|Application ||WB, IHC-P, IF, E|
|Other Accession||NP_001248357, 387528013|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||Predicted: 107 kDa |
Observed: 125 kDa
|Application Notes||LPIN1 antibody can be used for detection of LPIN1 by Western blot at 1 - 2 µg/mL.|
|Target/Specificity||LPIN1; LPIN1 antibody is human and mouse reactive. At least four isoforms of LPIN1 are known to exist.|
|Reconstitution & Storage||LPIN antibody can be stored at 4℃ for three months and -20℃, stable for up to one year.|
|Precautions||LPIN1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Plays important roles in controlling the metabolism of fatty acids at differents levels. Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the reticulum endoplasmic membrane. Acts also as a nuclear transcriptional coactivator for PPARGC1A/PPARA to modulate lipid metabolism gene expression (By similarity). Is involved in adipocyte differentiation. May also be involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol (By similarity).|
|Cellular Location||Nucleus membrane. Cytoplasm, cytosol. Endoplasmic reticulum membrane|
|Tissue Location||Specifically expressed in skeletal muscle. Also abundant in adipose tissue. Lower levels in some portions of the digestive tract.|
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Provided below are standard protocols that you may find useful for product applications.
LPIN1 Antibody: LPIN1, also known as PAP1, is 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 (reviewed in 1). LPIN1 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 (1,2). Mutations in LPIN1 are associated with metabolic diseases such as type 2 diabetes and recurrent acute myoglobinuria (3,4) and it is also a candidate for several human lipodystrophy syndromes (5).
Reue K and Zhang P. The lipin protein family: dual roles in lipid biosynthesis and gene expression. FEBS Lett. 2008; 582:90-6.
Peterfy M, Phan J, Xu P, et al. Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin. Nat. Genet. 2001; 27:121-4.
Zhang R, Jiang F, Hu C, et al. Genetic variants of LPIN1 indicate an association with Type 2 diabetes mellitus in a Chinese population. Diabet. Med. 2013; 30:118-22.
Zeharia A, Shaag A, Houtkooper RH, et al. Mutations in LPIN1 cause recurrent acute myoglobinuria in childhood. Am. J. Hum. Genet. 2008; 83:489-94.
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