You Searched For: Nepsilon-acetyl-L-lysine

Catalog Number: (10387-542)

Supplier: Bioss

Description: Modulation of the chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. The N-terminal tail of core histones undergoes different posttranslational modifications including acetylation, phosphorylation and methylation. These modifications occur in response to cell signal stimuli and have a direct effect on gene expression. In most species, the histone H2B is primarily acetylated at lysines 5, 12, 15 and 20. Histone H3 is primarily acetylated at lysines 9, 14, 18 and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms. Phosphorylation at Ser10 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis.

Catalog Number: (10387-544)

Supplier: Bioss

Description: Modulation of the chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. The N-terminal tail of core histones undergoes different posttranslational modifications including acetylation, phosphorylation and methylation. These modifications occur in response to cell signal stimuli and have a direct effect on gene expression. In most species, the histone H2B is primarily acetylated at lysines 5, 12, 15 and 20. Histone H3 is primarily acetylated at lysines 9, 14, 18 and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms. Phosphorylation at Ser10 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis.

Catalog Number: (76084-920)

Supplier: Bioss

Description: Modulation of the chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. The N-terminal tail of core histones undergoes different posttranslational modifications including acetylation, phosphorylation and methylation. These modifications occur in response to cell signal stimuli and have a direct effect on gene expression. In most species, the histone H2B is primarily acetylated at lysines 5, 12, 15 and 20. Histone H3 is primarily acetylated at lysines 9, 14, 18 and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms. Phosphorylation at Ser10 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis.

Catalog Number: (CARL600401-939)

Supplier: Rockland Immunochemical

Description: Anti-Lysine Acetylated Antibody is suitable for use in ELISA, western blotting, immunofluorescence microscopy, and immunoprecipitation assays. Although not tested, this antibody is likely functional in RIA, flow cytometry, and immunochemistry.

Catalog Number: (89160-350)

Supplier: Enzo Life Sciences

Description: Fluor de Lys®-SIRT2 is a fluorogenic peptide substrate for SIRT2 (human Sirtuin 2). Based on residues 317-320 of p53 (Gln-Pro-Lys-Lys(Ac)), a site of regulatory acetylation by the PCAF acetyltransferase (lysine 320), it was the best for SIRT2 from among a panel of substrates patterned on p53, Histone H3, and Histone H4 acetylation sites. Fluor de Lys®-SIRT2 is deacetylated by SIRT2 at a rate of more than 50-fold that of the acetylated lysine substrate, Fluor de Lys® (BML-KI104; acetylated substrates both at 25 µM, 500 µM NAD+). Must be used in conjunction with Fluor de Lys® Developer II (BML-KI176). Sufficient for 100 assays of human recombinant SIRT2 (BML-SE251; 2U/well, 100 µM substrate).

Catalog Number: (89359-234)

Supplier: Genetex

Description: Histone proteins H3, H4, H2A, and H2B function as building blocks to package eukaryotic DNA into repeating nucleosome units that are folded in higher order chromatin fibers. The nucleosome is composed of an octamer containing a H3/H4 tetramer and two H2A/H2B dimers, surrounded by approximately 146 base pairs of DNA. A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation occurs on the N-terminal tail domains of histones. Acetylation of lysine residues within these N-terminal domains by histone acetyl-transferases (HATs), including Gcn5p, P/CAF, p300/CBP, and TAFII250, is associated with transcriptional activation. This modification results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. Conversely, histone deacetylation by histone deacetylases (HDACs) is associated with transcription repression reversing the chromatin remodeling process. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms.

Catalog Number: (76084-912)

Supplier: Bioss

Description: Modulation of the chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. The N-terminal tail of core histones undergoes different posttranslational modifications including acetylation, phosphorylation and methylation. These modifications occur in response to cell signal stimuli and have a direct effect on gene expression. In most species, the histone H2B is primarily acetylated at lysines 5, 12, 15 and 20. Histone H3 is primarily acetylated at lysines 9, 14, 18 and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms. Phosphorylation at Ser10 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis.

