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96-Well Plate
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48-602MAG
Buffer Detection Kit for Magnetic Beads
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Anti-phospho-Histone H2A/H4 (Ser1) Antibody is a Rabbit Polyclonal Antibody for detection of phospho-Histone H2A/H4 (Ser1) also known as Histone H2A/H4 ((phospho S1) & has been validated in WB.
More>>Anti-phospho-Histone H2A/H4 (Ser1) Antibody is a Rabbit Polyclonal Antibody for detection of phospho-Histone H2A/H4 (Ser1) also known as Histone H2A/H4 ((phospho S1) & has been validated in WB. Less<<
Anti-phospho-Histone H2A/H4 (Ser1) Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Antiserum containing 0.05% sodium azide before the addition of glycerol
Applications
Application
Anti-phospho-Histone H2A/H4 (Ser1) Antibody is a Rabbit Polyclonal Antibody for detection of phospho-Histone H2A/H4 (Ser1) also known as Histone H2A/H4 ((phospho S1) & has been validated in WB.
Key Applications
Western Blotting
Biological Information
Immunogen
Peptide corresponding to amino acids 1-9 of human histone H2A (pSGRGKQGGK-C)
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 is intronless and encodes a member of the histone H4 family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the large histone gene cluster on chromosome 6.
FUNCTION: SwissProt: P62805 # 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: 103 amino acids; 11367 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: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage (By similarity). & Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins. SIMILARITY: SwissProt: P62805 ## Belongs to the histone H4 family.
Molecular Weight
H2A (16kDa) and H4 (10kDa)
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Routinely evaluated by immunoblot on acid-extracted proteins from colcemid-arrested HeLa cells
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.
Phosphorylation and arginine methylation mark histone H2A prior to deposition during Xenopus laevis development. Wang, WL; Anderson, LC; Nicklay, JJ; Chen, H; Gamble, MJ; Shabanowitz, J; Hunt, DF; Shechter, D 2014
Analysis of histones in Xenopus laevis. I. A distinct index of enriched variants and modifications exists in each cell type and is remodeled during developmental transitions. Shechter, D; Nicklay, JJ; Chitta, RK; Shabanowitz, J; Hunt, DF; Allis, CD 2009
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Phosphorylation of histone H2A by protein kinase C and identification of the phosphorylation site. Takeuchi, F, et al. J. Biochem., 111: 788-92 (1992)
1992
In regenerating rat liver, nuclear protein histone H2A was shown to be phosphorylated on its amino-terminal serine residue [Sung et al. (1971) J. Biol. Chem. 246, 1358-1364], but the protein kinase which phosphorylates this residue has not been identified. To evaluate the possibility that protein kinase C can phosphorylate this residue, calf thymus histone H2A was 32P-labeled by incubation with [gamma-32P]ATP and highly purified protein kinase C from rat brain in the presence of calcium and phospholipid. About 1 mol of 32P was incorporated per mol of histone H2A and the Km and apparent Vmax of the reaction were calculated to be 2.1 microM and 0.35 mumol/min/mg, respectively. So histone H2A seemed to be a good substrate for protein kinase C. Further, the proteolytic phosphopeptides of 32P-labeled histone H2A were isolated by means of a series of column chromatographies and analyzed for their amino acid compositions. Comparison of the data with the known primary structure of histone H2A revealed their amino acid sequence as 1Ser-Gly-Arg. These data suggest that protein kinase C may be a candidate for the protein kinase which phosphorylates the amino-terminal serine residue of histone H2A during the regeneration of rat liver.
Millipore’s Histone H4 antibodies demonstrate specificity against linker histone H4. See below for H4 Antibodies, ChipAb+ Primer sets, and peptides, based on the expertise of Upstate & Chemicon. Weitere Informationen >>
