Product Pathways - Metabolism
Adipogenesis Marker Antibody Sampler Kit #12589
|12589S||1 Kit (7 x 40 µl)||---||In Stock||---|
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|Kit Includes||Quantity||Applications||Reactivity||Homology†||MW (kDa)||Isotype|
|Acetyl-CoA Carboxylase (C83B10) Rabbit mAb #3676||40 µl||W, IHC-P, IF-IC, F||H, M, R, Hm||280||Rabbit IgG|
|Adiponectin (C45B10) Rabbit mAb #2789||40 µl||W||M, R||H||27||Rabbit IgG|
|C/EBPα Antibody #2295||40 µl||W, IF-IC||H, M, R||42, 28||Rabbit|
|FABP4 (D25B3) XP® Rabbit mAb #3544||40 µl||W, IF-IC||M||H||15||Rabbit IgG|
|Fatty Acid Synthase (C20G5) Rabbit mAb #3180||40 µl||W, IP, IHC-P, IHC-F, IF-IC||H, M, R||B||273||Rabbit IgG|
|Perilipin (D1D8) XP® Rabbit mAb #9349||40 µl||W, IP, IHC-P, IF-F, IF-IC||H, M||62||Rabbit IgG|
|PPARγ (C26H12) Rabbit mAb #2435||40 µl||W, IHC-P, IF-IC||H, M||R||53, 57||Rabbit IgG|
|Anti-rabbit IgG, HRP-linked Antibody #7074||100 µl||Goat|
†Species predicted to react based on 100% sequence homology.
Applications Key: W=Western Blotting, IHC-P=Immunohistochemistry (Paraffin), IF-IC=Immunofluorescence (Immunocytochemistry), F=Flow Cytometry, IP=Immunoprecipitation, IHC-F=Immunohistochemistry (Frozen), IF-F=Immunofluorescence (Frozen)
Reactivity Key: H=Human, M=Mouse, R=Rat, Hm=Hamster
Western blot analysis of extracts from THP-1 and 3T3-L1 cells using C/EBPα Antibody #2295.
Western blot analysis of extracts from NIH/3T3 and 3T3-L1 cells (differentiated 6 days) using PPARγ (C26H12) Rabbit mAb #2435.
Western blot analysis of extracts from NIH/3T3 and 3T3-L1 cells using Adiponectin (C45B10) Rabbit mAb #2789.
Western blot analysis of extracts from 293, HeLa, and NIH/3T3 cells using Fatty Acid Synthase (C20G5) Rabbit mAb #3180.
Western blot analysis of extracts from NIH/3T3 and differentiated 3T3-L1 cells using FABP4 (D25B3) XP® Rabbit mAb #3544.
Western blot analysis of extracts from various cell lines using Acetyl-CoA Carboxylase (C83B10) Rabbit mAb #3676.
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 four western blot experiments with each primary antibody.
Specificity / Sensitivity
Each antibody recognizes endogenous total levels of its specific target protein. The Adiponectin (C45B10) Rabbit mAb detects endogenous levels of total adiponectin protein monomer. It will not detect higher molecular weight forms of adiponectin. The Acetyl-CoA Carboxylase (C83B10) Rabbit mAb detects endogenous levels of all isoforms of acetyl-CoA carboxylase protein.
Source / Purification
Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser523 of human acetyl-CoA carboxylase α1, to human adiponectin, to the sequence of human FABP4, to residues surrounding Gly46 of human fatty acid synthase, to residues surrounding Ile419 of human perilipin protein, or to residues surrounding Asp69 of human PPARγ. Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the sequence of human C/EBPα. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
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).
- Tuncman, G. et al. (2006) Proc Natl Acad Sci U S A 103, 6970-5.
- Haunerland, N.H. and Spener, F. (2004) Prog Lipid Res 43, 328-49.
- Kadowaki, T. et al. (2006) J Clin Invest 116, 1784-92.
- Hu, E. et al. (1996) J Biol Chem 271, 10697-703.
- Tontonoz, P. et al. (1995) Curr Opin Genet Dev 5, 571-6.
- Rosen, E.D. et al. (1999) Mol Cell 4, 611-7.
- Castle, J.C. et al. (2009) PLoS One 4, e4369.
- Ha, J. et al. (1994) J Biol Chem 269, 22162-8.
- Abu-Elheiga, L. et al. (2001) Science 291, 2613-6.
- Levert, K.L. et al. (2002) J Biol Chem 277, 16347-50.
- Lekstrom-Himes, J. and Xanthopoulos, K.G. (1998) J Biol Chem 273, 28545-8.
- Ross, S.E. et al. (1999) Mol Cell Biol 19, 8433-41.
- Greenberg, A.S. et al. (1991) J Biol Chem 266, 11341-6.
- Brasaemle, D.L. (2007) J Lipid Res 48, 2547-59.
- Ducharme, N.A. and Bickel, P.E. (2008) Endocrinology 149, 942-9.
- Egan, J.J. et al. (1990) J Biol Chem 265, 18769-75.
- Brasaemle, D.L. et al. (2009) Mol Cell Biochem 326, 15-21.
- Katsurada, A. et al. (1990) Eur J Biochem 190, 427-33.
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