Catalog Number: (89359-236)

Supplier: Genetex

Description: Histone proteins H3, H4, H2A, and H2B function as building blocks to package eukaryotic DNA into repeating nucleosome units that are folded in higher order chromatin fibers. The nucleosome is composed of an octamer containing a H3/H4 tetramer and two H2A/H2B dimers, surrounded by approximately 146 base pairs of DNA. A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation occurs on the N-terminal tail domains of histones. Acetylation of lysine residues within these N-terminal domains by histone acetyl-transferases (HATs), including Gcn5p, P/CAF, p300/CBP, and TAFII250, is associated with transcriptional activation. This modification results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. Conversely, histone deacetylation by histone deacetylases (HDACs) is associated with transcription repression reversing the chromatin remodeling process. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms.

Catalog Number: (76084-922)

Supplier: Bioss

Description: Modulation of the chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. The N-terminal tail of core histones undergoes different posttranslational modifications including acetylation, phosphorylation and methylation. These modifications occur in response to cell signal stimuli and have a direct effect on gene expression. In most species, the histone H2B is primarily acetylated at lysines 5, 12, 15 and 20. Histone H3 is primarily acetylated at lysines 9, 14, 18 and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms. Phosphorylation at Ser10 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis.

Catalog Number: (10781-930)

Supplier: Biosensis

Description: Lysine acetylation of histones and non-histone proteins plays an important part in many cellular processes such as chromatin and nuclear signaling, transcription, gene silencing, cell cycle progression, apoptosis, differentiation, DNA replication and repair.

Supplier: Bachem Americas

Description: Sequence: Ac-Lys(Ac)-OH

Catalog Number: (103008-178)

Supplier: Anaspec Inc

Description: This Histone 3 peptide is acetylated at lysine residue at 9th position. In a glioblastoma xenograft expressing a O6-methylguanine-DNA methyltransferase (MGMT), increased H3K9-ac was observed in correlation to histone acetylation and MGMT upregulation, thus demonstrating a mechanism driven by chromatin-mediated MGMT upregulation in potentially directing epigenetic therapies to influence the mechanisms of resistance development in glioblastomas.
Sequence:ARTKQTAR-K(Ac)-STGGKAPRKQLATKA
MW:2597 Da
% peak area by HPLC:95
Storage condition:-20° C

Catalog Number: (103009-624)

Supplier: Anaspec Inc

Description: This peptide is Histone H3 amino acid residues 1-21. It is tri-methylated at lysine 4, acetylated at lysine 9 and phosphorylated at serine 10.
Sequence:ART-K(Me3)-QTAR-K(Ac)-pS-TGGKAPRKQLA
MW:2418.7 Da
% peak area by HPLC:95
Storage condition:-20° C

Catalog Number: (103008-544)

Supplier: Anaspec Inc

Description: This peptide is histone H4 (1-21), acetylated at lysine 12. The N-terminus contains a C-terminus GG linker followed by a biotinylated lysine. The acetylation of histone H4 plays a crucial role in structural changes that amplifies the binding of transcription factors to their recognition sites within the nucleosomes. Provided at >95% peptide purity, this peptide was dissolved in distilled water at 1 mg/ml and re-lyophilized to powder form.
Sequence:Ac-SGRGKGGKGLG-K(Ac)-GGAKRHRKV-GGK(Biotin)
MW:2644.1 Da
% peak area by HPLC:95
Storage condition:-20° C

Catalog Number: (CARL600403-939)

Supplier: Rockland Immunochemical

Description: This affinity-purified antibody is suitable for use in ELISA and western blotting assays.  The antibody reacts specifically with acetylated lysine residues.

Catalog Number: (103008-864)

Supplier: Anaspec Inc

Description: This peptide is a synthetic peptide corresponding to amino acids 69 to 89 of histone H3. It is acetylated at Lys79 and biotinylated on the C-terminal Lys90. The acetylation of histone H3 at Lysine (K) 79 is observed in vivo in S. cerevisiae.
Sequence:RLVREIAQDF-K(Ac)-TDLRFQSSAV-K(biotin)
MW:2877.4 Da
% peak area by HPLC:95
Storage condition:-20° C