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AB60269

Anti-Perilipin-1 antibody

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(5 Publications)

Goat Polyclonal Perilipin-1 antibody. Suitable for WB and reacts with Human samples. Cited in 5 publications. Immunogen corresponding to Synthetic Peptide within Human PLIN1 aa 450-500.

View Alternative Names

PERI, PLIN, PLIN1, Perilipin-1, Lipid droplet-associated protein

1 Images
Western blot - Anti-Perilipin-1 antibody (AB60269)
  • WB

Unknown

Western blot - Anti-Perilipin-1 antibody (AB60269)

Primary incubation was 1 hour. Detected by chemiluminescence.

All lanes:

Western blot - Anti-Perilipin-1 antibody (ab60269) at 0.01 µg/mL

All lanes:

Human adipose lysate (35µg protein in RIPA buffer)

Predicted band size: 56 kDa

Observed band size: 60 kDa

false

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Synthetic Peptide within Human PLIN1 aa 450-500. The exact immunogen used to generate this antibody is proprietary information.

O60240

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
Purified from goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide.
Storage buffer
pH: 7.3 Preservative: 0.02% Sodium azide Constituents: Tris buffered saline, 0.5% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Perilipin-1 also known as PLIN1 is a protein with a mass of approximately 57 kDa. It plays an important role in lipid metabolism within adipose tissue. This protein is mainly found in adipocytes where it coats lipid droplets. By controlling the access of lipases to the lipid core Perilipin-1 regulates lipolysis. It prevents unnecessary breakdown of lipids by acting as a barrier and ensuring the protection and storage of energy reserves. This targeted regulation is important for maintaining energy homeostasis in the body.
Biological function summary

Perilipin-1 influences cellular energy balance and fat storage. It is an important member of the PAT family of proteins which includes perilipin A. Perilipin-1 does not typically form part of a larger protein complex; however it works closely with other proteins on the surface of lipid droplets. Its presence on the droplet surface is essential for controlling lipid mobilization particularly during fasting or energy-deprived states when organisms require a mechanism to access stored energy efficiently.

Pathways

The activity of Perilipin-1 is important in the lipolytic pathway. This pathway is involved in hydrolyzing stored triglycerides into free fatty acids and glycerol an essential process in energy metabolism. Perilipin-1 acts in tandem with hormone-sensitive lipase (HSL) to regulate this pathway. Upon activation by adrenaline or other stimuli perilipin-1 undergoes phosphorylation which in turn facilitates HSL translocation to the lipid droplet and enhances lipolysis. Besides its direct role Perilipin-1 also interacts with adipose triglyceride lipase (ATGL) further impacting lipid breakdown processes.

The dysfunction of Perilipin-1 can lead to metabolic diseases like obesity and type 2 diabetes. Abnormal regulation or mutations in the Perilipin-1 gene have been observed in these conditions affecting normal lipid metabolism. Disordered Perilipin-1 function can lead to excessive lipid storage impaired energy mobilization and increased insulin resistance. Additionally Perilipin-1 interacts indirectly with other proteins such as perilipin-2 which can also influence the development of these metabolic disorders. Understanding these interactions helps in exploring therapeutic strategies aimed at targeting lipid metabolism and related diseases.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase (HSL). Its absence may result in leanness. Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels.
See full target information PLIN1

Publications (5)

Recent publications for all applications. Explore the full list and refine your search

Science advances 11:eadu6998 PubMed40991692

2025

Steric repulsion counteracts ER-to-lipid droplet protein movement.

Applications

Unspecified application

Species

Unspecified reactive species

Alicia Damm,Mohyeddine Omrane,Ozren Stojanović,Bianca M Esch,Mehdi Zouiouich,Maxime Carpentier,Robin Klemm,Florian Fröhlich,Lionel Forêt,Abdou Rachid Thiam

Advanced science (Weinheim, Baden-Wurttemberg, Germany) 10:e2305042 PubMed37880864

2023

Unloading-Induced Skeletal Interoception Alters Hypothalamic Signaling to Promote Bone Loss and Fat Metabolism.

Applications

Unspecified application

Species

Unspecified reactive species

Qiaoyue Guo,Ningrong Chen,Kalp Patel,Mei Wan,Junying Zheng,Xu Cao

Nutrients 14: PubMed35807797

2022

Positive Effects of a Mediterranean Diet Supplemented with Almonds on Female Adipose Tissue Biology in Severe Obesity.

Applications

Unspecified application

Species

Unspecified reactive species

Óscar Osorio-Conles,Romina Olbeyra,Violeta Moizé,Ainitze Ibarzabal,Oriol Giró,Judith Viaplana,Amanda Jiménez,Josep Vidal,Ana de Hollanda

BioMed research international 2017:3795950 PubMed28133606

2017

Hypothyroidism Reduces the Size of Ovarian Follicles and Promotes Hypertrophy of Periovarian Fat with Infiltration of Macrophages in Adult Rabbits.

Applications

Unspecified application

Species

Unspecified reactive species

J Rodríguez-Castelán,M Méndez-Tepepa,Y Carrillo-Portillo,A Anaya-Hernández,J Rodríguez-Antolín,E Zambrano,F Castelán,E Cuevas-Romero

Journal of virology 84:6782-98 PubMed20335253

2010

Rotaviruses associate with cellular lipid droplet components to replicate in viroplasms, and compounds disrupting or blocking lipid droplets inhibit viroplasm formation and viral replication.

Applications

ICC/IF

Species

Rhesus monkey

Winsome Cheung,Michael Gill,Alessandro Esposito,Clemens F Kaminski,Nathalie Courousse,Serge Chwetzoff,Germain Trugnan,Nandita Keshavan,Andrew Lever,Ulrich Desselberger
View all publications

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