Anti-Perilipin A/B 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.

synthetic peptide corresponding amino acid residues 6-17 of mouse and rat perilipin A/B with C-terminal added cysteine, conjugated to KLH. The corresponding human sequence differs by two residues.

Anti-Perilipin A/B antibody produced in rabbit has been used in immunoblotting and immunofluorescence staining.

Rabbit polyclonal anti-Perilipin A/B antibody is used to tag Perilipin A/B for detection and quantitation by immunocytochemical and immunohistochemical (IHC) techniques. It is used as a probe to determine the presence and roles of Perilipin A/B in the regulation of triacylglycerol storage in adipocytes.

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 cAMP-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), that is devoid of phosphorylation by PKA.

Rabbit polyclonal anti-Perilipin A/B antibody recognizes mouse Perilipin A/B by immunoblotting (46 kDa and ~62 kDa) and indirect immunofluorescence. Detection of the perilipin A and B bands by immunoblotting is specifically inhibited with the immunizing peptide.

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

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