Histone H2B (a.a. 33-47) Blocking Peptide
€155.00
In stock
SKU
ECM-HX4315
Background:
The nucleosome is a protein complex consisting of four core histones (H2A, H2B, H3, and H4). Two molecules of each histone forms an octamer that makes up the nucleosome. DNA wraps around repeating nucleosome units to generate chromatin structures. The structure of chromatin determines the accessiblity to transcription factors. Post-translational modification of the amino-terminal tail of histones in nucleosomes alters chromatin structure to promote or inhibit transcription. Complex alterations in acetylation, methylation, ubiquination, and/or phosphorylation determine the chromatin structural changes that occur during specific phases of the cell cycle or in response to cell stimuli. One mode of regulating histone H2B activity is through phosphorylation in the amino terminal region. Important sites of phosphorylation include Ser-14, Ser-32, and Ser-36. AMPK phosphorylates Ser-36 on histone H2B during cell stress leading to increased transcription and cell survival, while ectopic expression of an unphosphorylatable histone H2B during cell stress reduces transcription of AMPK-dependent genes and lowers cell survival.
Sequence: Histone H2B synthetic peptide corresponding to amino acids 33 to 47 in human histone H2B. This sequence is well conserved in most isoforms of rat and mouse histone H2B, and has low homology to other histone family members.
Specificity: The peptide is specifically recognized by anti-Histone H2B (a.a. 33-47) antibody (HP4311) in ELISA, and has been shown to block the reactivity of HP4311 during Western blot. In addition, the peptide is recommended for use in blocking HP4311 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
The nucleosome is a protein complex consisting of four core histones (H2A, H2B, H3, and H4). Two molecules of each histone forms an octamer that makes up the nucleosome. DNA wraps around repeating nucleosome units to generate chromatin structures. The structure of chromatin determines the accessiblity to transcription factors. Post-translational modification of the amino-terminal tail of histones in nucleosomes alters chromatin structure to promote or inhibit transcription. Complex alterations in acetylation, methylation, ubiquination, and/or phosphorylation determine the chromatin structural changes that occur during specific phases of the cell cycle or in response to cell stimuli. One mode of regulating histone H2B activity is through phosphorylation in the amino terminal region. Important sites of phosphorylation include Ser-14, Ser-32, and Ser-36. AMPK phosphorylates Ser-36 on histone H2B during cell stress leading to increased transcription and cell survival, while ectopic expression of an unphosphorylatable histone H2B during cell stress reduces transcription of AMPK-dependent genes and lowers cell survival.
Sequence: Histone H2B synthetic peptide corresponding to amino acids 33 to 47 in human histone H2B. This sequence is well conserved in most isoforms of rat and mouse histone H2B, and has low homology to other histone family members.
Specificity: The peptide is specifically recognized by anti-Histone H2B (a.a. 33-47) antibody (HP4311) in ELISA, and has been shown to block the reactivity of HP4311 during Western blot. In addition, the peptide is recommended for use in blocking HP4311 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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