Anti-Ubiquityl-Histone H2B (Lys120) Mouse mAb

Primary Antibodies

Histone H2B

Store at -20°C. Avoid freeze/thaw cycles.

Stable for 12 months from date of receipt/reconstitution.

Ubiquitin (Ub) is a highly conserved 76-amino acid protein that plays a critical role in regulating a wide range of cellular processes. Through a three-step process involving Ub-activating (E1), Ub-conjugating (E2), and Ub-ligating (E3) enzymes, ubiquitin covalently attaches to target proteins and marks them for proteasomal degradation, alters protein-protein interactions, modulates membrane protein trafficking, and controls the activity of many signal transduction pathways. Mono-ubiquitination of Histone H2B at Lys120 (H2BK120ub) serves signaling purposes and is reversible by ubiquitin-specific proteases (USPs). The enzymes responsible for H2BK120ub are Rad6 E2 proteins (HR6A and HR6B in human) and Bre1 E3 ligase (RNF20 and RNF40 in human). This modification triggers a “trans-histone” modification cascade, resulting in trimethylation of Lys4 and Lys79 in histone H3, which promotes gene activity.

Anti-Ubiquityl-Histone H2B (Lys120) Mouse mAb detects histone H2B only when it is ubiquitinated at Lys120. This antibody has been shown to selectively recognize ubiquitinated H2B peptide at Lys120, but not the acetylated, succinylated, 2-hydroxyisobutyrylated, β-Hydroxybutyrylated, or unmodified H2B peptide at Lys120.

Ubiquityl

Ubiquitinated human histone H2B (Lys120) peptide

Ubiquitin (Ub) is a highly conserved 76-amino acid protein that plays a critical role in regulating a wide range of cellular processes. Through a three-step process involving Ub-activating (E1), Ub-conjugating (E2), and Ub-ligating (E3) enzymes, ubiquitin covalently attaches to target proteins and marks them for proteasomal degradation, alters protein-protein interactions, modulates membrane protein trafficking, and controls the activity of many signal transduction pathways. Mono-ubiquitination of Histone H2B at Lys120 (H2BK120ub) serves signaling purposes and is reversible by ubiquitin-specific proteases (USPs). The enzymes responsible for H2BK120ub are Rad6 E2 proteins (HR6A and HR6B in human) and Bre1 E3 ligase (RNF20 and RNF40 in human). This modification triggers a “trans-histone” modification cascade, resulting in trimethylation of Lys4 and Lys79 in histone H3, which promotes gene activity.