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P1998

Sigma-Aldrich

Anti-Perilipin A antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-FPLD4, Anti-PERI, Anti-PLIN

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About This Item

Numéro MDL:
MFCD07370428
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~62 kDa

Espèces réactives

mouse, human

Technique(s)

indirect immunofluorescence: 5-10 μg/mL using differentiated mouse NIH3T3-L1 cells.
western blot (chemiluminescent): 1-2 μg/mL using whole extract of differentiated mouse NIH3T3-L1 cells

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... PLIN(5346)
mouse ... Plin(103968)
rat ... Plin(25629)

Catégories apparentées

Description générale

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.

Immunogène

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.

Application

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)

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

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Characterization of Cre recombinase activity for in vivo targeting of adipocyte precursor cells
Krueger KC, et al.
Stem Cell Reports, 3(6), 1147-1158 (2014)
Absence of perilipin results in leanness and reverses obesity in Lepr db/db mice
Martinez BJ, et al.
Nature Genetics, 26(4), 474-474 (2000)
Ann-Cathrin Volz et al.
ALTEX, 35(4), 464-476 (2018-06-15)
Vascularized adipose tissue models are highly demanded as alternative to existing animal models to elucidate the mechanisms of widespread diseases, screen for new drugs or asses corresponding safety levels. Standardly used animal-derived sera therein, are associated to ethical concerns, the
Perilipins are associated with cholesteryl ester droplets in steroidogenic adrenal cortical and Leydig cells
Servetnick DA, et al.
The Journal of Biological Chemistry, 270(28), 16970-16973 (1995)
Jörn Söhle et al.
PloS one, 7(2), e31193-e31193 (2012-03-03)
Since the worldwide increase in obesity represents a growing challenge for health care systems, new approaches are needed to effectively treat obesity and its associated diseases. One prerequisite for advances in this field is the identification of genes involved in
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