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Render Timestamp: 2024-11-25T11:26:51.714Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-09-30 01:59:06.808
Product last modified at: 2024-11-02T15:15:07.554Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

ACTL6B/BAF53B (E5X8C) Rabbit mAb #46787

Filter:
  • WB
  • ChIP

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 45
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • ChIP-Chromatin Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    For optimal ChIP and ChIP-seq results, use 5 μl of antibody and 10 μg of chromatin (approximately 4 x 106 cells) per IP. This antibody has been validated using SimpleChIP® Enzymatic Chromatin IP Kits.
    Application Dilution
    Western Blotting 1:1000
    Chromatin IP 1:100
    Chromatin IP-seq 1:100

    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.

    Protocol

    Specificity / Sensitivity

    ACTL6B/BAF53B (E5X8C) Rabbit mAb recognizes endogenous levels of total ACTL6B/BAF53B protein. This antibody does not cross-react with ACTL6A/BAF53A protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro75 of human ACLT6B/BAF53B protein.

    Background

    The modulation of chromatin structure is an essential component in the regulation of transcriptional activation and repression. Modifications can be made by at least two evolutionarily conserved strategies, through the disruption of histone-DNA contacts by ATP-dependent chromatin remodelers, or by histone tail modifications including methylation and acetylation. One of the four classes of ATP-dependent histone remodelers is the SWI/SNF complex, the central catalytic subunit of which is Brg1 or the highly related protein hBRM (1). This SWI/SNF complex contains varying subunits but its association with either Brg1 or hBRM remains constant (1). SWI/SNF complexes have been shown to regulate gene activation, cell growth, the cell cycle, and differentiation (1). Brg1/hBRM have been shown to regulate transcription through enhancing transcriptional activation of glucocorticoid receptors (2). Although usually associated with transcriptional activation, Brg1/hBRM have also been found in complexes associated with transcriptional repression, including HDACs, Rb, and Tif1β (3-5). Brg1/hBRM plays a vital role in the regulation of gene transcription during early mammalian embryogenesis. In addition, Brg1/hBRM also plays a role as a tumor suppressor and Brg1 is mutated in several tumor cell lines (6-8).

    ACTL6/BAF53 proteins are highly homologous, actin-related proteins found in the SWI/SNF complex (9). In addition to the canonical SWI/SNF complex, ACT6LA/BAF53A is also a member of the embryonic SWI/SNF complex, known as esBAF, which plays a role in pluripotency and development (10-12). ACTL6B/BAF53B is a member of the neural-specific SWI/SNF complex that facilitates binding to target genes and is involved in memory and synaptic plasticity (13-15). ACTL6/BAF53 has been shown to interact with c-Myc, where it functions as a cofactor and is important in the transformation process (16). Further studies have shown ACTL6/BAF53 is associated with EMT and transformation in various cancers (17,18).
    1. Trotter, K.W. and Archer, T.K. (2008) Nucl Recept Signal 6, e004.
    2. Trotter, K.W. and Archer, T.K. (2007) Mol Cell Endocrinol 265-266, 162-7.
    3. Sif, S. et al. (2001) Genes Dev 15, 603-18.
    4. Zhang, H.S. et al. (2000) Cell 101, 79-89.
    5. Underhill, C. et al. (2000) J Biol Chem 275, 40463-70.
    6. Magnani, L. and Cabot, R.A. (2009) Reproduction 137, 23-33.
    7. Medina, P.P. et al. (2008) Epigenetics 3, 64-8.
    8. Medina, P.P. et al. (2008) Hum Mutat 29, 617-22.
    9. Zhao, K. et al. (1998) Cell 95, 625-36.
    10. Ho, L. et al. (2009) Proc Natl Acad Sci U S A 106, 5181-6.
    11. Krasteva, V. et al. (2012) Blood 120, 4720-32.
    12. Bao, X. et al. (2013) Cell Stem Cell 12, 193-203.
    13. Olave, I. et al. (2002) Genes Dev 16, 2509-17.
    14. Vogel-Ciernia, A. et al. (2013) Nat Neurosci 16, 552-61.
    15. Yoo, M. et al. (2017) J Neurosci 37, 3686-3697.
    16. Park, J. et al. (2002) Mol Cell Biol 22, 1307-16.
    17. Saladi, S.V. et al. (2017) Cancer Cell 31, 35-49.
    18. Sun, W. et al. (2017) Oncol Rep 37, 2405-2417.
    For Research Use Only. Not For Use In Diagnostic Procedures.
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