This website uses cookies to ensure you get the best experience on our website.
- Table of Contents
Facts about Phosphatidate phosphatase LPIN1.
Acts also as nuclear transcriptional coactivator for PPARGC1A/PPARA regulatory pathway to modulate lipid metabolism gene expression. Is involved in adipocyte differentiation.
Mouse | |
---|---|
Gene Name: | Lpin1 |
Uniprot: | Q91ZP3 |
Entrez: | 14245 |
Belongs to: |
---|
lipin family |
DKFZp781P1796; EC 3.1.3.18; EC 3.1.3.4; EC 5.4.2.7; KIAA0188phosphatidate phosphatase LPIN1; Lipin 1; lipin-1; LPIN1; PAP1
Mass (kDA):
102.002 kDA
Mouse | |
---|---|
Location: | 12 A1.1|12 7.9 cM |
Sequence: | 12; |
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 brain.
If you're looking for a high-affinity primary antibody for use in cell culture experiments, Boster Bio is a company you should check out. This company offers many high-affinity prima antibodies for a variety uses. Learn more about Boster Bio, and the high-affinity prima antibodies it offers. You can also view the FAQs, Products, or other information.
Boster Bio has several primary anti-LPIN1 antibodies for research projects involving this protein. These antibodies have been validated in many different applications including Western Blotting, Immunohistochemistry, and ELISA. The Boster primary antibodies against LPIN1 can be used to confirm the marker's identity, which is crucial for accurate analysis of immunohistochemistry.
These high-affinity primary antibodies against LRIN1 allow researchers to ask more questions about specific proteins within a sample. These antibodies are dual-labelable, allowing researchers more information and questions about a specimen's function. All major histocompatibility tests are compatible with the Boster Bio primary antibodies.
A mutation in the LPIN1 gene was discovered in a family with a history involving adult-onset muscular weakness. The mutations were localized to the gene's protein and genome structure, and Sanger sequencing showed compound heterozygosity. Mutants had mutations R734Q and I683L, respectively. These mutations were highlighted in (*).
Multiple downstream genes regulate the gene LPIN1 including STEADG and PPAR. PPAR activates the retinoid-X receptor and binds to specific DNA sequences in the promoter region of its target genes, thereby affecting lipid metabolism and cell differentiation. PPARG promotes the synthesis of milkfat by regulating the transcriptions of ADRP (stearoyl-CoA desaturase 1), two enzymes that are necessary for the synthesis.
Human embryos born with a defect in LPIN1 can develop severe muscle phenotypes. Lipin1 deficiency can also affect the integrity neuromuscular synapses. This could be due to a defective response to touch. However, when lipin 1 mRNA is co-injected with the LPIN1wt mRNA, the defect can be rescued.
By binding to PPREs, PPARG can regulate LPIN1 gene transcription. PPARG could also regulate the expression of LPIN1.
Lipin 1 deficiencies are a common genetic defect that can cause muscular and neurological disorders. It was able to knock down over 70% of siRNA when it was introduced into mammalian cells. The siRNA-based knockdown produced abnormal levels of muscle and neuronal marker gene expressions. Quantitative analysis of gene expressions showed similar results. These results suggest a conserved role of LPIN1 for muscle gene expression.
PMID: 11792863 by Huffman T.A., et al. Insulin-stimulated phosphorylation of lipin mediated by the mammalian target of rapamycin.
PMID: 11138012 by Peterfy M., et al. Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin.