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Mouse Anti-LPIN1 Recombinant Antibody (CBYJL-1919) (CBMAB-L1953-YJ)

Provided herein is a Mouse monoclonal antibody, which binds to Lipin 1 (LPIN1). The antibody can be used for immunoassay techniques, such as IHC-P, WB.
See all LPIN1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYJL-1919
Antibody Isotype
IgG1
Application
IHC-P, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Buffer
PBS, pH 7.3, 1% BSA, 50% Glycerol
Preservative
0.02% Sodium Azide
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
lipin 1
Introduction
LPIN1 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. 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, acute recurrent rhabdomyolysis, and autosomal recessive acute recurrent myoglobinuria (ARARM). LPIN1 is also a candidate for several human lipodystrophy syndromes.
Entrez Gene ID
23175
UniProt ID
Q14693
Alternative Names
PAP1; phosphatidate phosphatase LPIN1; EC 3.1.3.4
Function
Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis and therefore controls the metabolism of fatty acids at different levels (PubMed:20231281, PubMed:29765047).
Is involved in adipocyte differentiation (By similarity).
Acts also as nuclear transcriptional coactivator for PPARGC1A/PPARA regulatory pathway to modulate lipid metabolism gene expression (By similarity).
Recruited at the mitochondrion outer membrane and is involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol (By similarity).
Biological Process
Animal organ regenerationIEA:Ensembl
Cellular lipid metabolic processManual Assertion Based On ExperimentIBA:GO_Central
Cellular response to insulin stimulusManual Assertion Based On ExperimentIBA:GO_Central
Fatty acid catabolic processISS:UniProtKB
Mitotic nuclear membrane disassemblyTAS:Reactome
Negative regulation of myelinationIEA:Ensembl
Negative regulation of phosphatidate phosphatase activityIEA:Ensembl
Phosphatidic acid biosynthetic processIEA:Ensembl
Phosphatidic acid metabolic processIDA:UniProtKB
Positive regulation of cold-induced thermogenesisBy SimilarityISS:YuBioLab
Positive regulation of DNA replicationIEA:Ensembl
Positive regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIBA:GO_Central
Triglyceride biosynthetic processManual Assertion Based On ExperimentIDA:UniProtKB
Triglyceride mobilizationISS:UniProtKB
Cellular Location
Cytoplasm, cytosol
Endoplasmic reticulum membrane
Nucleus membrane
Translocates from the cytosol to the endoplasmic reticulum following acetylation by KAT5.
Involvement in disease
Myoglobinuria, acute recurrent, autosomal recessive (ARARM):
Recurrent myoglobinuria is characterized by recurrent attacks of rhabdomyolysis (necrosis or disintegration of skeletal muscle) associated with muscle pain and weakness and followed by excretion of myoglobin in the urine. Renal failure may occasionally occur.
PTM
Phosphorylated at multiple sites in response to insulin. Phosphorylation is controlled by the mTOR signaling pathway. Phosphorylation is decreased by epinephrine. Phosphorylation may not directly affect the catalytic activity but may regulate the localization. Dephosphorylated by the CTDNEP1-CNEP1R1 complex (By similarity).
Acetylation at Lys-425 and Lys-595 by KAT5 in response to fatty acids promotes translocation to the endoplasmic reticulum and synthesis of diacylglycerol.
Sumoylated.

Dai, W., Zheng, P., Luo, D., Xie, Q., Liu, F., Shao, Q., ... & Qian, K. (2022). LPIN1 is a regulatory factor associated with immune response and inflammation in sepsis. Frontiers in Immunology, 13, 820164.

Zhou, F., Fan, X., & Miao, Y. (2022). LPIN1 promotes triglycerides synthesis and is transcriptionally regulated by PPARG in buffalo mammary epithelial cells. Scientific Reports, 12(1), 2390.

Xu, Y., Chen, X., Zhao, C., Wang, X., Cheng, Y., Xi, F., ... & Yu, T. (2021). MiR-99b-5p attenuates adipogenesis by targeting SCD1 and Lpin1 in 3T3-L1 cells. Journal of Agricultural and Food Chemistry, 69(8), 2564-2575.

Tong, K., & Yu, G. S. (2021). Acute recurrent rhabdomyolysis in a Chinese boy associated with a novel compound heterozygous LPIN1 variant: a case report. BMC neurology, 21, 1-9.

Minton, T., Forrester, N., Al Baba, S., Urankar, K., & Brady, S. (2020). A rare case of adult onset LPIN1 associated rhabdomyolysis. Neuromuscular Disorders, 30(3), 241-245.

Che, R., Wang, C., Zheng, B., Zhang, X., Ding, G., Zhao, F., ... & Feng, Q. (2020). A rare case of pediatric recurrent rhabdomyolysis with compound heterogenous variants in the LPIN1. BMC pediatrics, 20(1), 1-6.

Chao, X., Guo, L., Wang, Q., Huang, W., Liu, M., Luan, K., ... & Luo, Q. (2020). miR-429-3p/LPIN1 axis promotes chicken abdominal fat deposition via PPARγ pathway. Frontiers in cell and developmental biology, 8, 595637.

Han, B., Yuan, Y., Liang, R., Li, Y., Liu, L., & Sun, D. (2019). Genetic effects of LPIN1 polymorphisms on milk production traits in dairy cattle. Genes, 10(4), 265.

Zhao, S., Li, J., Zhang, G., Wang, Q., Wu, C., Zhang, Q., ... & Yang, S. (2019). Exosomal miR-451a functions as a tumor suppressor in hepatocellular carcinoma by targeting LPIN1. Cell Physiol Biochem, 53(1), 19-35.

Sellers, R. S., Mahmood, S. R., Perumal, G. S., Macaluso, F. P., & Kurland, I. J. (2019). Phenotypic modulation of skeletal muscle fibers in LPIN1-deficient lipodystrophic (fld) mice. Veterinary pathology, 56(2), 322-331.

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For research use only. Not intended for any clinical use.

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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