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The protein encoded by PLIN1 coats lipid storage droplets in adipocytes, thereby protecting them until they can be broken down by hormone-sensitive lipase. Additionally we are shipping PLIN1 Antibodies (122) and PLIN1 Proteins (6) and many more products for this protein.
Showing 10 out of 27 products:
Human PLIN1 ELISA Kit for Sandwich ELISA - ABIN418419
Eleftheriadis, Antoniadi, Liakopoulos, Pissas, Arampatzis, Sparopoulou, Galaktidou, Stefanidis: Perilipin-1 in hemodialyzed patients: association with history of coronary heart disease and lipid profile. in Therapeutic apheresis and dialysis : official peer-reviewed journal of the International Society for Apheresis, the Japanese Society for Apheresis, the Japanese Society for Dialysis Therapy 2012
Mouse (Murine) PLIN1 ELISA Kit for Sandwich ELISA - ABIN425922
Kowalska, Olejnik, Rychlik, Grajek: Cranberries (Oxycoccus quadripetalus) inhibit lipid metabolism and modulate leptin and adiponectin secretion in 3T3-L1 adipocytes. in Food chemistry 2015
The strong association of PLIN1, CFD (show CFD ELISA Kits) and ADIPOQ (show ADIPOQ ELISA Kits) genes with adipogenesis prompted authors to study the influence the bone health status as evaluated by quantitative ultrasound (QUS) bone densitometer in a North Indian cohort. Overall, ADIPOQ (show ADIPOQ ELISA Kits) (rs1501299 and rs3774261) and combined cluster of PLIN1 rs2304796 and rs2304795) and CFD (show CFD ELISA Kits) (rs1683563) demonstrated correlation.
Perilipin 1 expression increased with adipocytic differentiation of liposarcoma subtypes showing statistical significance.
Based on the PCR with mismatched primers PLIN1 polymorphisms could be identified effectively in Chinese Han population.
Conserved amphipathic helices mediate lipid droplet targeting of PLIN1, PLIN2 (show PLIN2 ELISA Kits), and PLIN3 (show PLIN3 ELISA Kits).
Skeletal muscle PLIN proteins likely play a role in the hydrolysis of triglycerides stored in lipid droplets and the passage of fatty acids to the mitochondria for oxidation.
The functional PLIN1 rs6496589 may influence the risk of central obesity through possible regulation of lipid storage.
After bariatric surgery-induced weight loss, PLIN1 gene/protein expression in SAT increased significantly. Findings suggest a positive functional interaction between PLIN1 & mitochondrial biogenesis-related genes in human adipose tissue.
Use of molecular docking software to design perilipin-1 inhibitors as antiobesity agents.
This plin1 variant binds and stabilizes ABHD5 (show ABHD5 ELISA Kits) expression but still fails to inhibit basal lipolysis as effectively as wild-type perilipin 1.
In long-term steatosis models in vitro, TIP47 (show PLIN3 ELISA Kits), MLDP (show PLIN5 ELISA Kits), adipophilin (show PLIN2 ELISA Kits), and finally perilipin were gradually induced
Perilipin, which was thought to be characteristic for lipid droplets of adipocytes and steroidogenic cells, becomes de novo expressed in hepatocytes of human, mouse, and cattle liver.
Here, we identify synthetic ligands that release ABHD5 (show ABHD5 ELISA Kits) from PLIN1 or PLIN5 (show PLIN5 ELISA Kits) without PKA activation and rapidly activate adipocyte and muscle lipolysis.
Heterozygous Plin1+/- SVCs were able to develop lipid droplets, with both the number and size more than in Plin1-/- SVCs but less than in Plin1+/+ SVCs, indicating that Plin1 haploinsufficiency accounts for attenuated adipogenesis.
Plin1 deficiency in bone marrow-derived cells may be responsible for reduced atherosclerotic lesions in the mice
Perilipin+ embryonic preadipocytes actively proliferate along growing vasculatures for adipose expansion.
Data suggest cardiotrophin-1 up-regulates lipolysis in adipocytes via 1) induction of Plin1, 2) activation of hormone sensitive lipase (via phosphorylation by PKA), and 3) inactivation of adipose triglyceride lipase (via up-regulation of G0S2).
Adipocytes of Plin1/ mice showed robust basal lipolysis and fatty acid efflux to the plasma. Such adipose tissue dysfunctions accounted for the ectopic lipid accumulation and enhanced fatty acid transport and oxidation in Plin1/ hearts.
QRFP-43 attenuates lipolysis by preventing the formation of an active complex between perilipin A, caveolin-1 (show CAV1 ELISA Kits), the catalytic subunit of protein kinase (show CDK7 ELISA Kits) and hormone-sensitive lipase (show LIPE ELISA Kits) on lipid droplets.
ESR1 (show ESR1 ELISA Kits) regulates ATGL (show PNPLA2 ELISA Kits) and perilipin-mediated lipid metabolism and droplet size in femurs from mice.
Collectively these data suggest that whereas perilipin 1 potently suppresses basal lipolysis in adipocytes, perilipins 2 and 3 facilitate higher rates of basal lipolysis
these findings indicated that PLIN1 disruption leads to the increase of round spermatid-containing seminiferous tubules at the meiotic stage of the first wave of spermatogenesis through regulating spermatogenic related genes.
PLIN1 and PLIN2 (show PLIN2 ELISA Kits) 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 gene (JN860199:g.173G>A) and the 3' untranslated region of the PLIN2 (show PLIN2 ELISA Kits) gene (GU461317:g.98G>A); results obtained indicate that the PLIN2 (show PLIN2 ELISA Kits) polymorphism could be a useful marker for lean growth.
In pig muscle PLIN1 and PLIN2 (show PLIN2 ELISA Kits) proteins are localized in correspondence with extra and intra-myocellular lipids, respectively.
This work describes the cloning and sequencing of porcine PLIN and M6PRBP1 (show PLIN3 ELISA Kits) cDNAs, the chromosome mapping of these two genes, as well as the expression pattern of porcine PAT genes.
The protein encoded by this gene coats lipid storage droplets in adipocytes, thereby protecting them until they can be broken down by hormone-sensitive lipase. The encoded protein is the major cAMP-dependent protein kinase substrate in adipocytes and, when unphosphorylated, may play a role in the inhibition of lipolysis. Alternatively spliced transcript variants varying in the 5' UTR, but encoding the same protein, have been found for this gene.
, perilipin 1
, lipid droplet-associated protein
, perilipin A
, perilipin B
, adipocyte lipid droplet binding protein