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New Antibody Study Links Survivin To Histone H3 In Mitosis

Cell division and renewal i.e. mitosis, is in the backbone of each antibody catalog, with antibodies to proteins controlling mitoses, such as histone H3, which is widely utilized in areas like cancer research and epigenetics.

A current antibody study threw exciting new light on how histone H3 works. To know about anti ma2 antibody you can search boster bio for elisa kits, antibodies, antibody company online.

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The histone family contains 4 proteins that, collectively, form the octamer around which DNA is wrapped to form chromatin (i.e. the chromosome part within the nucleus.) The DNA and histone core collectively form the nucleosome.

Gene expression is controlled by acetylation of the histone proteins. During DNA transcription, all 4 are highly altered. But, H3 undergoes the most advanced post-translational changes, with variability in order and alteration states thought to be important to gene control

Phospho-specific immunized investigations have shown that H3 is phosphorylated and dephosphorylated in the anaphase steps of mitosis.

This is accomplished by the addition of a phosphate group in the threonine 3 website (H3T3). Currently, researchers at Rockefeller University have found a connection with Survivin, which also has a vital role in mitosis.

Survivin is part of the CPC (chromosomal passenger complex) of proteins. Past antibody studies have shown that CPC is essential to cell division, migrating to the chromatin to promote spindle microtubule assembly through the protein Aurora B.

The new study showed that H3 phosphorylation is recognized using a binding pocket at the BIR region of Survivin. This was followed by CPC raising to the chromatin, and Aurora activation.