Recombinant Mouse Phosphatidate phosphatase LPIN1(Lpin1) ,partial

Code CSB-YP842063MO
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Source Yeast
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Code CSB-EP842063MO
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Source E.coli
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Code CSB-EP842063MO-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP842063MO
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Source Baculovirus
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Code CSB-MP842063MO
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names Lpin1
Uniprot No. Q91ZP3
Alternative Names Lpin1; FldPhosphatidate phosphatase LPIN1; EC 3.1.3.4; Fatty liver dystrophy protein; Lipin-1
Species Mus musculus (Mouse)
Protein Length Partial
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Data

Function Plays important roles in controlling the metabolism of fatty acids at different levels. Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. Acts also as nuclear transcriptional coactivator for PPARGC1A/PPARA regulatory pathway to modulate lipid metabolism gene expression. Is involved in adipocyte differentiation. Isoform 1 is recruited at the mitochondrion outer membrane and is involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol.
Gene References into Functions
  1. 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. PMID: 29323242
  2. 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. PMID: 29534981
  3. Data demonstrate that myeloid cell-specific deletion of lipin-1 ameliorated inflammation and alcoholic hepatitis in mice via activation of endocrine adiponectin-FGF15 signaling. PMID: 27666676
  4. 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. PMID: 28982975
  5. 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 PMID: 28123341
  6. Time course analysis demonstrated that the adipogenic 'hub', sampled by PPARgamma and Lpin1, undergoes orchestrated reorganization during adipogenesis. PMID: 28755519
  7. 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. PMID: 27725442
  8. lipin-1 has a critical role in the regulation of macrophage inflammatory responses to modified-LDL PMID: 26288136
  9. c-fos has a role in increasing the catalytic efficiency of lipin 1 beta PMID: 26475860
  10. 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 PMID: 26296887
  11. deficits in hepatic PAP activity do not impair TG synthesis and accumulation PMID: 25722343
  12. lipin-1 PAP activity functions in autophagy to activate the PKD-Vps34 cascade to promote autolysosome maturation. PMID: 24930972
  13. 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. PMID: 25252959
  14. in addition to their roles during early adipogenesis, lipin1 and lipin2 also have a role in lipid droplet biogenesis. PMID: 24133206
  15. 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. PMID: 23787969
  16. 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. PMID: 23862673
  17. 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 PMID: 23627357
  18. These results suggested that ER stress might be involved inthe pathogenesis of obesity through lipin-1 depletion. PMID: 23291236
  19. Lipin 1 coactivates HNF4alpha to activate the expression of a variety of genes encoding enzymes involved in fatty acid catabolism. PMID: 23236470
  20. negatively controls mast cell degranulation and the anaphylactic response PMID: 23065777
  21. Lipin 1 is a reciprocal regulator of triglyceride synthesis and hydrolysis in adipocytes. PMID: 23267081
  22. The absence of Lpin1 leads to defects in adipocyte maturation. Inactivation of Lpin1 in mature adipocytes protects aP2Cre-ERT2/+/LpfEx2-3/fEx2-3 mice against high-fat-diet-induced obesity. PMID: 23028044
  23. Mouse lipin-1 and lipin-2 cooperate to maintain glycerolipid homeostasis in liver and aging cerebellum. PMID: 22908270
  24. Nrf1 binds to the antioxidant response elements (AREs) in regulatory regions of the Lipin1 and PGC-1beta genes and the binding of Nrf1 to the AREs activates reporter gene transcription. PMID: 22586274
  25. Lipin1 mRNA levels were also decreased in adiponectin-deficient mice. PMID: 22051776
  26. fld hearts exhibit unchanged oleate esterification, as well as oleate and glucose oxidation, despite the absence of lipin-1. However, lipin-1 deficiency increases the accumulation of newly synthesized phosphatidate and induces aberrant cell signaling. PMID: 22058427
  27. Ethanol-induced up-regulation of lipin-1 gene expression is mediated through inhibition of AMPK and activation of SREBP-1. PMID: 21953514
  28. Lipin-1 phosphatidic phosphatase activity modulates phosphatidate levels to promote peroxisome proliferator-activated receptor gamma (PPARgamma) gene expression during adipogenesis. PMID: 22157014
  29. lipin 1 acts as a transcriptional coactivator through its direct interaction with peroxisome proliferator-activated receptor (PPAR) gamma coactivator-1alpha (PGC-1alpha) and PPARalpha(review) PMID: 21804322
  30. Data show that in the high-Chol diet apoE-KO mice, the mRNA and protein expression of lipin-1 and lipin-2 was markedly decreased. PMID: 21857965
  31. Estrogen-related receptor gamma (ERRgamma) is a novel transcriptional regulator of phosphatidic acid phosphatase, LIPIN1, and inhibits hepatic insulin signaling PMID: 21911493
  32. In lipin-1-depleted adipocytes, mRNA and protein expression levels of monocyte chemoattractant protein-1 (MCP-1) were significantly increased, although the other genes tested were not altered. PMID: 22033411
  33. Lpin1 expression in response to nutritional stress is controlled through the reactive oxygen species-ATM-p53 pathway. PMID: 22055193
  34. Study demonstrates that mTORC1 regulates SREBP by controlling the nuclear entry of lipin 1, a phosphatidic acid phosphatase; these findings establish lipin 1 as a key component of the mTORC1-SREBP pathway. PMID: 21816276
  35. lipin 1 is highly expressed in myocardium; hat cardiac lipin 1 expression is altered in response to physiologic and pathophysiologic stimuli that impact fatty acid metabolism PMID: 21549711
  36. Findings indicate that the hypotriglyceridemic effect of GW501516 in HFD-fed mice is accompanied by an increase in phospho-AMPK levels and the amplification of the PGC-1alpha-lipin 1-PPARalpha pathway. PMID: 21363937
  37. The involvement of phosphatidic acid phosphohydrolase 1 (PAP-1) and protein kinase C (PKC) in the Toll-like receptor-4 (TLR-4) activation of GIVA PLA(2), is demonstrated. PMID: 19230851
  38. Results identify a role for the lipin1 polybasic motif as both a lipid binding motif and a primary nuclear localization sequence. PMID: 20660155
  39. analysis of mRNA abundance and expression of SLC27A, ACC, SCD, FADS, LPIN, INSIG, and PPARGC1 gene isoforms in mouse mammary glands during the lactation cycle PMID: 20603810
  40. The functional interaction between lipin 1 and the nuclear factor of activated T cells c4 (NFATc4), is described. PMID: 20385772
  41. Studies suggest that insulin may modulate the cellular function of lipin-1 by regulating its subcellular localization through interactions with 14-3-3 proteins. PMID: 19955570
  42. Co-IP shows that lipin-1 forms a protein complex with MEF2c. PMID: 19753306
  43. Sumoylation mediates nuclear localization of lipin-1 alpha in neuronal cells. PMID: 19753306
  44. sumoylation facilitates the nuclear localization and transcriptional coactivator behavior of lipin-1alpha, which may act as a sumoylation-regulated transcriptional coactivator in brain PMID: 19753306
  45. Lpin1 null mutations lead to lipoatrophy of the epineurium, and to the dysregulation of a battery of genes required for the regulation of storage lipid metabolism in both the endoneurium and peri/epineurium PMID: 14522948
  46. Results suggest that lipin expression is required prior to peroxisome proliferator-activated receptor (PPAR)gamma during adipocyte differentiation. PMID: 15123608
  47. This review summarizes the recent discovery of lipin, a new factor with critical roles in both adipocyte development and function. PMID: 15753971
  48. the two lipin isoforms have distinct, but complementary, functions in adipogenesis, with lipin-alpha playing a primary role in differentiation and lipin-beta being predominantly involved in lipogenesis PMID: 16049017
  49. Lipin is a lipodystrophy and obesity gene PMID: 16054046
  50. effects of genetic variation in lipin levels on glucose homeostasis across species by analyzing lipin transcript levels in human and mouse adipose tissues PMID: 16357106

