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mouse trachea (courtesy of J.Heß, University Hospital Heidelberg) Zoom

mouse trachea (courtesy of J.Heß, University Hospital Heidelberg)

anti-Perilipin 1 (N-terminus) guinea pig polyclonal, serum

The antiserum reacts specifically with perilipin 1 located at the surface of intracellular storage lipid droplets present e.g. in the adrenal gland, adipocytes of white and brown adipose tissue, Leydig cells.
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Cat. No.: GP29
Quantity:  100 µL

Delivery Time: usually 1-7 working days

Excl. 19% Tax, excl. Shipping Cost

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Product description

Host guinea pig
Antibody Type polyclonal
Immunogen duplicated e N-terminus of mouse/ rat perilipin / PLIN1 (aa 1-20); MSMNKGPTLLDGDLPEQENV-C
Purification stabilized antiserum
Conjugate unconjugated
Formulation contains 0.09% sodium azide
Storage short term at 2 – 8 °C; long term storage in aliquots at - 20 °C; avoid freeze/ thaw cycles
Note centrifuge prior to opening
Intended use Research use only
Tested species reactivity bovine, human, mouse, rat


Tested applications Tested dilutions
Immunohistochemistry (IHC) - frozen 1:100 – 1:500
Immunohistochemistry (IHC) - paraffin 1:100 – 1:500 (microwave treatment recommended)
Western Blot (WB) 1:2,000



Perilipins build a family of phosphoproteins. The predominant forms in adipocytes, PLIN1 A and B arise by alternative RNA splicing from a single gene, generating polypeptides of 57 and 46 kD, respectively. The N-terminus, however, remains unchanged.
The antiserum reacts specifically with PLIN1 (A and B) located at the surface of intracellular storage lipid droplets present e.g. in the adrenal gland, adipocytes of white and brown adipose tissue and cultured cells such as 3T3-L1 adipocytes and cultured steroidogenic adrenal cortical and Leydig cells.
It also is a useful pathological marker since PLIN1 becames expressed de novo in hepatocyte steatogenesis.
The antiserum does not cross-react with ADRP (adipophilin, also named PLIN2) or TIP47 (also named PLIN3) proteins (or additional members of the PLIN/PAT-family, e.g. MLDP or OXPAT/PAT-1, also named PLIN5 or LSDP5).

Learn more about PROGEN Perilipin antibodies.



Bialešová, L. et al. Epigenetic Regulation of PLIN 1 in Obese Women and its Relation to Lipolysis. Sci.Rep. 7, 10152 (2017). human WB
Takahashi, Y. et al. Reciprocal Inflammatory Signaling Between Intestinal Epithelial Cells and Adipocytes in the Absence of Immune Cells. EBioMedicine. 23, 34-45 (2017). mouse IHC-IF (paraffin)
Furukawa, S., Nagaike, M. & Ozaki, K. Databases for technical aspects of immunohistochemistry. J. Toxicol. Pathol. 30, 79–107 (2017). rat IHC (paraffin)
Barquissau, V. et al. White-to-brite conversion in human adipocytes promotes metabolic reprogramming towards fatty acid anabolic and catabolic pathways. Mol. Metab. 5, 352–366 (2016). human WB
Gallardo-Montejano, V. I. et al. Nuclear Perilipin 5 integrates lipid droplet lipolysis with PGC-1a/SIRT1-dependent transcriptional regulation of mitochondrial function. Nat. Commun. 7, (2016). mouse WB
Inoue, J. et al. Identification of BCL11B as a regulator of adipogenesis. Sci. Rep. 6, 32750 (2016). mouse WB
Kozusko, K. et al. Clinical and molecular characterization of a novel PLIN1 frameshift mutation identified in patients with familial partial lipodystrophy Europe PMC Funders Group. Diabetes 64, 299–310 (2015). human, mouse WB
Frisdal, E. et al. Adipocyte ATP-Binding Cassette G1 Promotes Triglyceride Storage, Fat Mass Growth, and Human Obesity. Diabetes 64, 840–855 (2015). mouse WB, IHC (paraffin)
Heid, H. et al. On the formation of lipid droplets in human adipocytes: the organization of the perilipin-vimentin cortex. PLoS One 9, e90386 (2014). human WB, ICC-IF
Mcdonough, P. M. et al. Differential Phosphorylation of Perilipin 1A at the Initiation of Lipolysis Revealed by Novel Monoclonal Antibodies and High Content Analysis. PLoS One 8, (2013). mouse ICC-IF
Dahlhoff, M. et al. PLIN2, the major perilipin regulated during sebocyte differentiation, controls sebaceous lipid accumulation in vitro and sebaceous gland size in vivo NIH Public Access. Biochim. Biophys. Acta 1830, 4642–4649 (2013). human IHC (paraffin)
Stenson, B. M. et al. Liver X Receptor (LXR) Regulates Human Adipocyte Lipolysis. J. Biol. Chem. 286, 370–379 (2011). human WB
Straub, B. K. et al. Lipid droplet-associated PAT-proteins show frequent and differential expression in neoplastic steatogenesis. Mod. Pathol. 23, 480–492 (2010). human WB, IHC
Buers, I. et al. TIP47, a Lipid Cargo Protein Involved in Macrophage Triglyceride Metabolism. Arterioscler. Thromb. Vasc. Biol. 29, 767–773 (2009). human WB, ICC-IF
Alsted, T. J. et al. Adipose triglyceride lipase in human skeletal muscle is upregulated by exercise training. Am. J. Physiol. - Endocrinol. Metab. 296, E445–E453 (2008). human WB
Straub, B. K., Stoeffel, P., Heid, H., Zimbelmann, R. & Schirmacher, P. Differential pattern of lipid droplet-associated proteins and de novo perilipin expression in hepatocyte steatogenesis. Hepatology 47, 1936–1946 (2008). human, bovine WB, IHC
Muthusamy, K., Halbert, G. & Roberts, F. Immunohistochemical staining for adipophilin, perilipin and TIP47. J. Clin. Pathol. 59, 1166–1170 (2006). human IHC (paraffin)
Yamaguchi, T., Omatsu, N., Omukae, A. & Osumi, T. Analysis of interaction partners for perilipin and ADRP on lipid droplets∗. Mol. Cell. Biochem. 284, 167–173 (2006). mouse ICC-IF
Roepstorff, C. et al. Sex differences in hormone-sensitive lipase expression, activity, and phosphorylation in skeletal muscle at rest and during exercise. Am. J. Physiol. - Endocrinol. Metab. 291, E1106–E1114 (2006). human WB
Yamaguchi, T., Matsushita, S., Motojima, K., Hirose, F. & Osumi, T. MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha. J. Biol. Chem. 281, 14232–40 (2006). mouse WB, ICC-IF
Forcheron, F. et al. Genes of Cholesterol Metabolism in Human Atheroma: Overexpression of Perilipin and Genes Promoting Cholesterol Storage and Repression of ABCA1 Expression. Arterioscler. Thromb. Vasc. Biol. 25, 1711–1717 (2005). human, rat WB, IHC (paraffin)
Robenek, H., Robenek, M. J. & Troyer, D. PAT family proteins pervade lipid droplet cores. J. Lipid Res. 46, 1331–1338 (2005). human IEM
Rydén, M. et al. Targets for TNF-α-induced lipolysis in human adipocytes. Biochem. Biophys. Res. Commun. 318, 168–175 (2004). human WB

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