Histone H3.2 protein (His tag)

N° du produit ABIN7939147

Protéine Recombinant Histone H3.2 exprimée dans Escherichia coli (E. coli).

Aperçu rapide pour Histone H3.2 protein (His tag) (ABIN7939147)

Antigène: Histone H3.2

Type de proteíne: Recombinant

Origine: Humain

Source: Escherichia coli (E. coli)

Application: Activity Assay (AcA), Functional Studies (Func), Screening Assay (ScA)

Détail du produit

Purification/Conjugué: His tag

Fonction: Recombinant Histone H3.2

Attributs du produit: Histone H3 is one of the core components of the nucleosome. The nucleosome is the smallest subunit of chromatin and consists of 146 base pairs of DNA wrapped around an octamer of core histone proteins (two each of H2A, H2B, H3 and H4). Histone H1 is a linker protein, present at the interface between the nucleosome core and DNA entry/exit points. Nuclear core histone H3 exist as several variants: H3.1, H3.2, H3.3, CENP-A and H3t. These variants have been suggested to have specific functions in the regulation of gene expression and genome stability. In mammals, histone H3 non-centromeric variants, H3.1, H3.2 and H3.3, differ in their chromatin deposition patterns and PTMs despite having a high degree of sequence similarity. H3.1 and H3.2, which are enriched in repressive chromatin marks, are predominantly expressed during S-Phase and deposited in DNA synthesis-coupled fashion during DNA replication and repair. In contrast, H3.3 is enriched in active chromatin marks and is expressed throughout the cell cycle. Canonical histone H3.2 is expressed during S phase and differs by only one amino acid residue from the variant histone H3.1, and four amino acid residues from histone H3.3. According to some researches, H3.1 is preferentially acetylated and dimethylated on lysines 14 and 9, respectively, while H3.2 is preferentially subjected to trimethylation on lysine 27.

Information d'application

Indications d'application: Optimal working dilution should be determined by the investigator.

Restrictions: For Research Use only

Stockage

Format: Liquid

Buffer: Recombinant Histone H3.2 is supplied in 25 mM Tris-HCl pH 7.4, 150 mM NaCl, and 5 % glycerol.

Conseil sur la manipulation: Avoid repeated freeze/thaw cycles,keep on ice when not in storage

Stock: -80 °C

Stockage commentaire: Recombinant proteins in solution are temperature sensitive and must be stored at -80°C to prevent degradation. Avoid repeated freeze/thaw cycles and keep on ice when not in storage.

Détail du antigène

Antigène: Histone H3.2

Sujet:

Protein Background: Histone H3 is one of the core components of the nucleosome. The nucleosome is the smallest subunit of chromatin and consists of 146 base pairs of DNA wrapped around an octamer of core histone proteins (two each of H2A, H2B, H3 and H4). Histone H1 is a linker protein, present at the interface between the nucleosome core and DNA entry/exit points. Nuclear core histone H3 exist as several variants: H3.1, H3.2, H3.3, CENP-A and H3t. These variants have been suggested to have specific functions in the regulation of gene expression and genome stability. In mammals, histone H3 non-centromeric variants, H3.1, H3.2 and H3.3, differ in their chromatin deposition patterns and PTMs despite having a high degree of sequence similarity. H3.1 and H3.2, which are enriched in repressive chromatin marks, are predominantly expressed during S-Phase and deposited in DNA synthesis-coupled fashion during DNA replication and repair. In contrast, H3.3 is enriched in active chromatin marks and is expressed throughout the cell cycle. Canonical histone H3.2 is expressed during S phase and differs by only one amino acid residue from the variant histone H3.1, and four amino acid residues from histone H3.3. According to some researches, H3.1 is preferentially acetylated and dimethylated on lysines 14 and 9, respectively, while H3.2 is preferentially subjected to trimethylation on lysine 27.

Short Description: Recombinant Histone H3.2 was expressed in E. coli cells as full length protein (accession number NP_066403.2) and has an observed molecular weight of 15.4 kDa.