means to promote hepatic lipid droplet catabolism.
CGI-58 (show ABHD5 Antibodies) regulates hepatic neutral lipid storage and inflammation in the genetic absence of ATGL.
Enhanced lipolysis in response to mitochondrial uncoupling relies on a form of autophagy as lipid droplets are captured by endolysosomal vesicles which is HSL (show LIPE Antibodies)/ATGL-independent.
The Atgl is down-regulated by the basal transcription factor Sp1 (show SP1 Antibodies) in preadipocytes and that the magnitude of down-regulation depends on interactions between Sp1 (show SP1 Antibodies) and peroxisome proliferator-activated receptor gamma (PPARgamma (show PPARG Antibodies)).
Tissue distribution of ATGL gene expression was highest in fat and muscle (skeletal and cardiac) tissue, while protein expression was solely detectible in the adipose tissue.
Results identified functional polymorphisms providing new evidence of PNPLA2 as an important candidate gene for fat deposition and carcass traits in pigs.
Resveratrol activated sirtuin 1 (Sirt1 (show SIRT1 Antibodies)) gene expression and increased adipose triglyceride lipase (ATGL) gene expression and glycerol release. Furthermore, this study found the opposite Sirt1 (show SIRT1 Antibodies) regulation pattern for PPARgamma (show PPARG Antibodies) to that of ATGL in adipocytes.
analysis of porcine adipose triglyceride lipase (PNPLA2) gene
JAK (show JAK3 Antibodies)-STAT (show STAT1 Antibodies) and MAPK (show MAPK1 Antibodies) signaling pathways, as well as PPAR gamma (show PPARG Antibodies) all played important roles in the ATGL expression mediated by leptin (show LEP Antibodies)
patatin-like phospholipase domain containing 2 gene (PNPLA2) is assiged to chromosome 2 in pigs.
ATGL expression reacts to hormonal stimuli and plays a role in catecholamine-induced lipolysis in porcine adipose tissue.
the ATGL gene plays an important role in triglyceride lipolysis in GMECs; ATGL may be involved in lipid metabolism during lactation
This gene encodes an enzyme which catalyzes the first step in the hydrolysis of triglycerides in adipose tissue. Mutations in this gene are associated with neutral lipid storage disease with myopathy.
, adipose triglyceride lipase
, calcium-independent phospholipase A2
, patatin-like phospholipase domain containing protein 2
, patatin-like phospholipase domain-containing protein 2
, pigment epithelium-derived factor
, transport-secretion protein 2.2
, triglyceride hydrolase
, patatin-like phospholipase domain containing 2
, transport-secretion protein