Anti-Succinyllysine Rabbit pAb

Primary Antibodies

Ambient temperature

Multiple

Post-Translational Modificaiton

Succinylation is a post-translational modification that involves the addition of a succinyl group (-CO-CH2-CH2-CO2 h) is added to a lysine residue of a protein molecule. This modification is found in many proteins, including histones. Although the precise implications of succinylation are under investigation, due to its impact on lysine's charge, transitioning it from +1 to -1 (under physiological pH conditions), and because succinylation introduces a relatively substantial structural moiety with a mass of 100 Da, which is notably larger than the moieties introduced by acetylation (42 Da) or methylation (14 Da), succinylation is anticipated to induce more substantial alterations in both protein structure and function. Key players in the succinylation process comprise 'writers' such as carnitine palmitoyltransferase 1A (CPT1A) and lysine acetyltransferase 2A (KAT2A/GCN5), 'erasers' like sirtuin 5 (SIRT5) and sirtuin 7 (SIRT7), and the pH-dependent reader, the YEATS domain of glioma-amplified sequence 41 (GAS41).

Anti-Succinyllysine Rabbit pAb detects proteins post-translationally modified by succinylation on lysine residues. This pan antibody recognizes succinylated lysine independent of its surrounding sequences.

Succinyl

Succinylated lysine peptides

Succinylation is a post-translational modification that involves the addition of a succinyl group (-CO-CH2-CH2-CO2 h) is added to a lysine residue of a protein molecule. This modification is found in many proteins, including histones. Although the precise implications of succinylation are under investigation, due to its impact on lysine's charge, transitioning it from +1 to -1 (under physiological pH conditions), and because succinylation introduces a relatively substantial structural moiety with a mass of 100 Da, which is notably larger than the moieties introduced by acetylation (42 Da) or methylation (14 Da), succinylation is anticipated to induce more substantial alterations in both protein structure and function. Key players in the succinylation process comprise 'writers' such as carnitine palmitoyltransferase 1A (CPT1A) and lysine acetyltransferase 2A (KAT2A/GCN5), 'erasers' like sirtuin 5 (SIRT5) and sirtuin 7 (SIRT7), and the pH-dependent reader, the YEATS domain of glioma-amplified sequence 41 (GAS41).