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Render Timestamp: 2024-11-01T10:41:08.118Z
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XML generation date: 2024-10-16 17:30:13.818
Product last modified at: 2024-08-09T13:45:12.579Z
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PDP - Template Name: Antibody Sampler Kit
PDP - Template ID: *******4a3ef3a

PPARγ Regulated Fatty Acid Metabolism Antibody Sampler Kit #8660

    Product Information

    Product Description

    PPARγ Regulated Fatty Acid Metabolism Antibody Sampler Kit provides an economical means to evaluate PPARγ and related proteins involved in lipid metabolism. This kit contains enough primary antibody to perform two western blots per primary.

    Specificity / Sensitivity

    Phospho-AMPKα (Thr172) (40H9) Rabbit mAb detects endogenous AMPKα only when phosphorylated at Thr172. Phospho-AMPKα (Thr172) (40H9) Rabbit mAb detects both α1 and α2 isoforms of the catalytic subunit, but does not detect the regulatory β or γ subunits. AMPKα (D5A2) Rabbit mAb, CBP (D6C5) Rabbit mAb, GCN5L2 (C26A10) Rabbit mAb, PPARγ (C26H12) Rabbit mAb, SirT1 (C14H4) Rabbit mAb, and RXRα (D6H10) Rabbit mAb all detect endogenous levels of their respective total proteins.

    Source / Purification

    Monoclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr172 of human AMPKα protein or with a synthetic peptide corresponding to the respective sequences of human AMPKα, CBP, GCN5L2, PPARγ, SirT1 and RXRα protein.

    Background

    AMPK is a heterotrimeric complex composed of a catalytic α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 2, 3) (1). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia (1). The tumor suppressor LKB1 phosphorylates AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (2-4). Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS (5).
    CBP (CREB-binding protein) is a transcriptional co-activator that associates with PPARγ (6,7). CBP also contains histone acetyltransferase (HAT) activity, allowing it to acetylate histones and other proteins (7).
    General Control of Amino Acid Synthesis Yeast Homolog Like 2 (GCN5L2) is a transcription adaptor protein and a histone acetyltransferase (HAT) that functions as the catalytic subunit of the STAGA and TFTC transcription coactivator complexes (8). GCN5L2 is 73% homologous to the p300/CBP-associated factor PCAF, another HAT protein found in similar complexes (9). GCN5L2 acetylates non-histone proteins such as the transcription co-activator PGC1-α (10).
    Peroxisome proliferator-activated receptor γ (PPARγ) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator (11). PPARγ is preferentially expressed in adipocytes as well as in vascular smooth muscle cells and macrophage (12).
    The Silent Information Regulator (SIR2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as class III histone deacetylases (13). SirT1, the mammalian ortholog of Sir2, is a nuclear protein implicated in the regulation of many cellular processes, including apoptosis, cellular senescence, endocrine signaling, glucose homeostasis, aging, and longevity. Targets of SirT1 include PPARγ (14), and the PPARγ coactivator-1α (PGC-1α) protein (15). Deacetylation of PPARγ and PGC-1α regulates the gluconeogenic/glycolytic pathways in the liver and fat mobilization in white adipocytes in response to fasting (14,15).
    The human retinoid X receptors (RXRs) are type-II nuclear hormone receptors encoded by three distinct genes (RXRα, RXRβ, and RXRγ) and bind selectively and with high affinity to the vitamin A derivative, 9-cis-retinoic acid. Nuclear RXRs form heterodimers with PPAR to help regulate transcription during lipid metabolism (16).
    1. Carling, D. (2004) Trends Biochem Sci 29, 18-24.
    2. Hawley, S.A. et al. (1996) J Biol Chem 271, 27879-87.
    3. Lizcano, J.M. et al. (2004) EMBO J 23, 833-43.
    4. Shaw, R.J. et al. (2004) Proc Natl Acad Sci U S A 101, 3329-35.
    5. Hardie, D.G. (2004) J Cell Sci 117, 5479-87.
    6. Goodman, R.H. and Smolik, S. (2000) Genes Dev 14, 1553-77.
    7. Chan, H.M. and La Thangue, N.B. (2001) J Cell Sci 114, 2363-73.
    8. Candau, R. et al. (1996) Mol Cell Biol 16, 593-602.
    9. Yang, X.J. et al. (1996) Nature 382, 319-24.
    10. Lerin, C. et al. (2006) Cell Metab 3, 429-38.
    11. Tontonoz, P. et al. (1995) Curr Opin Genet Dev 5, 571-6.
    12. Rosen, E.D. et al. (1999) Mol Cell 4, 611-7.
    13. Guarente, L. (1999) Nat Genet 23, 281-5.
    14. Picard, F. et al. (2004) Nature 429, 771-6.
    15. Rodgers, J.T. et al. (2005) Nature 434, 113-8.
    16. Gronemeyer, H. et al. (2004) Nat Rev Drug Discov 3, 950-64.
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    U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.
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