Anti-glutaryllysine rabbit polyclonal antibody
Rabbit polyclonal Anti-glutaryllysine antibody
Anti-glutaryllysine antibody detects proteins post-translationally modified by lysine glutarylation. The antibody recognizes glutaryllysine in a wide range of sequence contexts, both in histones and non-histone substrates, but not the structurally similar malonyllysine and succinyllysine.
The pan polyclonal anti-glutaryllysine antibody is produced by immunizing rabbits with glutarylated BSA. Antibodies are purified by glutaryl-lysine agarose affinity chromatography. The product specifically recognizes proteins with lysine glutarylated residues but not the structurally-similar modified lysine residues or non-modified lysine residues. Besides common applications in Western blotting, the antibody has been well utilized for proteomic screening to lysine glutarylated substrates from protease-digested proteins both in prokaryotic and eukaryotic cells.
Antibody is supplied in PBS with 50% glycerol and 0.01% sodium azide.
Store product at -20 ℃. Avoid repeated freeze/thaw cycles. Stable for 12 months from the date of receipt.
For Western blotting, incubate membrane with diluted antibody in 5% nonfat milk, 1 x TBS, 0.1% Tween-20 at room temperatue with gentle shaking two hours.
Use at an assay dependent concentration. Optimal dilutions/concentrations should be determined by the end user.
A. Dot blotting analysis on glutarylated peptide library (Lane 1), succinylated peptide library (Lane 2), malonylated peptide library (Lane 3), acetylated peptide library (Lane 4) and unmodified peptide library using anti-glutaryllysine rabbit pAb. B. Western blotting analysis on 30 ug of crude proteins from human HeLa, mouse MEF, Drosophila S2, yeast S. cerevisiae and bacteria E. coli whole cell lysates using anti-glutaryllysine rabbit pAb(1:2000).
Lysine glutarylation is a newly-identified histone post-translational modification by integrated proteomic approaches and elaborate biochemistry analyses. It has been shown that lysine glutarylation is an evolutionarily conserved PTM in multiple species of both prokaryotes and eukaryotes in a wide range of proteins, both in histones and non-histone substrates. Lysine glutarylation is a SIRT5- and nutrient-regulated PTM, which impacts metabolic processes and other mitochondrial functions.
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