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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 Kits (25) and PLIN1 Proteins (5) and many more products for this protein.
Showing 10 out of 99 products:
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
Show all 6 references for ABIN113463
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
Show all 2 references for ABIN452158
Dog (Canine) Polyclonal PLIN1 Primary Antibody for IHC (fro), IF - ABIN374794
Wolins, Brasaemle, Bickel: A proposed model of fat packaging by exchangeable lipid droplet proteins. in FEBS letters 2006
Show all 2 references for ABIN374794
Human Polyclonal PLIN1 Primary Antibody for WB - ABIN374835
Garcia-Carbonero, Supko, Maki, Manola, Ryan, Harmon, Puchalski, Goss, Seiden, Waxman, Quigley, Lopez, Sancho, Jimeno, Guzman, Demetri: Ecteinascidin-743 (ET-743) for chemotherapy-naive patients with advanced soft tissue sarcomas: multicenter phase II and pharmacokinetic study. in Journal of clinical oncology : official journal of the American Society of Clinical Oncology 2005
Show all 2 references for ABIN374835
Chicken Polyclonal PLIN1 Primary Antibody for WB - ABIN2777126
Moore, Silver, Mottillo, Bernlohr, Granneman: Perilipin targets a novel pool of lipid droplets for lipolytic attack by hormone-sensitive lipase. in The Journal of biological chemistry 2005
Conserved amphipathic helices mediate lipid droplet targeting of PLIN1, PLIN2 (show PLIN2 Antibodies), and PLIN3 (show PLIN3 Antibodies).
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 Antibodies) 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 Antibodies), MLDP (show PLIN5 Antibodies), adipophilin (show PLIN2 Antibodies), and finally perilipin were gradually induced
Independently and in an interactive manner, PLIN (and ENPP1 (show ENPP1 Antibodies)) 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, 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.
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 Antibodies) up-regulates lipolysis in adipocytes via 1) induction of Plin1, 2) activation of hormone sensitive lipase (show LIPE Antibodies) (via phosphorylation by PKA), and 3) inactivation of adipose triglyceride lipase (show PNPLA2 Antibodies) (via up-regulation of G0S2 (show G0S2 Antibodies)).
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 Antibodies), the catalytic subunit of protein kinase (show CDK7 Antibodies) and hormone-sensitive lipase (show LIPE Antibodies) on lipid droplets.
ESR1 (show ESR1 Antibodies) regulates ATGL (show PNPLA2 Antibodies) 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 (show SREBF1 Antibodies)) activation in white adipose tissue (WAT).
In pig muscle PLIN1 and PLIN2 (show PLIN2 Antibodies) 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 Antibodies) 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