Recombinant Human Histone H2A type 2-C (H2AC20)

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Abbreviation

HIST2H2AC

Purity

>85% (SDS-PAGE)

Target Names

HIST2H2AC

Uniprot NO.

Q16777

Alternative Names

HIST2H2AC; H2AFQ; Histone H2A type 2-C; Histone H2A-GL101; Histone H2A/q

Species

Homo sapiens (Human)

Source

Yeast

Expression Region

2-129

Target Protein Sequence

SGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YMAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK TESHKAKSK
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Buffer

Lyophilized from Tris/PBS-based buffer, 6% Trehalose, pH 8

Storage

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

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.

Gene References into Functions

we found an excess of mutations in genes encoding histone H2A and H2B, as well as significant amplification of the segment of chromosome 6p harboring the histone gene cluster containing these genes.We also found frequent deletions of the genes TP53 and MBD3 (a member with CHD4 of the nucleosome remodeling deacetylase complex). PMID:27791010
Glycated-H2A histone is better bound by serum anti-DNA autoantibodies in systemic lupus erythematosus patients, and could be a likely trigger for the disease. PMID:25065453
Our results provide mechanistic insight into how post-translational modification of H2A at the site of a photolesion initiates the repair process and directly affects the stability of the human genome. PMID:22334663
Aurora-B-dependent phosphorylation of condensin promotes its association with histone H2A and H2A.Z, which we identify as conserved chromatin 'receptors' of condensin PMID:21633354
L3MBTL2-specific RNAi resulted in increased expression of target genes that exhibited a significant reduction in H2A lysine 119 monoubiquitination. PMID:21596310
AT1R modify the composition of histone H2A and post-translational modifications. PMID:20838438
deiminated residues were present in H2A (1-56) and H4 (1-52) PMID:15823041
Monoubiquitinated histone H2A in native chromatin coimmunoprecipitates with the endogenous DDB1-CUL4A(DDB2) complex in response to UV irradiation. PMID:16473935
The 2 MDa GCN5 HAT-containing metazoan TFTC/STAGA complexes contain a histone H2A and H2B deubiquitinase activity. PMID:18206972
DDB1-CUL4B(DDB2) is more efficient than DDB1-CUL4A(DDB2) in monoubiquitinating histone H2A in vitro. PMID:18593899
The change in nucleosome core particle conformation induced by global histone acetylation is dependent on H2A/H2A.Z acetylation. PMID:19385636
Study demonstrated that RNF168 is endowed with ubiquitin ligase activity both in vitro and in vivo, which targets histones H2A and H2AX, but not H2B, forming K63 polyubiquitin chains. PMID:19500350
Results demonstrate the potential of C-terminal truncated H2A to contribute to the process of carcinogenesis through epigenetic mechanisms. PMID:19667409