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Merck

P1998

Sigma-Aldrich

Anti-Perilipin A antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(e):

Anti-FPLD4, Anti-PERI, Anti-PLIN

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rabbit

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

antigen ~62 kDa

Speziesreaktivität

mouse, human

Methode(n)

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

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

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

Verwandte Kategorien

Allgemeine Beschreibung

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.

Immunogen

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.

Anwendung

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)

Biochem./physiol. Wirkung

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.

Physikalische Form

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

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

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)
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
Hao Yang et al.
Diabetes, 65(11), 3396-3409 (2016-08-25)
Obesity and type 2 diabetes are associated with impaired mitochondrial function in adipose tissue. To study the effects of primary deficiency of mitochondrial energy metabolism in fat, we generated mice with adipose-specific deficiency of fumarate hydratase (FH), an integral Krebs

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