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anti-Human PLIN1 Antibodies:
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Human Polyclonal PLIN1 Primary Antibody for ELISA, ICC - ABIN253096
Rigamonti, Brennand, Lau, Cowan: Rapid cellular turnover in adipose tissue. in PLoS ONE 2011
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Human Polyclonal PLIN1 Primary Antibody for ICC, IF - ABIN258311
Kadereit, Kumar, Wang, Miranda, Snapp, Severina, Torregroza, Evans, Silver: Evolutionarily conserved gene family important for fat storage. in Proceedings of the National Academy of Sciences of the United States of America 2008
Show all 6 Pubmed References
Polyclonal PLIN1 Primary Antibody for WB - ABIN540340
Brasaemle, Barber, Wolins, Serrero, Blanchette-Mackie, Londos: Adipose differentiation-related protein is an ubiquitously expressed lipid storage droplet-associated protein. in Journal of lipid research 1998
Show all 3 Pubmed References
Cow (Bovine) Polyclonal PLIN1 Primary Antibody for IHC (fro), IHC (p) - ABIN113463
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
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Human Polyclonal PLIN1 Primary Antibody for ELISA, WB - ABIN4344849
Famulla, Schlich, Sell, Eckel: Differentiation of human adipocytes at physiological oxygen levels results in increased adiponectin secretion and isoproterenol-stimulated lipolysis. in Adipocyte 2013
Show all 2 Pubmed References
Human Polyclonal PLIN1 Primary Antibody for IF (p), IHC (p) - ABIN704141
Stelmanska, Szrok, Swierczynski et al.: Progesterone-induced down-regulation of hormone sensitive lipase (Lipe) and up-regulation of G0/G1 switch 2 (G0s2) genes expression in inguinal adipose tissue of female rats is reflected by ... in The Journal of steroid biochemistry and molecular biology 2015
Dog (Canine) Polyclonal PLIN1 Primary Antibody for IF, ELISA - ABIN547893
Wolins, Brasaemle, Bickel: A proposed model of fat packaging by exchangeable lipid droplet proteins. in FEBS letters 2006
Human Polyclonal PLIN1 Primary Antibody for ICC, IF - ABIN4344853
Finlin, Memetimin, Confides, Kasza, Zhu, Vekaria, Harfmann, Jones, Johnson, Westgate, Alexander, Sullivan, Dupont-Versteegden, Kern: Human adipose beiging in response to cold and mirabegron. in JCI insight 2018
Cow (Bovine) Monoclonal PLIN1 Primary Antibody for IHC (fro), IF - ABIN452158
Blanchette-Mackie, Dwyer, Barber, Coxey, Takeda, Rondinone, Theodorakis, Greenberg, Londos: Perilipin is located on the surface layer of intracellular lipid droplets in adipocytes. in Journal of lipid research 1995
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OPA1 mediates adrenergic control of lipolysis in human adipocytes by regulating phosphorylation of perilipin 1.
It was identified that PLIN1 serves a crucial role in the pathogenesis and progression of liposarcoma and may be a potential therapeutic target for its clinical management.
Classification of cells as containing few large or many small LDs followed by calculating the percentage of cells in each class proved to discriminate the positive PLIN1-suppressed phenotype from the untreated negative control with an area under the receiver operating characteristic curve of 0.98.
Expression of UCP2 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 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 (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, and PLIN3.
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 expression but still fails to inhibit basal lipolysis as effectively as wild-type perilipin 1.
In long-term steatosis models in vitro, TIP47, MLDP, adipophilin, and finally perilipin were gradually induced
Independently and in an interactive manner, PLIN (and ENPP1) 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.
Although specific for invasive sebaceous carcinoma, perilipin expression was not helpful in distinguishing sebaceous carcinoma in situ from squamous cell carcinoma in situ with clear cell change.
Perilipin is almost exclusively expressed in white adipocytes, so the serious metabolic sequelae observed in patients suggest that primary defects in adipose tissue can lead to all the typical features seen in patients with the metabolic syndrome.[review]
Plin1 is required to restrain fat loss and pro-inflammatory responses in adipose tissue by reducing futile lipolysis to maintain metabolic homeostasis.
This mouse model might mimic and explain the pathogenesis of hepatosteatosis occurring in two typical disorders of adipose tissue dysfunction, obesity and lipodystrophy, particularly in lipodystrophic patients with Plin1 mutation.
IP6K1 is a novel regulator of PLIN1 mediated lipolysis
ex vivo studies in human primary adipocytes, demonstrate that perilipin 1 binds to AQP7, and that catecholamine activated protein kinase A phosphorylates the N-terminus of AQP7, thereby reducing complex formation
Here, we identify synthetic ligands that release ABHD5 from PLIN1 or PLIN5 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, the catalytic subunit of protein kinase and hormone-sensitive lipase on lipid droplets.
ESR1 regulates ATGL 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.
Data indicate that perilipin (plin) deficiency suppresses sterol regulatory element-binding protein-1 (SREBP-1) activation in white adipose tissue (WAT).
Perilipin1 (Plin1), another adipocyte-specific lipid droplet-associated protein, is an Fsp27 activator.
FSP27 acts to constitutively limit the lipid droplet presence of ATGL, perilipin 1 plays an essential role in mediating the response of ATGL action to beta-adrenergic hormones.
the reduction of perilipin1 in white adipose tissues may at least in part contribute to conjugated linoleic acid -mediated alternation of lipolysis of white adipose tissues.
Perilipin 1 ablation has limited consequences on energy balance. It does not impair exercise performance; fatty acids mobilization during exercise is not impaired, whereas their oxidation is enhanced
Lipolysis is differently regulated between perigonadal and mesenteric adipocytes, and these depot-specific differences might be explained by altered regulation of G0S2 and/or perilipin.
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 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 gene (GU461317:g.98G>A); results obtained indicate that the PLIN2 polymorphism could be a useful marker for lean growth.
In pig muscle PLIN1 and PLIN2 proteins are localized in correspondence with extra and intra-myocellular lipids, respectively.
This work describes the cloning and sequencing of porcine PLIN and M6PRBP1 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