REAGENT:
Anti-P-Perilipin 1-Serine 522 Antibody (Cat. 4856)
Description
Amount: 100 µL
Background: Lipid droplets are coated with a layer of proteins that regulate their growth and metabolism. The major lipid droplet-associated protein in adipocytes is perilipin [1]. Mice in which the endogenous gene for perilipin is knocked out have a lean phenotype due to reduced accumulation of fat [2,3], suggesting that perilipin may have a “gate-keeper” function under basal conditions to protect the triglycerides from metabolism by lipases. Upon activation of lipolytic pathways, perilipin is subject to phosphorylation at serine 497 and 522 by cyclic-AMP-dependent protein kinase, and phosphorylation of perilipin helps to recruit hormone sensitive lipase (HSL) to the lipid droplets.
Immunogen: Synthetic peptide corresponding to the carboxy terminus of the human perilipin sequence, near serine 522
Specificity/Target: Recognizes human perilipin 1 phosphorylated at serine 522 (equivalent to serine 517 of the murine sequence)
Species Reactivity: human, mouse (verified)
Tested Applications: Immunocytochemistry/immunofluorescence (ICC/IF), Western blotting (WB)
Recommended Dilutions: ICC/IF 1:30 | WB 1:5000
Storage: 4°C short-term; -20°C long-term
Available volume discounts and contract testing services.
This reagent has been featured in 39 peer-reviewed publications.

Human subcutaneous adipocytes were incubated in the presence and absence of the lipolytic activator Lys-3γ-MSH prior to being stained for nuclei (blue), lipid droplets (green), and phospho-perilipin (Ser 522) (red) using Vala Sciences’ lipid droplet staining kit (#4805) and mouse monoclonal antibody to phospho-perilipin (Ser 522) (# 4856).

Western blotting of protein extracts from 3T3L1 cells that were differentiated into adipocytes and treated with and without 6 µM forskolin. The phospho-perilipin (Ser 522) antibody (#4856) recognizes a distinct band at approximately 57 kD.
References
- Bickel PE, Tansey JT, Welte MA. PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores. Biochim Biophys Acta. Jun 2009;1791(6):419-440.
- Tansey JT, Sztalryd C, Gruia-Gray J, et al. Perilipin ablation results in a lean mouse with aberrant adipocyte lipolysis, enhanced leptin production, and resistance to diet-induced obesity. Proc Natl Acad Sci U S A. May 22 2001;98(11):6494-6499.
- Martinez-Botas J, Anderson JB, Tessier D, et al. Absence of perilipin results in leanness and reverses obesity in Lepr(db/db) mice. Nat Genet. Dec 2000;26(4):474-479.
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