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anti-Perilipin 2 (C-terminus) guinea pig polyclonal, serum

New specific marker for liposarcoma. Adipophilin/Perilipin 2 is present in milk fat globule membranes and on the surface of lipid droplets in various cultured cell lines; inducible by etomoxir. Detected in the glandular cells of lactating mammary gland, adrenal gland, Sertoli cells, in fat-accumulating hepatocytes of alcoholic cirrhotic fatty liver; In CD68-positive macrophages. Adipocytes are negative.
Cat. No.: GP41
Quantity:  100 µL

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€266.00
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Product description

Host guinea pig
Antibody Type polyclonal
Immunogen synthetic peptide (C-terminal aa 423 - 437 of human adipophilin)
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
Tested species reactivity human

Applications

Immunohistochemistry (IHC) - frozen 1:100 (for staining protocols see ref. Ohsaki et al. 2005)
Immunohistochemistry (IHC) - paraffin 1:100 (for staining protocol see Straub et al. 2008)
Western Blot (WB) 1:2,000

Background

Details

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 (see Heid et al. 1998 & 2013; for review see Targett-Adams et al.); inducible by etomoxir.

Enhanced expression of 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 the virus entry via lipid droplets (see Hope et al. 2002).

Polypeptide reacting: Adipophilin/ ADRP/ PLIN2, MW 48,100 (calculated from aa sequence data); apparent Mr 52,000 (after SDS-PAGE); pI 6.72

Tissue Immunolocalization: Adipophilin 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.

Reference

Reference

  1. Sastre, C. et al. Genetic deletion or TWEAK blocking antibody administration reduce atherosclerosis and enhance plaque stability in mice. J. Cell. Mol. Med. 18, 721–734 (2014).
  2. 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).
  3. Heid, H. et al. Lipid droplets, perilipins and cytokeratins--unravelled liaisons in epithelium-derived cells. PLoS One 8, e63061 (2013).
  4. Timmers, S. et al. Augmenting muscle diacylglycerol and triacylglycerol content by blocking fatty acid oxidation does not impede insulin sensitivity. Proc. Natl. Acad. Sci. USA 109, 11711–11716 (2012).
  5. Dichlberger, A. et al. Lipid body formation during maturation of human mast cells. J. Lipid Res. 52, 2198–208 (2011).
  6. Straub, B. K. et al. Lipid droplet-associated PAT-proteins show frequent and differential expression in neoplastic steatogenesis. Mod. Pathol. 23, 480–492 (2010).
  7. 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).
  8. 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).
  9. Targett-Adams, P. et al. Live Cell Analysis and Targeting of the Lipid Droplet-binding Adipocyte Differentiation-related Protein. J. Biol. Chem. 278, 15998–16007 (2003).
  10. Hope, R. G., Murphy, D. J. & McLauchlan, J. The Domains Required to Direct Core Proteins of Hepatitis C Virus and GB Virus-B to Lipid Droplets Share Common Features with Plant Oleosin Proteins. J. Biol. Chem. 277, 4261–4270 (2002).
  11. Imamura, M. et al. ADRP stimulates lipid accumulation and lipid droplet formation in murine fibroblasts. Am. J. Physiol. - Endocrinol. Metab. 283, E775–E783 (2002).
  12. Fukumoto, S. & Fujimoto, T. Deformation of lipid droplets in fixed samples. Histochem. Cell Biol. 118, 423–428 (2002).
  13. 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).
  14. 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).
  15. Buechler, C. et al. Adipophilin is a sensitive marker for lipid loading in human blood monocytes. Biochim. Biophys. Acta 1532, 97–104 (2001).
  16. Graham 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).
  17. 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).
  18. Heid, H. W., Lzer, M. S. & Keenan, T. W. Adipocyte differentiation-related protein is secreted into milk as a constituent of milk lipid globule membrane. Biochem. J 320, 1025–1030 (1996).

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