P1873
Anti-Perilipin A/B antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-FPLD4, Anti-PERI, Anti-PLIN
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About This Item
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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.
Specificity
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.
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.
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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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Aurelia Defour et al.
Human molecular genetics, 26(11), 1979-1991 (2017-03-24)
Repair of skeletal muscle after sarcolemmal damage involves dysferlin and dysferlin-interacting proteins such as annexins. Mice and patient lacking dysferlin exhibit chronic muscle inflammation and adipogenic replacement of the myofibers. Here, we show that similar to dysferlin, lack of annexin
The perilipin family of lipid droplet proteins: Gatekeepers of intracellular lipolysis
Sztalryd C and Brasaemle DL
Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, 1862(10), 1221-1232 (2017)
Lijun Wang et al.
PLoS biology, 16(11), e2006522-e2006522 (2018-11-14)
During the aging process, bone marrow mesenchymal stem cells (BMSCs) exhibit declined osteogenesis accompanied by excess adipogenesis, which will lead to osteoporosis. Here, we report that the H3 lysine 36 trimethylation (H3K36me3), catalyzed by histone methyltransferase SET-domain-containing 2 (SETD2), regulates
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
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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