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Description_x000D_
General description_x000D_
Perilipin is an intracellular neutral lipid storage droplet surface protein in white and brown fat adipocytes. It is also found in lower quantity coating droplets in steroidogenic-cells of the adrenal cortex, ovaries and testicular Leydig cells, on the surface of smaller droplets containing cholesteryl esters. Perilipin has multiple isoforms, resulting from differential splicing events. Perilipin A is most abundant in adipocytes and steroidogenic cells. Perilipin B is a minor form in adipocytes. Steroidogenic cells selectively express perilipins C and D._x000D_
Immunogen_x000D_
synthetic peptide corresponding to amino acid residues 492-505 of human perilipin A with C-terminal added cysteine, conjugated to KLH. The corresponding sequence differs by one residue in mouse and rat._x000D_
Application_x000D_
Anti-Perilipin A antibody produced in rabbit has also been used in:_x000D_
• indirect immunofluorescence_x000D_
• immunoblotting_x000D_
• immunohistochemistry_x000D_
Physical form_x000D_
Solution in 0.01 M phophate buffered saline, pH 7.4, containing 15 mM sodium azide._x000D_
Disclaimer_x000D_
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals._x000D_
Biochem/physiol Actions_x000D_
Perilipin is a gatekeeper protein that is involved in regulating triacylglycerol storage in adipocyte through the suppression of basal lipolysis apparently through protecting triacylglycerol against hydrolysis. Perilipin also enhances cyclic adenosine monophosphate (c-AMP)-dependent protein kinase (PKA)-stimulated lipolysis by hormone-sensitive lipase (HSL) and non-HSLs. Perilipin knockout mice exhibit reduced adipose tissue mass and resistance to diet induced obesity. Their lipid storage droplets are coated with adipose differentiation-related protein (ADRP, adipophilin), which is not phosphorylated by PKA.
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