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anti-Human PLIN2 Antikörper:
anti-Mouse (Murine) PLIN2 Antikörper:
anti-Rat (Rattus) PLIN2 Antikörper:
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Human Polyclonal PLIN2 Primary Antibody für ICC, IF - ABIN258339
Wohlers, Jackson, Spangenburg: Lipolytic signaling in response to acute exercise is altered in female mice following ovariectomy. in Journal of cellular biochemistry 2011
Show all 7 Pubmed References
Human Polyclonal PLIN2 Primary Antibody für IHC (fro), IHC (p) - ABIN285650
Frances, Niemann: Stem cell dynamics in sebaceous gland morphogenesis in mouse skin. in Developmental biology 2012
Dog (Canine) Monoclonal PLIN2 Primary Antibody für IHC (fro), IF - ABIN112185
Heid, Schnölzer, Keenan: Adipocyte differentiation-related protein is secreted into milk as a constituent of milk lipid globule membrane. in The Biochemical journal 1997
Show all 5 Pubmed References
Human Polyclonal PLIN2 Primary Antibody für IHC, IHC (p) - ABIN258342
Goh, Tan, Tan, Seow, Ong, Lim, Sun, Ghosh, Silver: Postnatal Deletion of Fat Storage-inducing Transmembrane Protein 2 (FIT2/FITM2) Causes Lethal Enteropathy. in The Journal of biological chemistry 2015
Human Monoclonal PLIN2 Primary Antibody für IHC, ELISA - ABIN1724874
Shepherd, Cocks, Tipton, Ranasinghe, Barker, Burniston, Wagenmakers, Shaw: Preferential utilization of perilipin 2-associated intramuscular triglycerides during 1 h of moderate-intensity endurance-type exercise. in Experimental physiology 2012
Human Monoclonal PLIN2 Primary Antibody für ELISA, IF - ABIN5572070
Kern, Di Gregorio, Lu, Rassouli, Ranganathan: Perilipin expression in human adipose tissue is elevated with obesity. in The Journal of clinical endocrinology and metabolism 2004
Human Polyclonal PLIN2 Primary Antibody für WB - ABIN513123
Cantley, Yoshimura, Camporez, Zhang, Jornayvaz, Kumashiro, Guebre-Egziabher, Jurczak, Kahn, Guigni, Serr, Hankin, Murphy, Cline, Bhanot, Manchem, Brown, Samuel, Shulman: CGI-58 knockdown sequesters diacylglycerols in lipid droplets/ER-preventing diacylglycerol-mediated hepatic insulin resistance. in Proceedings of the National Academy of Sciences of the United States of America 2013
PLIN2 gene Ser251Pro missense mutation is associated with reduced insulin (zeige INS Antikörper) secretion and increased insulin (zeige INS Antikörper) sensitivity.
Interference with PLIN2 and PPARalpha (zeige PPARA Antikörper) resulted in major alterations in gene expression, especially affecting lipid, glucose, and purine metabolism.
This study shows that hepatitis C virus suppresses hepatic ADRP expression in infected patients and cell lines. Forcing the expression of miR (zeige MLXIP Antikörper)-148a and miR (zeige MLXIP Antikörper)-30a limits the suppressive effect of hepatitis C virus on ADRP.
ADP was expressed in a small proportion of lung adenocarcinoma suggesting that ADP-positive lung adenocarcinoma could be a distinct subtype of lung adenocarcinoma, induced by up-regulation of the lipogenic pathway.
Activation of ARF1 (zeige ARF1 Antikörper) dissociates ADRP from lipid droplets. A constitute active form of ARF1 (zeige ARF1 Antikörper) (ARF1Q71I) promotes HCV assembly. ADRP played a positive role in Hepatitis C virus replication and negative role in Hepatitis C virus assembly.
PLIN2 expression is significantly upregulated in human masticatory mucosa during wound healing
Adipophilin was present in 24 of 26 colorectal hyperplastic polyps, but did not correlate with presence of white opaque substance (i.e. lipid droplets) on magnifying endoscopy with narrow band imaging.
Conserved amphipathic helices mediate lipid droplet targeting of PLIN1 (zeige PLIN1 Antikörper), PLIN2, and PLIN3 (zeige PLIN3 Antikörper).
In hepatitis C virus -infected human livers, occludin (zeige OCLN Antikörper) and ADRP mRNA expression levels correlated with each other. Hepatitis C virus increases occludin (zeige OCLN Antikörper) expression via the upregulation of ADRP.
