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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 (114) and PLIN1 Kits (25) and many more products for this protein.
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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 Proteins), and PLIN3 (show PLIN3 Proteins).
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 Proteins) 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 Proteins), MLDP (show PLIN5 Proteins), adipophilin (show PLIN2 Proteins), and finally perilipin were gradually induced
Independently and in an interactive manner, PLIN (and ENPP1 (show ENPP1 Proteins)) contribute to the risk of type 2 diabetes in a Taiwanese population.
Chinese adults with high waist circumference may have a high risk of diabetes, especially those with allele T in rs1052700 or with allele A in rs894160 of perilipin gene and those with perilipin genotype AA (rs894160) may have a high risk of obesity.
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 Proteins) from PLIN1 or PLIN5 (show PLIN5 Proteins) 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 (show CTF1 Proteins) up-regulates lipolysis in adipocytes via 1) induction of Plin1, 2) activation of hormone sensitive lipase (show LIPE Proteins) (via phosphorylation by PKA), and 3) inactivation of adipose triglyceride lipase (show PNPLA2 Proteins) (via up-regulation of G0S2 (show G0S2 Proteins)).
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 Proteins), the catalytic subunit of protein kinase (show CDK7 Proteins) and hormone-sensitive lipase (show LIPE Proteins) on lipid droplets.
ESR1 (show ESR1 Proteins) regulates ATGL (show PNPLA2 Proteins) 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.
In pig muscle PLIN1 and PLIN2 (show PLIN2 Proteins) 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 Proteins) 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