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  3. HDAC4 (4A3) Mouse Monoclonal Antibody (BSA and Azide Free)

HDAC4 (4A3) Mouse Monoclonal Antibody (BSA and Azide Free) #42718

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  • WB
  • ELISA+

    Product Specifications

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 140
    Source/Isotype Mouse IgG2a
    Application Key:
    • WB-Western Blotting 
    • ELISA+-ELISA and/or ELISA-like Assays 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    This product is the carrier free version of product #5392. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.

    This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.

    BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.

    Formulation

    Supplied in 1X PBS (10 mM Na2HPO4, 3 mM KCl, 2 mM KH2PO4, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.

    For standard formulation of this product see product #5392

    Storage

    Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.

    Specificity / Sensitivity

    HDAC4 (4A3) Mouse Monoclonal Antibody (BSA and Azide Free) detects endogenous levels of total HDAC4 protein. This antibody may cross-react with HDAC5.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a recombinant protein corresponding to the amino terminus of human HDAC4 protein. The epitope corresponds to a region surrounding Gln115 of human HDAC4.

    Background

    Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).
    Histone deacetylases (HDACs) interact with an increasing number of transcription factors, including myocyte enhancer factor 2 (MEF2), to negatively regulate gene expression. HDACs are regulated in part by shuttling between the nucleus and cytoplasm, where export to the cytoplasm facilitates gene activation by removing HDACs from their target genes (8,9). The cytoplasmic export is facilitated by 14-3-3 proteins, which bind to specific phosphoserine residues on the HDAC proteins (8,9). These phosphoserine 14-3-3 binding modules are highly conserved between HDAC proteins, allowing for their collective regulation in response to specific cell stimuli. For example, the highly conserved HDAC4 Ser246, HDAC5 Ser259 and HDAC7 Ser155 residues are all phosphorylated by CAMK and PKD kinases in response to multiple cell stimuli, including VEGF-induced angiogenesis in endothelial cells, B cell and T cell activation, and differentiation of myoblasts into muscle fiber (10-14).
    1. Marmorstein, R. (2001) Cell Mol Life Sci 58, 693-703.
    2. Gregory, P.D. et al. (2001) Exp Cell Res 265, 195-202.
    3. Liu, Y. et al. (2000) Mol Cell Biol 20, 5540-53.
    4. Cress, W.D. and Seto, E. (2000) J Cell Physiol 184, 1-16.
    5. Gray, S.G. and Ekström, T.J. (2001) Exp Cell Res 262, 75-83.
    6. Thiagalingam, S. et al. (2003) Ann. N.Y. Acad. Sci. 983, 84-100.
    7. Vigushin, D.M. and Coombes, R.C. (2004) Curr Cancer Drug Targets 4, 205-18.
    8. Grozinger, C.M. and Schreiber, S.L. (2000) Proc Natl Acad Sci USA 97, 7835-40.
    9. Wang, A.H. et al. (2000) Mol Cell Biol 20, 6904-12.
    10. Ha, C.H. et al. (2008) J Biol Chem 283, 14590-9.
    11. Wang, S. et al. (2008) Proc Natl Acad Sci USA 105, 7738-43.
    12. Matthews, S.A. et al. (2006) Mol Cell Biol 26, 1569-77.
    13. Parra, M. et al. (2005) J Biol Chem 280, 13762-70.
    14. McKinsey, T.A. et al. (2000) Nature 408, 106-11.

    Alternate Names

    AHO3; BDMR; HA6116; HD4; HDAC-4; HDAC-A; HDAC4; HDACA; Histone deacetylase 4; histone deacetylase A; KIAA0288

    Database Links

    UniProt ID: P56524


    Entrez-Gene Id: 9759


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    For Research Use Only. Not for Use in Diagnostic Procedures.
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