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12-358 Acetyl-Histone H3 (Lys9) Peptide

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12-358
100 µg  
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Overview

Replacement Information

Key Specifications Table

Key ApplicationsEntrez Gene NumberModificationsUni Prot Number
WBNM_002107.3 Acetylation Q16695
Description
Catalogue Number12-358
Brand Family Upstate
Trade Name
  • Upstate
DescriptionAcetyl-Histone H3 (Lys9) Peptide
References
Product Information
PresentationLyophilized powder
Quality LevelMQ100
Applications
ApplicationRoutinely evaluated in a Dot Blot Assay by spotting on nitrocellulose & detecting by using a Anti-acetyl Histone H3 (Lys9) (06-942).
Key Applications
  • Western Blotting
Biological Information
Entrez Gene Number
Entrez Gene SummaryHistones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene contains introns and its mRNA is polyadenylated, unlike most histone genes. The protein encoded is a replication-independent member of the histone H3 family.
Gene Symbol
  • H3F3A
  • MGC87783
  • H3.3A
  • MGC87782
  • H3F3
  • H3.3B
  • H3F3B
Modifications
  • Acetylation
UniProt Number
UniProt SummaryFUNCTION: SwissProt: Q16695 # Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
SIZE: 136 amino acids; 15508 Da
SUBUNIT: The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
SUBCELLULAR LOCATION: Nucleus.
PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 impairs methylation at Arg-9. Acetylation on Lys-19 and Lys-24 favors methylation at Arg-18 (By similarity). & Citrullination at Arg-9 and/or Arg-18 by PADI4 impairs methylation and represses transcription (By similarity). & Asymmetric dimethylation at Arg-18 by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 by PRMT5 is linked to gene repression (By similarity). & Methylation at Lys-5, Lys-37 and Lys-80 are linked to gene activation. Methylation at Lys-5 facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 and Lys-28 are linked to gene repression. Methylation at Lys-10 is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 and acetylation of H3 and H4. Methylation at Lys-5 and Lys-80 require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 and Lys-28 are enriched in inactive X chromosome chromatin (By similarity). & Phosphorylated at Thr-4 by GSG2/haspin during prophase and dephosphorylated during anaphase. At centromeres, specifically phosphorylated at Thr-12 from prophase to early anaphase. Phosphorylated at Ser-11 during the whole mitosis. Phosphorylation at Ser-11, which is linked to gene activation, prevents methylation at Lys-10 but facilitates acetylation of H3 and H4. Phosphorylated at Ser-29 by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation (By similarity). & Phosphorylation at 'Ser-11' is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at 'Ser-11' is important during interphase because it enables the transcription of genes following external stimulation, like stress or growth factors. Phosphorylation at 'Ser-11' is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylation at 'Ser-11' by AURKB/Aurora-B mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. & Ubiquitinated (By similarity).
SIMILARITY: SwissProt: Q16695 ## Belongs to the histone H3 family.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality AssuranceRoutinely evaluated in a Dot Blot Assay by spotting on nitrocellulose and detecting by using a Anti-acetyl Histone H3 (Lys9) (06-942).
Usage Statement
  • 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.
Storage and Shipping Information
Storage Conditions2 years at -20°C
Packaging Information
Material Size100 µg
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalog Number GTIN
12-358 04053252477591

Documentation

Acetyl-Histone H3 (Lys9) Peptide Certificates of Analysis

TitleLot Number
Acetyl-Histone H3 (Lys9) Peptide - 18692 18692
Acetyl-Histone H3 (Lys9) Peptide - 23085 23085
Histone H3 (Ac Lys9) Peptide (residues 1-12) - 2370139 2370139
Histone H3 (Ac Lys9) Peptide - 1990172 1990172
Histone H3 (Ac Lys9) Peptide - 3494921 3494921
Histone H3 (Ac Lys9) Peptide - 4145781 4145781
Histone H3 (Ac Lys9) Peptide - 4146074 4146074
Histone H3 (Ac Lys9) Peptide -2800511 2800511

References

Reference overviewPub Med ID
West Nile virus activity--United States, September 8-14, 2004.
Morbidity and mortality weekly report
MMWR. Morbidity and mortality weekly report  53  2004

Show Abstract
15371969 15371969

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Categories

Life Science Research > Proteins and Enzymes > Substrate & Control Proteins > Control Histones