rev:  December 28, 2004

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  ANTIBODIES  

(anti-Human and others as indicated)

RDI Divison of researchd Industries Intl  offers a wide line of  antibodies. Since no one antibody works best for all applications (neutralization, blotting, ELISA, etc), we offer many different types of antibodies to help solve this problem. Please inquire for other applications or types of antibodies not listed below.


PERILIPIN (see below 1 guinea pig polyclonal and 2 rabbit polyclonals)
Guinea Pig (Polyclonal Antibody) to Perilipin

Cat#RDI-PROGP29        $469.00

Category                          Guinea Pig polyclonal

Form/Purification             Whole antiserum

Immunogen                        Duplicated N-terminus of perilipin (cf, Greenberg et al, 1992, JBC 266, 11341-11346)

Description/Specificity   Perilipins build a family of phosphoproteins. The predominat forms in adipocytes, perilipin A and B arise by alternative RNA splicing from a single gene, generating polypeptides of 57 and 46kd, respectively. The N-terminus, however, remains unchanged.

The antiserum reacts specifically with perilipins located at the surface of intracellular storage lipid droplets present e.g. in the adrenal gland, adipocytes of white and brown adipose tissue and cultured cells such as 3T3-L1 and adipocytes and cultured steriodogenic adrenal cortical and Leydig cells.

Species tested so far             Human , rat and mouse

Application           -Immunohistochemistry on frozen sections

                             -paraffin sections ( with high temp antigen retrieval)

                             - immunoblotting

Working Dilution      1:100-1:200 for immunohistochemistry

                                -1:2000 for western blotting (chemiluminescence detection)

Incubation time:       1 hour at RT, extended for paraffin sections

Storage                     At 2-8°C one year

Quantity / Volume    100ul; contains 0.09% sodium azide

Ref:

Blanchette-Mackle EJ, Dwyer NK, Barber T, Coxey RA, Takeda T, Ronidine CM  Theodorakis JL, Greenberg AS, Londos C. Perilipin is lcoated on thesurface layer of intracellular lipid droplets in adipocytes. J. Lipid Res 36(6) 1211-1226 (1995)

Souza SA, LM de Vargas, MT Yamato, P Lien, MD Franciosa, LG Moss and AS Greenberg. Overexpression of Perilipin A and B Blocks the ability of Tumor Necrosis Factor Alpha to  Increase Lipolysis in 3T3-L1 adipocytes. JBC 273(38), 24665-24669 (1998)

Heid HW, Moll R, Schwetlick I, Rackwitz HR, TW Keenan. Adipophilin Is a specific marker of  lipid accumulation in diverse cell types and dseases. Cell Tissue res 294, 309-321 (1998)

Wolins NE, et al, TIP47 associates with lipd droplets J Biol Chem 276:5101-5108 (2001)

Martinez-Botas et al, Absence of perilipin results in leaness and reverses obesity in Lep(db/db) mice Nat. Genet 26,474-479 (2000)

Ryden M et al:Targets for TNF-alpha induced lipolysis in human adipocytes, Biochem Biophys Res Com 318, 168-175 (2004)


Perilipin C is not detectable in Western blots  of steroidogenic tissue, although expressed abundantly together with perilipin A. Our antibody  detects perilipin A, B and C, which are splice variants of perilipin.

J Biol Chem 1995 Jul 14;270(28):16970-3

Perilipins are associated with cholesteryl ester droplets in steroidogenic adrenal cortical and Leydig cells. Servetnick DA, Brasaemle DL, Gruia-Gray J, Kimmel AR, Wolff J, Londos C Laboratory of Cellular and Developmental Biology, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA.

Steroidogenic cells store cholesteryl esters, precursors for steroid hormone synthesis, in  intracellular lipid droplets. Cholesteryl ester hydrolysis is activated by protein kinase A and  catalyzed by cholesteryl esterase. The esterase is similar, if not identical, to hormone-sensitive  lipase in adipocytes where an analogous lipolytic mechanism occurs. Perilipins, proteins located exclusively at lipid droplet surfaces in adipocytes, are polyphosphorylated by protein kinase A in response to lipolytic stimuli, suggesting a role for these proteins in mediating lipid metabolism. The present study reveals that perilipins are associated with cholesteryl ester droplets in two steroidogenic cell lines: Y-1 adrenal cortical cells and MA-10 Leydig cells. The relative abundance of perilipin mRNAs and protein is much less in steroidogenic cells than in adipocytes. Like adipocytes, steroidogenic cells express perilipin A; additionally, the latter cells contain relatively abundant amounts of perilipin C, a protein that is not detectable in adipocytes by Western analysis. The data suggest a strong link between perilipins and lipid hydrolysis that is mediated by the hormone-sensitive lipase/cholesteryl esterase class of enzymes.

