Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Alle Spezies anzeigen
Weitere Synonyme anzeigen
Wählen Sie die Spezies und Applikation aus
anti-Mouse (Murine) Antikörper:
anti-Rat (Rattus) Antikörper:
Sie gelangen zu unserer vorgefilterten Suche.
Polyclonal LPIN1 Primary Antibody für IHC (fro), WB - ABIN540690
Péterfy, Phan, Reue: Alternatively spliced lipin isoforms exhibit distinct expression pattern, subcellular localization, and role in adipogenesis. in The Journal of biological chemistry 2005
Show all 3 Pubmed References
Polyclonal LPIN1 Primary Antibody für WB - ABIN540692
Huffman, Mothe-Satney, Lawrence: Insulin-stimulated phosphorylation of lipin mediated by the mammalian target of rapamycin. in Proceedings of the National Academy of Sciences of the United States of America 2002
Show all 3 Pubmed References
Human Polyclonal LPIN1 Primary Antibody für IHC (p), IHC - ABIN189479
Kim, Kim, Koh, Kim, Lee, Chanda, Park, Min, Lee, Park, Choi: Estrogen-related receptor γ (ERRγ) is a novel transcriptional regulator of phosphatidic acid phosphatase, LIPIN1, and inhibits hepatic insulin signaling. in The Journal of biological chemistry 2011
Show all 2 Pubmed References
Dog (Canine) Polyclonal LPIN1 Primary Antibody für ELISA - ABIN547769
Suviolahti, Reue, Cantor, Phan, Gentile, Naukkarinen, Soro-Paavonen, Oksanen, Kaprio, Rissanen, Salomaa, Kontula, Taskinen, Pajukanta, Peltonen: Cross-species analyses implicate Lipin 1 involvement in human glucose metabolism. in Human molecular genetics 2006
Using surrogate models that recapitulate different aspects of HCV infection, we concluded that lipin1 is rate limiting for the generation of functional replicase complexes, in a step downstream primary translation that leads to early HCV RNA replication.
Normal human adipose tissue functions and differentiation has been found in rhabdomyolysis patients with biallelic LPIN1 inactivating mutations.
conclude that Lipin-1 can antagonize HSC activation through the inhibition of TGF-beta/SMAD signaling and that resveratrol may affect Lipin-1 gene induction and contribute to the inhibition of TGF-beta-mediated hepatic fibrogenesis
beta-TRCP depletion in HepG2 hepatocellular carcinoma cells resulted in increased Lipin1 protein abundance.
This study showed that LPIN1 knockdown blocks phospholipid synthesis and changes membrane lipid compositions, and that lipin-1 knockdown significantly inhibits tumor growth in vivo using an orthotopic xenograft breast mouse model.
The novel insights into the regulation of human Lipin-1 stability will be useful in planning further studies to elucidate its metabolic processes.
It seems that a new signaling axis, SIRT1-SFRS10-LPIN1 axis, acting in the pathogenesis of alcoholic fatty liver disease exists.
Consistent with these observations, LPIN1 levels were positively correlated with IRS1 expression in human breast cancer. Thus, our results indicate a mechanism by which IRS1 expression is increased in breast cancer, and LPIN1 may be a promising drug target for anticancer therapy
LPIN1 is upregulated in non-alcoholic fatty liver disease. Up-regulation of miR-122 can trigger the compensatory response of LPIN1 and CTDNEP1 in hepatosteatosis.
lipin-1-mediated downregulation of p21 is critical for the progress of keratinocyte differentiation
lipin-1 has a critical role in the regulation of macrophage inflammatory responses to modified-LDL
Results of our study suggest that rs2716610: C>T polymorphism of LPIN1 gene could have a protective effect against development of metabolic syndrome, while rs11693809: C>T might affect a glucose control in patients with MS.
Lipin-1 controls main cellular processes involved in cancer progression and that its targeting, alone or in combination with other treatments, could open new avenues in anticancer therapy.
Lipin1beta might play a role in the pathogenesis of insulin resistance in gestational diabetes mellitus
LPIN1 plays a functional role in lipid synthesis and storage, a role which is highly conserved from human to yeast.
the lipin-1 N-terminal domain is important for its catalytic activity, nuclear localization, and binding to PP-1cgamma
Lipin-1 deficiency is associated with lipid metabolism alterations resulting in massive rhabdomyolysis.
the SNP in the LPIN1 gene (rs10192566) had no effect on the trough rosiglitazone steady-state concentration.
Phosphorylation of lipin 1 and charge on the phosphatidic acid head group control its phosphatidic acid phosphatase activity and membrane association
Data suggests common single nucleotide polymorphisms within the LPIN1 region were associated with Type 2 diabetes and metabolic traits in the Chinese population.
