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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. Zusätzlich bieten wir Ihnen PLIN1 Antikörper (121) und PLIN1 Kits (31) und viele weitere Produktgruppen zu diesem Protein an.
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Expression of UCP2 (zeige UCP2 Proteine) and PLIN1 genes influences the resting metabolic rate in obese individuals and could predict the weight loss after bariatric surgery.
The PLIN 6 polymorphism of the perilipin gene may influence the risk of obesity during adolescence.
Variability at the PLIN1 locus is associated with variability in weight loss. Moreover, eating late is related to lower weight-loss effectiveness among carriers of the AA genotype at the PLIN1 14995A>T variant.
The strong association of PLIN1, CFD (zeige CFD Proteine) and ADIPOQ 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 (rs1501299 and rs3774261) and combined cluster of PLIN1 rs2304796 and rs2304795) and CFD (zeige CFD Proteine) (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 (zeige PLIN2 Proteine), and PLIN3 (zeige PLIN3 Proteine).
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.
IP6K1 (zeige IP6K1 Proteine) is a novel regulator of PLIN1 mediated lipolysis
ex vivo studies in human primary adipocytes, demonstrate that perilipin 1 binds to AQP7 (zeige AQP7 Proteine), and that catecholamine activated protein kinase A phosphorylates the N-terminus of AQP7 (zeige AQP7 Proteine), thereby reducing complex formation
Here, we identify synthetic ligands that release ABHD5 (zeige ABHD5 Proteine) from PLIN1 or PLIN5 (zeige PLIN5 Proteine) 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 (zeige CTF1 Proteine) up-regulates lipolysis in adipocytes via 1) induction of Plin1, 2) activation of hormone sensitive lipase (zeige LIPE Proteine) (via phosphorylation by PKA), and 3) inactivation of adipose triglyceride lipase (zeige PNPLA2 Proteine) (via up-regulation of G0S2 (zeige G0S2 Proteine)).
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 (zeige CAV1 Proteine), the catalytic subunit of protein kinase (zeige CDK7 Proteine) and hormone-sensitive lipase (zeige LIPE Proteine) on lipid droplets.
ESR1 (zeige ESR1 Proteine) regulates ATGL (zeige PNPLA2 Proteine) and perilipin-mediated lipid metabolism and droplet size in femurs from mice.
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.
PLIN1 and PLIN2 (zeige PLIN2 Proteine) 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 (zeige PLIN2 Proteine) gene (GU461317:g.98G>A); results obtained indicate that the PLIN2 (zeige PLIN2 Proteine) polymorphism could be a useful marker for lean growth.
In pig muscle PLIN1 and PLIN2 (zeige PLIN2 Proteine) proteins are localized in correspondence with extra and intra-myocellular lipids, respectively.
This work describes the cloning and sequencing of porcine PLIN and M6PRBP1 (zeige PLIN3 Proteine) 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.
lipid droplet-associated protein
, perilipin A
, perilipin B
, adipocyte lipid droplet binding protein
, perilipin 1