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MABS1942-25UG
Sigma-AldrichAnti-Perilipin-1 Antibody, clone Peri 112.17.1
Anti-Perilipin-1, clone Peri 112.17.1, Cat. No. MABS1942, is a mouse monoclonal antibody that detects Perilipin-1 and has been tested for use in Electron Microscopy, Immunocytochemistry, Immunohistochemistry, Immunoprecipitation, and Western Blotting.
More>>Anti-Perilipin-1, clone Peri 112.17.1, Cat. No. MABS1942, is a mouse monoclonal antibody that detects Perilipin-1 and has been tested for use in Electron Microscopy, Immunocytochemistry, Immunohistochemistry, Immunoprecipitation, and Western Blotting. Less<<
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Übersicht
Replacement Information
Description
Catalogue Number
MABS1942-25UG
Description
Anti-Perilipin-1 Antibody, clone Peri 112.17.1
Alternate Names
Lipid droplet-associated protein
Background Information
Perilipin-1 (UniProt: O60240; also known as Lipid droplet-associated protein) is encoded by the PLIN1 (also known as PERI, PLIN) gene (Gene ID: 5346) in human. Perilipins are lipid droplet (LD)- binding proteins that are required for optimal lipid storage and fatty acid release. In mammals the perilipin family of comprises five members: perilipin, adipophilin, TIP47, S3-12 and MLDP/OXPAT (also named PLIN1-5. Perilpin-1 is a modulator of adipocyte lipid metabolism that is detected in adipocytes and is also shown to be expressed in hepatocytes of human steatotic liver. It coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase. It is shown to play a role in unilocular lipid droplet formation by activating cell death inducing DFFA like effector c (CIDEC). Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. In adipocytes, perilipin-1 can undergo phosphorylation by protein kinase A that changes its conformation and permits lipolysis by hormone-sensitive lipase. Perilipin knockout mice are lean and display aberrant adipocyte lipolysis, enhanced leptin production, and resistance to diet-induced obesity. Mutations in PLIN1 gene are linked to familial lipodystrophy that is characterized by loss of subcutaneous adipose tissue primarily affecting the lower limbs, insulin-resistant diabetes mellitus, hypertriglyceridemia, and hypertension. (Ref.: Straub, BK et al. (2008). Hepatology. 47(6); 1936-1946; Tansey JT., et al. (2004). IUBMB Life. 56(7); 379-385).
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Applications
Application
Anti-Perilipin-1, clone Peri 112.17.1, Cat. No. MABS1942, is a mouse monoclonal antibody that detects Perilipin-1 and has been tested for use in Electron Microscopy, Immunocytochemistry, Immunohistochemistry, Immunoprecipitation, and Western Blotting.
Key Applications
Electron Microscopy
Immunocytochemistry
Immunohistochemistry
Immunoprecipitation
Western Blotting
Application Notes
Immunoprecipitation Analysis: A representative lot immunoprecipitated Perilipin-1 in Immunoprecipitation applications (Heid, H., et. al. (2014). PLoS One. 9(2):e90386).
Immunohistochemistry (Paraffin) Analysis: A 1:250 dilution from a representative lot detected Perilipin-1 in human breast and lipoma tissue sections.
Electron Microscopy Analysis: A representative lot detected Perilipin- positive lipid droplets by Immunoelectron Microscopy applications (Heid, H., et. al. (2014). PLoS One. 9(2):e90386).
Immunocytochemistry Analysis: A representative lot detected Perilipin-1 in Immunocytochemistry applications (Heid, H., et. al. (2014). PLoS One. 9(2):e90386).
Western Blotting Analysis: A representative lot detected Perilipin-1 in Western Blotting applications (Heid, H., et. al. (2014). PLoS One. 9(2):e90386).
Biological Information
Immunogen
KLH-conjugated linear peptide corresponding to first 20 amino acids from the N-terminal region of human Perilipin-1.
Clone
Peri 112.17.1
Concentration
Please refer to lot specific datasheet.
Host
Mouse
Specificity
Clone Peri 112.17.1 is a mouse monoclonal antibody that detects Perilipin-1. It targets an epitope within 20 amino acids from the N-terminal region.
~ 65 KDa observed; 55.99 kDa calculated. Uncharacterized bands may be observed in some lysate(s).
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blotting in NIH3T3/L1 cell lysate.
Western Blotting Analysis: A 1:500 Dilution of this antibody detected Perilipin-1 in NIH3T3/L1 cell lysate.
Usage Statement
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.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at 2-8°C from date of receipt.
Packaging Information
Material Size
25 μg
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Bestellnummer
GTIN
MABS1942-25UG
04061841276715
Documentation
Anti-Perilipin-1 Antibody, clone Peri 112.17.1 SDB
On the formation of lipid droplets in human adipocytes: the organization of the perilipin-vimentin cortex. Heid, H; Rickelt, S; Zimbelmann, R; Winter, S; Schumacher, H; Dörflinger, Y; Kuhn, C; Franke, WW PLoS One
9
e90386
2014
We report on the heterogeneity and diversity of lipid droplets (LDs) in early stages of adipogenesis by elucidating the cell and molecular biology of amphiphilic and cytoskeletal proteins regulating and stabilizing the generation of LDs in human adipose cells. A plethora of distinct and differently sized LDs was detected by a brief application of adipocyte differentiation medium and additional short treatment with oleic acid. Using these cells and highly specific antibodies for LD-binding proteins of the perilipin (PLIN) family, we could distinguish between endogenously derived LDs (endogenous LDs) positive for perilipin from exogenously induced LDs (exogenous LDs) positive for adipophilin, TIP47 and S3-12. Having optimized these stimulation conditions, we used early adipogenic differentiation stages to investigate small-sized LDs and concentrated on LD-protein associations with the intermediate-sized filament (IF) vimentin. This IF protein was described earlier to surround lipid globules, showing spherical, cage-like structures. Consequently - by biochemical methods, by immunofluorescence microscopy and by electron- and immunoelectron microscopy - various stages of emerging lipid globules were revealed with perilipin as linking protein between LDs and vimentin. For this LD-PLIN-Vimentin connection, a model is now proposed, suggesting an interaction of proteins via opposed charged amino acid domains respectively. In addition, multiple sheaths of smooth endoplasmic reticulum cisternae surrounding concentrically nascent LDs are shown. Based on our comprehensive localization studies we present and discuss a novel pathway for the LD formation.