PMID: 7622516, UI: 95348130

-For Research Use Only


Rabbit anti-Perilipin A (Mouse, Rat/Human)

cat# RDI-PERLIPAabr   $469.00/100ul

Package: 100 ul of affinity purified rabbit serum with 0.05% sodium azide. Store at -20C. Avoid repeated freeze/thaw cycles.

Immunogen: Synthetic Peptide: C E(502 ) P I L G R T Q Y S Q L R K K S(517)

Use: -western blot 1:1000

-detects perilipin A from 3T3-L1 cell extract. It has been successfully used in Western blot procedures. By Western blot, this antibody detects an ~62 kDa protein representing perilipin A from 3T3-L1 cell extract

The immunizing peptide corresponds to amino acid residues 502-517 from rat perilipin A. This sequence is 93% conserved in humans. This peptide (cat#RDI-PERILIPA-CP $156.00/50ug) is available for use in neutralization and control experiments.

Background: Adipose tissue is an energy reserve in animals and is strictly regulated in nondomestic species. Adipose cells produce and secrete numerous physiologically important proteins, such as lipoprotein lipase (LPL), leptin, adipocyte complement related protein of 30 kDa (Acrp30), resistin, and perilipin. Perilipin is an intracellular neutral lipid droplet protein that is hormonally regulated. This protein is localized exclusively to the surface of lipid droplets. In response to lypotic stimuli, perilipin is phosphorylated by protein kinase A. Once activated, perilipin has inhibitory affects upon hormone-sensitive lipase (HSL), a protein that mediates the hydrolysis of triacylglycerol, the major form of stored energy in the body.

Perilipin expression is limited to adipocytes and steroidogenic cells. There are currently two known isoforms, Perilipin A and B. Both of these proteins are encoded by a single-copy gene and are the result of differential splicing events.

For Research Use Only


Rabbit anti-Perilipin A/B (Mouse, Rat/Human)

cat# RDI-PERLIPABabr   $469.00/100ul

Package: 100 ul of affinity purified rabbit serum with 0.05% sodium azide. Store at -20C. Avoid repeated freeze/thaw cycles.

Immunogen: Synthetic Peptide: M(1) S M N K G P T L L D G D L P E Q(17) C

Use: -western blot 1:1000

-detects perilipin A and B from 3T3-L1 cell extract. It has been successfully used in Western blot procedures. By Western blot, this antibody detects ~62 and 46 kDa proteins representing perilipin A and B, respectively from 3T3-L1 cell extract

The immunizing peptide corresponds to amino acid residues 1-17 from rat perilipin A and B. This sequence is 82% conserved in humans. This peptide (cat#RDI-PERILIPAB-CP $156.00/50ug) is available for use in neutralization and control experiments.

Background: Adipose tissue is an energy reserve in animals and is strictly regulated in nondomestic species. Adipose cells produce and secrete numerous physiologically important proteins, such as lipoprotein lipase (LPL), leptin, adipocyte complement related protein of 30 kDa (Acrp30), resistin, and perilipin. Perilipin is an intracellular neutral lipid droplet protein that is hormonally regulated. This protein is localized exclusively to the surface of lipid droplets. In response to lypotic stimuli, perilipin is phosphorylated by protein kinase A. Once activated, perilipin has inhibitory effects upon hormone-sensitive lipase (HSL), a protein that mediates the hydrolysis of triacylglycerol, the major form of stored energy in the body.

Perilipin expression is limited to adipocytes and steroidogenic cells. There are currently two known isoforms, Perilipin A and B. Both of these proteins are encoded by a single-copy gene and are the result of differential splicing events.

For Research Use Only

see also guinea pig anti-perilipin cat#RDI-PROGP29 $469.00

and rabbit anti-perilipin A cat#RDI-PERLIPAabr      $469.00/100ul


need a secondary antibody?


RDI Divison of researchd Industries Intl

San Jose, 95123 CA Snell ave 658

USA

phone (800) 370-2222

      or (978) 371-6446 or (800) 370-2222

EMAIL:margaret@cellular-research.com

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