Me2-H4(K20) Antibody Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P62805 |
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Clone Names | 80928002 |
Gene ID | 121504;554313;8294;8359;8360;8361;8362;8363;8364;8365;8366;8367;8368;8370 |
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Other Names | Histone H4, HIST1H4A, H4/A, H4FA |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP3674a was selected from the Methyl region of human hH4-K20 (Methyl 2). A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | H4C1 |
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Synonyms | H4/A, H4FA, HIST1H4A |
Function | 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. |
Cellular Location | Nucleus. Chromosome. |
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
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