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Involvement in disease Defects in Lpin1 are the cause of the fatty liver dystrophy phenotype (fld). Fld mutant mices are characterized by neonatal fatty liver and hypertriglyceridemia that resolve at weaning, and neuropathy affecting peripheral nerve in adulthood. Adipose tissue deficiency, glucose intolerance and increased susceptibility to atherosclerosis are associated with this mutation too. Two independent mutant alleles are characterized in this phenotype, fld and fld2j.
Subcellular Location Isoform 1: Mitochondrion outer membrane, Cytoplasm, Nucleus membrane, Note=Recruited at the mitochondrion outer membrane following phosphatidic acid formation mediated by PLD6, In neuronals cells, isoform 1 is exclusively cytoplasmic, In 3T3-L1 pre-adipocytes, it primarily located in the cytoplasm, SUBCELLULAR LOCATION: Isoform 2: Nucleus, Cytoplasm, Endoplasmic reticulum membrane
Protein Families Lipin family
Tissue Specificity Specifically expressed in skeletal muscle. Also expressed prominently in adipose tissue, and testis. Lower expression also detected in kidney, lung, brain and liver. Isoform 1 is the predominant isoform in the liver. Isoform 2 is the major form in the bra
Database Links

KEGG: mmu:14245

STRING: 10090.ENSMUSP00000070583

UniGene: Mm.153625

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