P1998
Anti-Perilipin A antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-FPLD4, Anti-PERI, Anti-PLIN
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biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~62 kDa
species reactivity
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
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... PLIN(5346)
mouse ... Plin(103968)
rat ... Plin(25629)
Related Categories
General description
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.
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)
Immunohistochemistry (1 paper)
Western Blotting (1 paper)
Biochem/physiol Actions
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.
Physical form
Solution in 0.01 M phophate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
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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Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Find documentation for the products that you have recently purchased in the Document Library.
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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