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The protein encoded by PLIN2 belongs to the perilipin family, members of which coat intracellular lipid storage droplets. Additionally we are shipping PLIN2 Kits (29) and PLIN2 Proteins (20) and many more products for this protein.
Showing 10 out of 170 products:
Human Polyclonal PLIN2 Primary Antibody for 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 references for ABIN258339
Dog (Canine) Monoclonal PLIN2 Primary Antibody for 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 references for ABIN112185
Cow (Bovine) Polyclonal PLIN2 Primary Antibody for IHC (fro), IHC (p) - ABIN113458
Heid, Moll, Schwetlick, Rackwitz, Keenan: Adipophilin is a specific marker of lipid accumulation in diverse cell types and diseases. in Cell and tissue research 1998
Show all 5 references for ABIN113458
Dog (Canine) Monoclonal PLIN2 Primary Antibody for FACS, IHC (fro) - ABIN112186
Hope, McLauchlan: Sequence motifs required for lipid droplet association and protein stability are unique to the hepatitis C virus core protein. in The Journal of general virology 2000
Show all 4 references for ABIN112186
Human Polyclonal PLIN2 Primary Antibody for 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 for ICC, FACS - ABIN1724917
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
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 (show PLIN1 Antibodies), PLIN2, and PLIN3 (show PLIN3 Antibodies).
In hepatitis C virus -infected human livers, occludin (show OCLN Antibodies) and ADRP mRNA expression levels correlated with each other. Hepatitis C virus increases occludin (show OCLN Antibodies) expression via the upregulation of ADRP.
PLIN2 involves lipid modulation of GSK3 (show GSK3b Antibodies) activity, GSK3 (show GSK3b Antibodies) substrate expression, and cell growth/survival.
PLIN2 inhibits insulininduced glucose uptake by activating NLRP3 (show NLRP3 Antibodies), caspase1 (show CASP1 Antibodies) and IL1beta (show IL1B Antibodies), leading to a decreased IRS1 (show IRS1 Antibodies) expression.
Plin2 appears to be associated with functional alterations of the muscle
Results demonstrate the clinical utility, specificity, and sensitivity of urine AQP1 (show AQP1 Antibodies) and PLIN2 to diagnose renal cell carcinoma (show MOK Antibodies).
Postprandial triglyceride rich lipoproteins may be involved in atherosclerotic plaque formation through the regulation of perilipin-2 and perilipin-3 (show PLIN3 Antibodies) proteins in macrophages.
Immunohistochemical distinction of renal cell carcinoma (show MOK Antibodies) from other carcinomas with clear-cell histomorphology: utility of CD10 (show MME Antibodies) and CA-125 (show MUC16 Antibodies) in addition to PAX-2 (show PAX2 Antibodies), PAX-8 (show PAX8 Antibodies), RCCma, and adipophilin.
ADRP was detectable in human BM during the whole 12 months of lactation period and its levels were intraindividually well-conserved.
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 (show PLIN3 Antibodies) 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.
phosphorylation of PLIN2 is dependent on AMPK (show PRKAA1 Antibodies) and occurs after the interaction of PLIN2 with the chaperone-mediated autophagy chaperone HSPA8/Hsc70 (show HSPA8 Antibodies).
demonstrate a mutually beneficial relationship between PLIN2 deficiency and elevated apoA-I (show APOA1 Antibodies)/HDL (show HSD11B1 Antibodies)-C in preventing atherosclerosis development
our findings highlight the relationship between protein stability and a previously unnoticed function of Plin2 during lipolysis in adipocytes.
Plin2 modulates rapid effects of diet on fecal lipid levels, enterocyte CLD (show LMF1 Antibodies) contents, and fuel utilization properties of mice that correlate with structural and functional differences in their gut (show GUSB Antibodies) microbial communities
flavonoids from Coreopsis tinctoria extracts can reduce blood lipid without liver function damage by down-regulating ADRP.
The structure and function of specific domains responsible for Plin2-lipid interactions were identified.
Plin2 has a critical pathogenic role in experimental alcoholic liver disease
PLIN2-mediated lipid accumulation and utilization by the liver is important for efficient liver regeneration in response to partial hepatectomy and toxic liver injury.
PLIN1 (show PLIN1 Antibodies) 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 (show PLIN1 Antibodies) 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 (show PLIN1 Antibodies) in porcine oocytes.
In pig muscle PLIN1 (show PLIN1 Antibodies) 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
, adipocyte differentiation-related protein