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Merck

P1873

Anti-Perilipin A/B antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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A propos de cet article

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IF, WB CL
Citations:
54
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biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~62 kDa (also band at 46 kDa)

species reactivity

mouse

technique(s)

indirect immunofluorescence: 5-10 μg/mL using differentiated mouse NIH3T3-L1 cells, western blot (chemiluminescent): 2.5-5 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)

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.

Immunogen

synthetic peptide corresponding amino acid residues 6-17 of mouse and rat perilipin A/B with C-terminal added cysteine, conjugated to KLH. The corresponding human sequence differs by two residues.

Application

Anti-Perilipin A/B antibody produced in rabbit has been used in immunoblotting and immunofluorescence staining.
Rabbit polyclonal anti-Perilipin A/B antibody is used to tag Perilipin A/B for detection and quantitation by immunocytochemical and immunohistochemical (IHC) techniques. It is used as a probe to determine the presence and roles of Perilipin A/B in the regulation of triacylglycerol storage in adipocytes.

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 cAMP-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), that is devoid of phosphorylation by PKA.
Rabbit polyclonal anti-Perilipin A/B antibody recognizes mouse Perilipin A/B by immunoblotting (46 kDa and ~62 kDa) and indirect immunofluorescence. Detection of the perilipin A and B bands by immunoblotting is specifically inhibited with the immunizing peptide.

Physical form

Solution in 0.01 M phosphate 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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Classe de stockage

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Joshua D Currie et al.
Biology open, 8(7) (2019-07-07)
The heterogeneous properties of dermal cell populations have been posited to contribute toward fibrotic, imperfect wound healing in mammals. Here we characterize an adult population of dermal fibroblasts that maintain an active Prrx1 enhancer which originally marked mesenchymal limb progenitors.
The amino and carboxyl termini of perilipin a facilitate the storage of triacylglycerols
Garcia A, et al.
The Journal of Biological Chemistry, 279(9), 8409-8416 (2004)
Takehiro Kasai et al.
The American journal of pathology, 187(12), 2627-2634 (2017-09-19)
Fatty degeneration of skeletal muscle leads to muscle weakness and loss of function. Preventing fatty degeneration in skeletal muscle is important, but no drug has been used clinically. In this study, we performed drug repositioning using human platelet-derived growth factor
Reestablishment of energy balance in a male mouse model with POMC neuron deletion of BMPR1A
Townsend KL, et al.
Endocrinology, 158(12), 4233-4245 (2017)
Christian Elabd et al.
Nature communications, 5, 4082-4082 (2014-06-11)
The regenerative capacity of skeletal muscle declines with age. Previous studies suggest that this process can be reversed by exposure to young circulation; however, systemic age-specific factors responsible for this phenomenon are largely unknown. Here we report that oxytocin--a hormone

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