Histone H2A Recombinant Rabbit mAb (一抗) - WB,IHC-P,IHC-F,IF | Bioss

bsm-63133R

重组兔单抗

Histone H2A Recombinant Rabbit mAb

组蛋白H2A重组兔单抗

H2A.1; H2A.2; H2A/a; H2AC4; H2AFA; HIST1H2AE; H2AB; HIST2H2AB; H2A/m; H2AC8; H2AFM; HIST1H2AB; H2A; H2A-GL101; H2A/q; H2AFQ; HIST2H2AC; 1190022L06; H2A1B_HUMAN; Histone H2A.2; Histone H2A/a; Histone H2A/m; H2A1_HUMAN; H2AC11; H2AC13; H2AC15; H2AC16; H2AC17; Histone H2A/ptl; H2AFP; HIST1H2AG; H2AFC; HIST1H2AI; H2AFD; HIST1H2AK; H2AFI; HIST1H2AL; H2AFN; HIST1H2AM; H2A1D_HUMAN; H2AC7; Histone H2A.3; Histone H2A/g; H2AFG; HIST1H2AD; H2A2C_HUMAN; H2AC20; H2A-clustered histone 20; Histone H2A-GL101; Histone H2A/q; H2A2A_HUMAN; H2AC18; H2AC19; H2A-clustered histone 18; H2A-clustered histone 19; Histone H2A/o; H2AFO; HIST2H2AA; HIST2H2AA3; HIST2H2AA4; H2A3_HUMAN; H2AC25; H2A-clustered histone 25; H2AW; HIST3H2A; H2A2B_HUMAN; H2AC21; H2A-clustered histone 21; H2A1C_HUMAN; H2AC6; H2A-clustered histone 6; Histone H2A/l; H2AFL; HIST1H2AC; H2A1H_HUMAN; H2AC12; H2A-clustered histone 12; Histone H2A/s; HIST1H2AH; H2A1A_HUMAN; H2AC1; H2A-clustered histone 1; Histone H2A/r; H2AFR; HIST1H2AA; H2A1J_HUMAN; H2AC14; Histone H2A/e; H2AFE; HIST1H2AJ; H2A4_MOUSE; H2A1_MOUSE; H2A clustered histone 4; H2A histone family, member M; histone 1, H2ab; histone cluster 1, H2ab; histone cluster 1 H2A family member b

Rabbit

A synthesized peptide derived from human Histone H2A: 70-100

IgG

Liquid

affinity purified by Protein A

Recombinant

2F12

14 kDa

14 kDa

10mM phosphate buffered saline(pH 7.4) with 150mM sodium chloride, 0.05% BSA, 0.02% Proclin300 and 50% glycerol.

Store at 4℃ for short term. Store at -20℃ for long term. Avoid repeated freeze/thaw cycles.

This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.

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.

H2AC4

Histone H2A type 1-B/E

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.

Nucleus. Chromosome.

Abundant expression is seen in the skeletal muscle. It is also widely expressed in other tissues.

The chromatin-associated form is phosphorylated on Thr-121 during mitosis (Probable).
Deiminated on Arg-4 in granulocytes upon calcium entry.
Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3. Monoubiquitination of Lys-120 by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Monoubiquitination and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events.
Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1.
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.

Belongs to the histone H2A family.

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.