Anti-Perilipin A antibody produced in rabbit

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.

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.

Anti-Perilipin A antibody produced in rabbit has also been used in:

• indirect immunofluorescence
• immunoblotting
• immunohistochemistry

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
Western Blotting (1 paper)

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.

Solution in 0.01 M phophate buffered saline, pH 7.4, containing 15 mM sodium azide.

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