Fatty acids stimulate Tip60-dependent acetylation and endoplasmic reticulum translocation of phosphatidic acid phosphatase lipin 1 to generate diacylglycerol for triacylglycerols synthesis.
Macrophage-associated lipin-1 contributes to atherogenesis through persistent activation of a protein kinase Calpha/betaII-extracellular receptor kinase1/2-jun proto-oncogene signaling cascade that contributes to foam cell proinflammatory responses.
Study demonstrated that chronic alcohol feeding resulted in adipose tissue lipodystrophy and subsequent liver injury including ER stress and apoptosis. Overexpression of LPIN1 in adipose tissue protected mice against alcohol-induced liver injury through restoration of WAT lipid storage function and leptin secretion suggesting that LPIN1 plays a significant role in the pathogenesis of alcohol-induced lipodystrophy and ALD.
Suppression of lipin 1 and lipin2 are the primary mechanism of increased phosphatidic acid levels in the liver during acetaminophen-induced liver injury and recovery.
Data demonstrate that myeloid cell-specific deletion of lipin-1 ameliorated inflammation and alcoholic hepatitis in mice via activation of endocrine adiponectin-FGF15 signaling.
Data suggest that phosphorylation does not affect catalytic activity of lipin 3 or its ability to associate with phosphatidic acid in vitro; different polybasic domains in lipin 1 and lipin 3 are responsible for phospho-regulation on the former but not the latter enzyme.
Data indicate a critical physiological function of beta-TRCP in regulating hepatic lipid metabolic homeostasis in part through modulating Lipin1 stability.
The insulin resistance induced by lipin-1 downregulation was related to the disturbance of lipid homeostasis. Lipin-1 silencing reduced intracellular DAG and TAG levels, but elevated ceramide accumulation in C2C12 myotubes
Time course analysis demonstrated that the adipogenic 'hub', sampled by PPARgamma and Lpin1, undergoes orchestrated reorganization during adipogenesis.
Our findings provide new insights into the physiological roles of hepatic Lipin1 in systemic energy homeostasis, and suggest that the moderate inactivation of hepatic Lipin1 represents a promising approach for preventing the development of obesity.
c-fos has a role in increasing the catalytic efficiency of lipin 1 beta
reveals a previously unknown role of lipin1 in skeletal muscle regeneration and expands our understanding of the cellular and molecular mechanisms underlying skeletal muscle regeneration
deficits in hepatic PAP activity do not impair TG synthesis and accumulation
lipin-1 PAP activity functions in autophagy to activate the PKD-Vps34 cascade to promote autolysosome maturation.
The findings demonstrate an unanticipated role for lipin-1 as a mediator of macrophage proinflammatory activation and support a critical link between lipid biosynthesis and systemic inflammatory responses.
in addition to their roles during early adipogenesis, lipin1 and lipin2 also have a role in lipid droplet biogenesis.
hepatic removal of lipin-1 in mice augmented ethanol-induced impairment of hepatic fatty acid oxidation and lipoprotein production, likely by way of deactivation of peroxisome proliferator-activated receptor gamma coactivator-1 alpha.
Data from atomic force microscopy suggest that (in the presence of 2 mM CaCl2) recombinant lipin 1b assembles on membranes (lipid bilayers) to form particles that on average are 12-fold larger than the lipin monomer.
lipin1 functions as a key regulator of PPARgamma activity through its ability to release co-repressors and recruit co-activators via a mechanism other than PPARalpha activation
The lipin1 gene may have a crucial effect on body lipid accumulation in pigs.
Different genotypes of the Lpin1 gene were associated with percentage of leaf fat and intramuscular fat.
The results of this study suggest that suggest that SLC27A6, ACSL1, FABP3, AGPAT6, and LPIN1 coordinately regulate the channeling of fatty acids toward copious milk fat synthesis in bovine mammary.
This gene encodes a magnesium-ion-dependent phosphatidic acid phosphohydrolase enzyme that catalyzes the penultimate step in triglyceride synthesis including the dephosphorylation of phosphatidic acid to yield diacylglycerol. Expression of this gene is required for adipocyte differentiation and it also functions as a nuclear transcriptional coactivator with some peroxisome proliferator-activated receptors to modulate expression of other genes involved in lipid metabolism. Mutations in this gene are associated with metabolic syndrome, type 2 diabetes, and autosomal recessive acute recurrent myoglobinuria (ARARM). This gene is also a candidate for several human lipodystrophy syndromes. Alternative splicing results in multiple transcript variants encoding distinct isoforms. Additional splice variants have been described but their full-length structures have not been determined.
, phosphatidate phosphatase LPIN1-like
, phosphatidate phosphatase LPIN1
, fatty liver dystrophy protein