Revision 1

#12589Store at -20C

1 Kit

(7 x 20 microliters)

Cell Signaling Technology

Orders: 877-616-CELL (2355) [email protected]

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For Research Use Only. Not for Use in Diagnostic Procedures.
Product Includes Product # Quantity Mol. Wt Isotype/Source
Acetyl-CoA Carboxylase (C83B10) Rabbit mAb 3676 20 µl 280 kDa Rabbit IgG
Adiponectin (C45B10) Rabbit mAb 2789 20 µl 27 kDa Rabbit IgG
C/EBPα (D56F10) XP® Rabbit mAb 8178 20 µl 42, 28 kDa Rabbit IgG
FABP4 Antibody 2120 20 µl 15 kDa Rabbit 
Fatty Acid Synthase (C20G5) Rabbit mAb 3180 20 µl 273 kDa Rabbit IgG
Perilipin-1 (D1D8) XP® Rabbit mAb 9349 20 µl 62 kDa Rabbit IgG
PPARγ (C26H12) Rabbit mAb 2435 20 µl 53, 57 kDa Rabbit IgG
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl Goat 

Please visit cellsignal.com for individual component applications, species cross-reactivity, dilutions, protocols, and additional product information.

Description

The Adipogenesis Marker Antibody Sampler Kit provides an economical means to evaluate proteins involved in the regulation of adipogenesis. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Background

Adipocytes are the primary cellular component of adipose tissue and play a key role in the storage of triacylglycerol. Adipogenesis is the cellular process where preadipocytes differentiate into adipocytes.

Fatty acid binding proteins (FABPs) act as cytoplasmic lipid chaperones by binding fatty acids and lipids for transport to various cellular pathways (1,2). The predominant fatty acid binding protein found in adipocytes is FABP4.

Adiponectin is an adipokine expressed exclusively in brown and white adipocytes and is secreted into the blood. It exists in three major forms: a low molecular weight trimer, a medium molecular weight hexamer and a high molecular weight multimer (3). Decreased adiponectin levels are seen in obese and insulin-resistant mice and humans (4), suggesting that this adipokine is critical for maintenance of insulin sensitivity.

Peroxisome proliferator-activated receptor γ (PPARγ) is a transcriptional activator preferentially expressed in adipocytes, vascular smooth muscle cells, and macrophages (5,6).

Acetyl-CoA carboxylase (ACC) is a key fatty acid biosynthesis and oxidation enzyme that is responsible for the carboxylation of acetyl-CoA to malonyl-CoA, (7). Phosphorylation of acetyl-CoA carboxylase by AMPK at Ser79 or by PKA at Ser1200 inhibits ACC enzymatic activity (8). ACC is a potential target of anti-obesity drugs (9,10).

CCAAT/enhancer-binding proteins (C/EBPs) transcription factors are critical for cellular differentiation, terminal function, and the inflammatory response (11). Phosphorylation of C/EBPα at Thr222, Thr226, and Ser230 by GSK-3 may be required for adipogenesis (12).

Perilipin localizes to the periphery of lipid droplets and serves as a protective coating against lipases. Evidence suggests that PKA regulates lipolysis by phosphorylating perilipin (13-17), resulting in a conformational change that exposes lipid droplets to endogenous, hormone-sensitive lipases (14). Hence, perilipin plays a pivotal role in lipid storage (14,17).

Fatty acid synthase (FASN) catalyzes the synthesis of long-chain fatty acids from acetyl-CoA and malonyl-CoA. FASN is active as a homodimer with seven different catalytic activities and produces lipids in the liver for export to metabolically active tissues or storage in adipose tissue. In most other human tissues, FASN is minimally expressed since they rely on circulating fatty acids for new structural lipid synthesis (18).

  1. Tuncman, G. et al. (2006) Proc Natl Acad Sci U S A 103, 6970-5.
  2. Haunerland, N.H. and Spener, F. (2004) Prog Lipid Res 43, 328-49.
  3. Kadowaki, T. et al. (2006) J Clin Invest 116, 1784-92.
  4. Hu, E. et al. (1996) J Biol Chem 271, 10697-703.
  5. Tontonoz, P. et al. (1995) Curr Opin Genet Dev 5, 571-6.
  6. Rosen, E.D. et al. (1999) Mol Cell 4, 611-7.
  7. Castle, J.C. et al. (2009) PLoS One 4, e4369.
  8. Ha, J. et al. (1994) J Biol Chem 269, 22162-8.
  9. Abu-Elheiga, L. et al. (2001) Science 291, 2613-6.
  10. Levert, K.L. et al. (2002) J Biol Chem 277, 16347-50.
  11. Lekstrom-Himes, J. and Xanthopoulos, K.G. (1998) J Biol Chem 273, 28545-8.
  12. Ross, S.E. et al. (1999) Mol Cell Biol 19, 8433-41.
  13. Greenberg, A.S. et al. (1991) J Biol Chem 266, 11341-6.
  14. Brasaemle, D.L. (2007) J Lipid Res 48, 2547-59.
  15. Ducharme, N.A. and Bickel, P.E. (2008) Endocrinology 149, 942-9.
  16. Egan, J.J. et al. (1990) J Biol Chem 265, 18769-75.
  17. Brasaemle, D.L. et al. (2009) Mol Cell Biochem 326, 15-21.
  18. Katsurada, A. et al. (1990) Eur J Biochem 190, 427-33.

Background References

    Trademarks and Patents

    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.
    All other trademarks are the property of their respective owners. Visit cellsignal.com/trademarks for more information.

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