SAB4200389
Anti-acetyl-Histone H3 [Ac-Lys23] antibody produced in rabbit
IgG fraction of antiserum, antigen mol wt ~15 kDa
Synonym(s):
Anti-H3.4, Anti-H3/g, Anti-H3FT, Anti-H3K23ac, Anti-H3t, Anti-HIST3H3, Anti-Hist1h2ai, Anti-Hist1h2ail, Anti-Hist1h3a, Anti-Hist1h3g, Anti-Hist1h3h, Anti-Hist1h3i
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About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IF, IHC, WB
Citations:
6
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~15 kDa
species reactivity
mouse, human, rat
technique(s)
immunohistochemistry: 1:100-1:200 using formalin-fixed paraffin-embedded human breast carcinoma., indirect immunofluorescence: 1:200-1:400 using HeLa cells., western blot: 1:2500-1:5000 using lysates of sodium butyrate treated NIH3T3 cells.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
acetylation (Lys23)
Gene Information
human ... HIST3H3(8290)
General description
Histone H3 is a component of the histone octamer of the nucleosome DNA complex. It possesses a lysine-rich N-terminal tail region. Histone H3 gene is mapped to human chromosome 1q42.13.
Immunogen
synthetic acetylated peptide containing acetylated Lys23 of human histone H3, conjugated to KLH. The corresponding sequence is identical in many species including rat and mouse histone H3.
Application
Anti-acetyl-Histone H3 [Ac-Lys23] antibody produced in rabbit may be used in:
- immunoblotting
- immunofluorescence
- immunohistochemistry
Biochem/physiol Actions
Anti-Acetyl-Histone H3 [Ac-Lys23] specifically recognizes human and mouse [Ac-Lys23] Histone H3.
Histones H3 and H4 are the predominant histones subjected to extensive covalent modifications. Active chromatin is also correlated with the hyperacetylation of histone tail. Histone H3 can be reversibly acetylated at Lys residues 9, 14, 18, 23, 27, 36 and 56. Histone H3 is acetylated at Lys18 by E1A binding protein p300/CREB-binding protein (CBP/p300) following estrogen stimulation, leading to acetylation of Lys23, and methylation of Arg17 by coactivator associated arginine methyltransferase 1 (CARM1). These events lead to transcriptional activation of the estrogen-responsive genes. Renal failure has been shown to increase cardiac histone H3 acetylation of Lys23 and Lys9, dimethylation of Lys4. Phosphorylation of Ser10 along with lysine dimethylation is reported to induce cardiomyopathy-related genes in a mice model of type 2 diabetes.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Preparation Note
For continuous use, store at 2-8 °C for upto one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers,is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Related Content
Instructions
Anil Bhanudas Gaikwad et al.
The American journal of pathology, 176(3), 1079-1083 (2010-01-16)
The combination of diabetes and renal failure is associated with accelerated cardiomyopathy, but the molecular mechanisms of how renal failure drives diabetic heart disease remain elusive. We speculated that the metabolic abnormalities of renal failure will affect the epigenetic control
Heather J Szerlong et al.
The Journal of biological chemistry, 285(42), 31954-31964 (2010-08-20)
Condensation of chromatin into higher order structures is mediated by intra- and interfiber nucleosome-nucleosome interactions. Our goals in this study were to determine the impact specific activator-dependent histone acetylation had on chromatin condensation and to ascertain whether acetylation-induced changes in
Sylvain Daujat et al.
Current biology : CB, 12(24), 2090-2097 (2002-12-25)
Dynamic changes in the modification pattern of histones, such as acetylation, phosphorylation, methylation, and ubiquitination, are thought to provide a code for the correct regulation of gene expression mostly by affecting chromatin structure and interactions of non-histone regulatory factors with
Global Trade Item Number
| SKU | GTIN |
|---|---|
| SAB4200389-200UL | 04061838036148 |