PLIN2 involves lipid modulation of GSK3 (zeige GSK3b Antikörper) activity, GSK3 (zeige GSK3b Antikörper) substrate expression, and cell growth/survival.
Although lipopolysaccharide (LPS (zeige TLR4 Antikörper)) can trigger inflammation in atherosclerosis, how LPS (zeige TLR4 Antikörper) promotes atherogenesis through acting on macrophages is not very clear. Here, we study the role of adipophilin in LPS (zeige TLR4 Antikörper)-induced inflammation. LPS (zeige TLR4 Antikörper) can promote the expression of adipophilin through the ERK1/2 (zeige MAPK1/3 Antikörper)-PPARgamma (zeige PPARG Antikörper) pathway.
Cardiac PLIN2 plays an important pathophysiological role in the development of dynamic steatosis and that the latter was prevented by upregulation of intracellular lipases, including Hormone-sensitive Lipase (zeige LIPE Antikörper).
Plin2 liver-specific ablation alleviates diet-induced hepatic steatosis and inflammation via a PEMT (zeige PEMT Antikörper)-mediated mechanism.
The relationship between M1-/M2-macrophage polarization and Adp-rich hepatocyte-consisting pseudolobules (PLs (zeige CTSC Antikörper)) was investigated in thioacetamide (TAA)-induced rat cirrhosis.
results identify PLIN2 as a determinant of global changes in the hepatic lipidome and suggest the hypothesis that these actions contribute to SREBP-regulated de novo lipogenesis involved in non-alcoholic fatty liver disease.
Taken together, these findings demonstrate that artesunate inhibits adipogenesis in 3T3-L1 preadipoytes through the reduced expression and/or phosphorylation levels of C/EBP-alpha (zeige CEBPA Antikörper), PPAR-gamma (zeige PPARG Antikörper), FAS (zeige FAS Antikörper), perilipin A (zeige PLIN1 Antikörper), and STAT-3 (zeige STAT3 Antikörper).
phosphorylation of PLIN2 is dependent on AMPK (zeige PRKAA1 Antikörper) and occurs after the interaction of PLIN2 with the chaperone-mediated autophagy chaperone HSPA8/Hsc70 (zeige HSPA8 Antikörper).
demonstrate a mutually beneficial relationship between PLIN2 deficiency and elevated apoA-I (zeige APOA1 Antikörper)/HDL (zeige HSD11B1 Antikörper)-C in preventing atherosclerosis development
our findings highlight the relationship between protein stability and a previously unnoticed function of Plin2 during lipolysis in adipocytes.
These results demonstrate that bovine embryos at the blastocyst stage expressed ADRP mRNA and protein, and that the embryonic culture system modified this expression.
Adipophilin and TIP47 (zeige PLIN3 Antikörper) are expressed in lipid droplets of vitamin A-storing hepatic stellate cells and additionally in lipid droplets of steatotic hepatocytes.
25 novel polymorphisms were identified within all exons and their flanking regions of ADFP, including the promoter region.
PLIN1 (zeige PLIN1 Antikörper) and PLIN2 have been evaluated as candidate genes for growth, carcass and meat quality traits in pigs; two single-nucleotide polymorphisms, one in intron 2 of the PLIN1 (zeige PLIN1 Antikörper) gene (JN860199:g.173G>A) and the 3' untranslated region of the PLIN2 gene (GU461317:g.98G>A); results obtained indicate that the PLIN2 polymorphism could be a useful marker for lean growth.
These findings suggested that PLIN2 was a major lipid droplet-associated protein (zeige PLIN1 Antikörper) in porcine oocytes.
In pig muscle PLIN1 (zeige PLIN1 Antikörper) and PLIN2 proteins are localized in correspondence with extra and intra-myocellular lipids, respectively.
PLIN2 can be a marker for carcass quality in pigs.
The protein encoded by this gene belongs to the perilipin family, members of which coat intracellular lipid storage droplets. This protein is associated with the lipid globule surface membrane material, and maybe involved in development and maintenance of adipose tissue. However, it is not restricted to adipocytes as previously thought, but is found in a wide range of cultured cell lines, including fibroblasts, endothelial and epithelial cells, and tissues, such as lactating mammary gland, adrenal cortex, Sertoli and Leydig cells, and hepatocytes in alcoholic liver cirrhosis, suggesting that it may serve as a marker of lipid accumulation in diverse cell types and diseases. Alternatively spliced transcript variants have been found for this gene.
, adipose differentiation-related protein
, adipose differentiation related protein
, perilipin 2
, adipocyte differentiation-related protein