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PNPLA2 encodes an enzyme which catalyzes the first step in the hydrolysis of triglycerides in adipose tissue. Additionally we are shipping Patatin-Like phospholipase Domain Containing 2 Kits (29) and Patatin-Like phospholipase Domain Containing 2 Proteins (9) and many more products for this protein.
Showing 10 out of 162 products:
Human Monoclonal PNPLA2 Primary Antibody for EIA, IHC (p) - ABIN356228
Fischer, Lefèvre, Morava, Mussini, Laforêt, Negre-Salvayre, Lathrop, Salvayre: The gene encoding adipose triglyceride lipase (PNPLA2) is mutated in neutral lipid storage disease with myopathy. in Nature genetics 2006
Show all 3 references for ABIN356228
Human Polyclonal PNPLA2 Primary Antibody for IHC, ELISA - ABIN190844
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 - ABIN334463
Steinberg, Kemp, Watt: Adipocyte triglyceride lipase expression in human obesity. in American journal of physiology. Endocrinology and metabolism 2007
the ATGL gene plays an important role in triglyceride lipolysis in GMECs; ATGL may be involved in lipid metabolism during lactation
A missense mutation in PNPLA2 is the rare cause of severe dilated cardiomyopathy secondary to neutral lipid storage disease.
A novel deletion was identified in PNPLA2 protein from a patient with complete deficiency of adipose triglyceride lipase.
Rab32 (show RAB32 Antibodies) controls intracellular lipid accumulation through inducing lipolysis via enhancing ATGL expression indirectly.
Data indicate that a tumor suppressor mechanism by which G0/G1 switch gene 2 (show G0S2 Antibodies) product (G0S2 (show G0S2 Antibodies)) directly inhibits activity of a key intracellular adipose triglyceride lipase (ATGL).
Authors show that rat ATGL, coactivated by rat CGI-58 (show ABHD5 Antibodies), efficiently hydrolyzes triglycerides and retinyl ester.
PNPLA2 mutations were associated with an extended phenotype, including brain involvement in cases of neutral lipid-storage disease with myopathy.
Distinct cardiac phenotype between two homozygotes born in a village with accumulation of a genetic deficiency of adipose triglyceride lipase.
ANGPTL8 is a stress-response protein that down-regulates expression of ATGL.
Study reports the clinical and genetic findings of a neutral lipid storage disease with myopathy family of Italian origin with 3 affected siblings. to highlight the effect that different gene mutations may have on ATGL lipase (show LIPG Antibodies) activity, authors performed a functional characterization of the novel PNPLA2 missense mutations identified in their patients
PLIN5 (show PLIN5 Antibodies) was significantly colocated with ATGL, mitochondria and CGI-58 (show ABHD5 Antibodies), indicating a close association between the key lipolytic effectors in resting skeletal muscle.
ATGL-dependent lipolysis plays a critical role in mediating diverse effects of FoxO (show FOXO3 Antibodies) proteins in the liver, including effects on gluconeogenic, glycolytic, and lipogenic gene expression and metabolism.
ATGL KO mice had significantly lower fasting plasma free fatty-acids compared to WT. Fasting endogenous glucose production and peripheral glucose metabolism were similar in KO and WT mice.
Pharmacological inhibition of ATGL may prove useful to prevent HFD-induced obesity and insulin (show INS Antibodies) resistance
A role for Atgl in kidney lipolysis:fasting up-regulates Atgl levels and phosphorylation in mouse kidney.
data provide mechanistic insights into Jordans' anomaly in neutrophils and suggest that ATGL is a potent regulator of immune cell function and inflammatory diseases.
Data show that obese adipocyte-specific adipose triglyceride lipase (ATGL) knockout (AAKO) mice had reduced adipocyte lipolysis.
transcriptional transactivation assays with a luciferase reporter system revealed that Fabps enhance the ability of Atgl/Cgi-58 (show ABHD5 Antibodies)-mediated lipolysis to induce the activity of peroxisome proliferator-activated receptors.
Data (including data from studies in atherosclerotic knockout mice) suggest CGI58- (abhydrolase domain containing 5 (show ABHD5 Antibodies)-)deficient macrophages store-up triglyceride droplets and have reduced phagocytic capacity, comparable to Atgl-deficient macrophages.
Data suggest that cardiotrophin-1 (show CTF1 Antibodies) up-regulates lipolysis in white adipocytes via 1) induction of perilipin (show PLIN1 Antibodies), 2) activation of hormone sensitive lipase (show LIPE Antibodies) (via phosphorylation by PKA), and 3) inactivation of ATGL (via up-regulation of its inhibitor G0S2 (show G0S2 Antibodies)).
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.
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.
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.
patatin-like phospholipase domain-containing protein 2
, patatin-like phospholipase domain containing 2
, adipose triglyceride lipase
, calcium-independent phospholipase A2
, patatin-like phospholipase domain containing protein 2
, pigment epithelium-derived factor
, transport-secretion protein 2.2
, triglyceride hydrolase
, transport-secretion protein