Render Target: STATIC
Render Timestamp: 2024-11-06T10:21:39.728Z
Commit: 642d75590e907c0f7dfc7c6e3b846bcc0b02197c
XML generation date: 2024-09-18 13:54:15.048
Product last modified at: 2024-09-26T14:15:12.674Z
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PDP - Template Name: InTraSeq Conjugate
PDP - Template ID: *******e148868
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Acetyl-Histone H3 (Lys27) (D5E4) XP® Rabbit mAb (InTraSeq 3' Conjugate 3020) #27234

Filter:
  • SCA

    Supporting Data

    REACTIVITY H M
    SENSITIVITY Endogenous
    MW (kDa)
    Source/Isotype Rabbit IgG
    Application Key:
    • SCA-Single Cell Analysis 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 

    Product Information

    Storage

    Supplied in PBS (pH 7.2), 2 mM EDTA, 0.05% Triton X-100, 2 mg/mL BSA, and 50% glycerol. Store at -20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Acetyl-Histone H3 (Lys27) (D5E4) XP® Rabbit mAb (InTraSeq™ 3' Conjugate 3020) recognizes endogenous levels of histone H3 protein only when acetylated at Lys27. This antibody does not cross-react with histone H3 acetylated at Lys9, 14, 18, 23, or 56. This antibody shows some cross-reactivity with acetyl-histone H2B lysine 5.

    Species Reactivity:

    Human, Mouse

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Hamster, Xenopus, Zebrafish, Horse, Guinea Pig, Rabbit

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding acetylated Lys27 of human histone H3 protein.

    Background

    The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1,2). Histone acetylation occurs mainly on the amino-terminal tail domains of histones H2A (Lys5), H2B (Lys5, 12, 15, and 20), H3 (Lys9, 14, 18, 23, 27, 36, and 56), and H4 (Lys5, 8, 12, and 16) and is important for the regulation of histone deposition, transcriptional activation, DNA replication, recombination, and DNA repair (1-3). Hyper-acetylation of the histone tails neutralizes the positive charge of these domains and is believed to weaken histone-DNA and nucleosome-nucleosome interactions, thereby destabilizing chromatin structure and increasing the accessibility of DNA to various DNA-binding proteins (4,5). In addition, acetylation of specific lysine residues creates docking sites for a protein module called the bromodomain, which binds to acetylated lysine residues (6). Many transcription and chromatin regulatory proteins contain bromodomains and may be recruited to gene promoters, in part, through binding of acetylated histone tails. Histone acetylation is mediated by histone acetyltransferases (HATs), such as CBP/p300, GCN5L2, PCAF, and Tip60, which are recruited to genes by DNA-bound protein factors to facilitate transcriptional activation (3). Deacetylation, which is mediated by histone deacetylases (HDAC and sirtuin proteins), reverses the effects of acetylation and generally facilitates transcriptional repression (7,8).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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    InTraSeq is a trademark of Cell Signaling Technology, Inc.
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