Rabbit Anti-LIPIN1 Recombinant Antibody (CBYCL-357) (CBMAB-L0258-YC)

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Basic Information

Host Animal
Rabbit
Clone
CBYCL-357
Application
WB, IP, IF
Specificity
Human, Mouse
Antibody Isotype
IgG
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!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
More Infomation

Target

Full Name
Lipin 1
Introduction
LPIN1 (Lipin 1) is a protein coding gene. Diseases associated with LPIN1 include Myoglobinuria, Acute Recurrent, Autosomal Recessive and Genetic Recurrent Myoglobinuria. Among its related pathways are Cell Cycle, Mitotic and Adipogenesis.
Entrez Gene ID
Human23175
Mouse14245
UniProt ID
HumanQ14693
MouseQ91ZP3
Alternative Names
PAP1
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.

Jama, A., Alshudukhi, A. A., Burke, S., Dong, L., Kamau, J. K., Voss, A. A., & Ren, H. (2023). Lipin1 plays complementary roles in myofibre stability and regeneration in dystrophic muscles. The Journal of Physiology, 601(5), 961-978.

Song, L., Liu, Z., Hu, H. H., Yang, Y., Li, T. Y., Lin, Z. Z., ... & Lin, S. C. (2020). Proto-oncogene Src links lipogenesis via lipin-1 to breast cancer malignancy. Nature communications, 11(1), 5842.

Brohée, L., Crémer, J., Colige, A., & Deroanne, C. (2021). Lipin-1, a versatile regulator of lipid homeostasis, is a potential target for fighting cancer. International Journal of Molecular Sciences, 22(9), 4419.

Wang, M., Xie, M., Yu, S., Shang, P., Zhang, C., Han, X., ... & Chen, S. (2021). Lipin1 alleviates autophagy disorder in sciatic nerve and improves diabetic peripheral neuropathy. Molecular Neurobiology, 58, 6049-6061.

Schweitzer, G. G., Collier, S. L., Chen, Z., McCommis, K. S., Pittman, S. K., Yoshino, J., ... & Finck, B. N. (2019). Loss of lipin 1–mediated phosphatidic acid phosphohydrolase activity in muscle leads to skeletal myopathy in mice. The FASEB Journal, 33(1), 652.

Stepien, K. M., Schmidt, W. M., Bittner, R. E., O'Toole, O., McNamara, B., & Treacy, E. P. (2019). Long‐term outcomes in a 25‐year‐old female affected with lipin‐1 deficiency. JIMD reports, 46(1), 4-10.

Fan, X., Weng, Y., Bai, Y., Wang, Z., Wang, S., Zhu, J., & Zhang, F. (2018). Lipin‐1 determines lung cancer cell survival and chemotherapy sensitivity by regulation of endoplasmic reticulum homeostasis and autophagy. Cancer medicine, 7(6), 2541-2554.

Li, T. Y., Song, L., Sun, Y., Li, J., Yi, C., Lam, S. M., ... & Lin, S. C. (2018). Tip60-mediated lipin 1 acetylation and ER translocation determine triacylglycerol synthesis rate. Nature communications, 9(1), 1916.

Meana, C., García-Rostán, G., Peña, L., Lordén, G., Cubero, Á., Orduña, A., ... & Balboa, M. A. (2018). The phosphatidic acid phosphatase lipin-1 facilitates inflammation-driven colon carcinogenesis. JCI insight, 3(18).

Alshudukhi, A. A., Zhu, J., Huang, D., Jama, A., Smith, J. D., Wang, Q. J., ... & Ren, H. (2018). Lipin-1 regulates Bnip3–mediated mitophagy in glycolytic muscle. The FASEB Journal, 32(12), 6796.

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

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