Histone H2A Protein, Xenopus laevis

Histone H2A, an integral nucleosome component, forms the histone octamer with H2B, H3, and H4. This molecular spool, consisting of two H2A-H2B heterodimers and one H3-H4 heterotetramer, wraps around approximately 147 base pairs of DNA, organizing chromatin structure. The intricate histone-DNA association, especially with H2A, plays a vital role in regulating cellular processes like gene expression and DNA packaging. Histone H2A Protein, Xenopus laevis is the recombinant Xenopus laevis-derived Histone H2A protein, expressed by E. coli , with tag free. The total length of Histone H2A Protein, Xenopus laevis is 181 a.a., with molecular weight of ~12.3 kDa.

Histone H2A is a crucial component of the nucleosome, a fundamental structural unit in chromatin organization. The nucleosome comprises a histone octamer composed of two copies each of H2A, H2B, H3, and H4, with one H3-H4 heterotetramer and two H2A-H2B heterodimers. This octameric assembly serves as a molecular spool around which approximately 147 base pairs of DNA are intricately wound, contributing to the compact and organized structure of chromatin. The intricate association of histones, including H2A, with DNA in the nucleosome is essential for the regulation of various cellular processes, including gene expression and DNA packaging.

Xenopus laevis

E. coli

Tag Free

Q6AZJ8 (T17-L197)

494591  [NCBI]

TRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKL

Approximately 12.3 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.