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12-359 Sigma-AldrichAcetyl-Histone H3 (Lys14) Peptide

Routinely evaluated by Dot Blot Assay. This peptide was recognized on a dot blot using Anti-acetyl Histone H3 (Lys14). The peptide was not recognized by anti-acetyl Histone H3 (Lys9) or anti-acetyl Histone H3 (Lys9,14).

Acetyl-Histone H3 (Lys14) Peptide MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

CoA
References

Key Applications: Immunoprecipitation, Western Blotting, Immunocytochemistry UniProt Number: Q16695 Entrez Gene Number: NM_002107.3

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12-359

100 µg

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Key Specifications Table

Key Applications	Entrez Gene Number	Modifications	Uni Prot Number
IP, WB, ICC	NM_002107.3	Acetylation	Q16695

Description
Catalogue Number	12-359
Brand Family	Upstate
Trade Name	Upstate
Description	Acetyl-Histone H3 (Lys14) Peptide

References

Product Information
Presentation	Lyophilized powder
Quality Level	MQ100

Applications
Application	Routinely evaluated by Dot Blot Assay. This peptide was recognized on a dot blot using Anti-acetyl Histone H3 (Lys14). The peptide was not recognized by anti-acetyl Histone H3 (Lys9) or anti-acetyl Histone H3 (Lys9,14).
Key Applications	Immunoprecipitation Western Blotting Immunocytochemistry

Biological Information
Entrez Gene Number	NM_002107.3
Entrez Gene Summary	Histones 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	Q16695
UniProt Summary	FUNCTION: 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 Assurance	Routinely evaluated by Dot Blot Assay. This peptide was recognized on a dot blot using Anti-acetyl Histone H3 (Lys14), (06-911). The peptide was not recognized by anti-acetyl Histone H3 (Lys9) or anti-acetyl Histone H3 (Lys9,14).
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 Conditions	2 years at -20°C

Packaging Information
Material Size	100 µg

Transport Information

Supplemental Information

Specifications

Global Trade Item Number
Catalog Number	GTIN
12-359	04053252272073

Documentation

Acetyl-Histone H3 (Lys14) Peptide Certificates of Analysis

Title	Lot Number
Acetyl-Histone H3 (Lys14) Peptide	2450120
Acetyl-Histone H3 (Lys14) Peptide - 0610042375	0610042375
Acetyl-Histone H3 (Lys14) Peptide - 0701049657	0701049657
Acetyl-Histone H3 (Lys14) Peptide - 0703056145	0703056145
Acetyl-Histone H3 (Lys14) Peptide - 18987	18987
Acetyl-Histone H3 (Lys14) Peptide - 23361	23361
Acetyl-Histone H3 (Lys14) Peptide - 31516	31516
Acetyl-Histone H3 (Lys14) Peptide - 3323137	3323137
Acetyl-Histone H3 (Lys14) Peptide - 4133798	4133798
Acetyl-Histone H3 (Lys14) Peptide -2585686	2585686

References

Reference overview	Pub Med ID
Opening the way to gene activity Pennisi, E Science, 275:155-7 (1997) 1997	8999545
Gcn5p is involved in the acetylation of histone H3 in nucleosomes Ruiz-García, A B, et al FEBS Lett, 403:186-90 (1997) 1997	9042963
Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines. Kuo, M H, et al. Nature, 383: 269-72 (1996) 1996 Show Abstract The yeast transcriptional adaptor, Gcn5p, is a catalytic subunit of a nuclear (type A) histone acetyltransferase linking histone acetylation to gene activation. Here we report that Gcn5p acetylates histones H3 and H4 non-randomly at specific lysines in the amino-terminal domains. Lysine 14 of H3 and lysines 8 and 16 of H4 are highly preferred acetylation sites for Gcn5p. We also demonstrate that lysine 9 is the preferred position of acetylation in newly synthesized yeast H3 in vivo. This finding, along with the fact that lysines 5 and 12 in H4 are predominant acetylation sites during chromatin assembly of many organisms, indicates that Gcn5p acetylates a distinct set of lysines that do not overlap with those sites characteristically used by type B histone acetyltransferases for histone deposition and chromatin assembly.	8805705

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12-425

Acetyl-Histone H3 (Lys14) Peptide, biotin conjugate

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12-359 Sigma-AldrichAcetyl-Histone H3 (Lys14) Peptide

Routinely evaluated by Dot Blot Assay. This peptide was recognized on a dot blot using Anti-acetyl Histone H3 (Lys14). The peptide was not recognized by anti-acetyl Histone H3 (Lys9) or anti-acetyl Histone H3 (Lys9,14).

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