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anti-Perilipin 2 (N-terminus) mouse monoclonal, AP125, purified

Positive in glandular cells of lactating mammary gland, zona fasciculata of the adrenal gland, Sertoli cells, and in fat-accumulating hepatocytes of alcoholic cirrhotic fatty liver; adipocytes are negative. Specific detection of liposarcoma.
Cat. No.: 610102
Quantity:  50 µg

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Product description

Host mouse
Antibody Type monoclonal
Isotype IgG1
Clone AP125
Immunogen synthetic peptide (aa 5-27 from N-terminus of human adipophilin/ PLIN2)
Purification affinity chromatography
Conjugate unconjugated
Formulation lyophilized; reconstitute in 1 ml dist. water (final solution contains 0.09 % sodium azide, 0.5% BSA in PBS buffer, pH 7.4)
Storage short term at 2 – 8 °C; long term storage in aliquots at - 20 °C; avoid freeze/ thaw cycles
Tested species reactivity dog, human, rat (negative with bovine, mouse)

Applications

Tested applications Tested dilutions
Immunohistochemistry (IHC) - frozen 1:10
Immunohistochemistry (IHC) - paraffin assay dependent (microwave treatment recommended)
Western Blot (WB) assay dependent

Background

Details

Perilipin 2/ Adipophilin/ ADRP/ PLIN2 is a ubiquitous component of lipid droplets. It has been found in milk fat globule membranes and on the surface of lipid droplets in various cultured cell lines; inducible by etomoxir.
Enhanced expression of Perilipin 2/ Adipophilin/ ADRP/ PLIN2 is a useful marker for pathologies characterized by increased lipid droplet accumulation. Such diseases include atheroma, steatosis, obesity and certain cases of liposarcoma. It also seems to be a potent marker for atherosclerosis. ADRP can also be used to study virus entry via lipid droplets.
Polypeptide reacting: Perilipin 2/ Adipophilin/ ADRP/ PLIN2, MW 48,100 (calculated from aa sequence data); apparent Mr 52,000 (after SDS-PAGE); pI 6.72
Immunolocalization: Perilipin 2/ Adipophilin/ ADRP/ PLIN2 is positively detected in the glandular cells of lactating mammary gland (ductal cells are negative), zona fasciculata of the adrenal gland, Sertoli cells of the testis, and in fat-accumulating hepatocytes of alcoholic cirrhotic fatty liver; adipocytes are negative.Also positively stained are lipid-storing CD 68-positive macrophages.
Tested cultured cell lines: Caco, PLC, HaCat, SV80, RD 125, HUVEC, RV, PC-12, MDCK

Learn more about PROGEN Perilipin antibodies.

