| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| IHC | 1:50-1:200 |
| FC | 1:50-1:200 |
LPIN1, also known as Lipin-1, serves as a critical regulator of lipid metabolism through its phosphatidate phosphatase activity, catalyzing the conversion of phosphatidic acid to diacylglycerol in the glycerolipid biosynthesis pathway. Beyond its enzymatic function, LPIN1 acts as a transcriptional coactivator influencing genes involved in fatty acid oxidation and adipogenesis. Dysregulation of LPIN1 has been implicated in metabolic disorders, lipodystrophy, and rhabdomyolysis, making it a compelling target for researchers investigating lipid homeostasis, metabolic disease mechanisms, and cellular energy balance.
This recombinant monoclonal antibody, generated against a synthetic peptide derived from human LPIN1, offers the reproducibility and sequence-defined consistency that demanding experimental workflows require. As a recombinant clone, it eliminates the lot-to-lot variability often encountered with traditional hybridoma-derived antibodies, ensuring your results remain comparable across extended studies.
Validation across multiple platforms demonstrates this antibody's versatility in your research toolkit. Western blot analysis in A549 whole cell lysate reveals a band at approximately 130 kDa, which exceeds the predicted molecular weight of 99 kDa. This size difference likely reflects post-translational modifications, particularly phosphorylation events known to regulate LPIN1 activity and localization. Immunohistochemistry performed on paraffin-embedded human kidney tissue confirms utility in tissue-based studies, while flow cytometry analysis in SH-SY5Y neuroblastoma cells demonstrates effective detection in single-cell applications.
Whether you are investigating adipocyte differentiation, hepatic lipid metabolism, or the molecular basis of metabolic myopathies, this antibody provides a reliable detection tool for interrogating LPIN1 expression and distribution across diverse experimental contexts.
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