REAGENT:

Anti-P-Perilipin 1-Serine 522 Antibody (Cat. 4856)

$500.00

Availability: In Stock

Online transactions are handled via PayPal.

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

  1. 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.
  2. 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.
  3. 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.

Interested in Learning More?

Please use this form to email Vala, or call today at (888) 742-VALA (8252).