Reference

Reference

PublicationSpeciesApplication
Ramos, S. V et al. Higher PLIN5 but not PLIN3 content in isolated skeletal muscle mitochondria following acute in vivo contraction in rat hindlimb. Physiol. Reports 2, (2014). rat WB
Heid, H. et al. On the formation of lipid droplets in human adipocytes: the organization of the perilipin-vimentin cortex. PLoS One 9, (2014). human ICC-IF
Pfisterer, S. G. et al. Lipid droplet and early autophagosomal membrane targeting of Atg2A and Atg14L in human tumor cells. J. Lipid Res. 55, 1267–78 (2014). human WB, ICC-IF
Straub, B. K. et al. Adipophilin/perilipin-2 as a lipid droplet-specific marker for metabolically active cells and diseases associated with metabolic dysregulation. Histopathology 62, 617–631 (2013). human IHC (paraffin)
Macpherson, R. E. K., Vandenboom, R., Roy, B. D. & Peters, S. J. Skeletal muscle PLIN3 and PLIN5 are serine phosphorylated at rest and following lipolysis during adrenergic or contractile stimulation. Physioligal Reports 1, (2013). rat WB
MacPherson, R. E. K., Ramos, S. V, Vandenboom, R., Roy, B. D. & Peters, S. J. Skeletal muscle PLIN proteins, ATGL and CGI-58, interactions at rest and following stimulated contraction. Am. J. Physiol. Regul. Integr. Comp. Physiol. 304, R644-50 (2013). rat WB, Co-IP
Heid, H. et al. Lipid droplets, perilipins and cytokeratins--unravelled liaisons in epithelium-derived cells. PLoS One 8, (2013). human WB, ICC-IF, IP
Lin, P. et al. Efficient Lentiviral Transduction of Human Mesenchymal Stem Cells That Preserves Proliferation and Differentiation Capabilities. Stem Cells Transl. Med. 1, 886–897 (2012). human ICC-IF
Dichlberger, A. et al. Lipid body formation during maturation of human mast cells. J. Lipid Res. 52, 2198–208 (2011). human WB, ICC-IF
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
Ostler, D. A. et al. Adipophilin expression in sebaceous tumors and other cutaneous lesions with clear cell histology: an immunohistochemical study of 117 cases. Mod. Pathol. 23, 567–573 (2010). human IHC (paraffin)
Ingelmo-Torres, M. et al. Hydrophobic and Basic Domains Target Proteins to Lipid Droplets. Traffic 10, 1785–1801 (2009). monkey ICC-IF
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
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 WB, IHC
Robenek, H. et al. Butyrophilin controls milk fat globule secretion. Proc. Natl. Acad. Sci. USA 103, 10385–10390 (2006). bovine ICC-IF, IEM
Muthusamy, K., Halbert, G. & Roberts, F. Immunohistochemical staining for adipophilin, perilipin and TIP47. J. Clin. Pathol. 59, 1166–1170 (2006). human IHC (paraffin)
Robenek, H. et al. Adipophilin-enriched domains in the ER membrane are sites of lipid droplet biogenesis. J. Cell Sci. 119, 4215–4224 (2006). human WB
Larigauderie, G. et al. Adipophilin increases triglyceride storage in human macrophages by stimulation of biosynthesis and inhibition of β-oxidation. FEBS J. 273, 3498–3510 (2006). human WB
Robenek, H., Lorkowski, S., Schnoor, M. & Troyer, D. Spatial Integration of TIP47 and Adipophilin in Macrophage Lipid Bodies. J. Biol. Chem. 280, 5789–5794 (2005). human WB, ICC-IF, IEM
Robenek, H. et al. Lipid Droplets Gain PAT Family Proteins by Interaction with Specialized Plasma Membrane Domains. J. Biol. Chem. 280, 26330–26338 (2005). human ICC-IF, IEM
Robenek, H., Robenek, M. J. & Troyer, D. PAT family proteins pervade lipid droplet cores. J. Lipid Res. 46, 1331–1338 (2005). human IEM
Ohsaki, Y., Maeda, T. & Fujimoto, T. Fixation and permeabilization protocol is critical for the immunolabeling of lipid droplet proteins. Histochem. Cell Biol. 124, 445–452 (2005). human ICC-IF
Fukumoto, S. & Fujimoto, T. Deformation of lipid droplets in fixed samples. Histochem. Cell Biol. 118, 423–8 (2002). human ICC-IF
Fujimoto, T., Kogo, H., Ishiguro, K., Tauchi, K. & Nomura, R. Caveolin-2 Is Targeted to Lipid Droplets, a New " Membrane Domain " in the Cell. J. Cell Biol. 152, 1079–1085 (2001). human WB
Ostermeyer, A. G. et al. Accumulation of Caveolin in the Endoplasmic Reticulum Redirects the Protein to Lipid Storage Droplets. J. Cell Biol. 152, 1071–1078 (2001). human ICC-IF
Buechler, C. et al. Adipophilin is a sensitive marker for lipid loading in human blood monocytes. Biochim. Biophys. Acta 1532, 97–104 (2001). human WB
Hope, R. & McLauchlan, J. Sequence motifs required for lipid droplet association and protein stability are unique to the hepatitis C virus core protein. J. Gen. Virol. 81, 1913–1925 (2000). syrian hamster WB
Heid, H. W., Moll, R., Schwetlick, I., Rackwitz, H. R. & Keenan, T. W. Adipophilin is a specific marker of lipid accumulation in diverse cell types and diseases. Cell Tissue Res. 294, 309–21 (1998). human, rat, dog IHC (frozen), ICC-IF, IEM

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