A portion of amino acids 1-119 from the human protein was used as the immunogen for the Ubiquitin antibody.
Ubiquitin is a small (8.5 kDa) regulatory protein found in most tissues of eukaryotic organisms. The addition of ubiquitin to a substrate protein is called ubiquitination or less frequently ubiquitylation. Ubiquitination affects proteins in many ways: it can mark them for degradation via the proteasome, alter their cellular location, affect their activity, and promote or prevent protein interactions. Ubiquitination involves three main steps: activation, conjugation, and ligation, performed by ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s), respectively. The result of this sequential cascade is to bind ubiquitin to lysine residues on the protein substrate via an isopeptide bond, cysteine residues through a thioester bond, serine and threonine residues through an ester bond, or the amino group of the proteins N-terminus via a peptide bond. [Wiki]
Western blot: 1-2ug/ml,Immunohistochemistry (FFPE): 1-2ug/ml for 30 min at RT
Application Notes:
The stated application concentrations are suggested starting points. Titration of the Ubiquitin antibody may be required due to differences in protocols and secondary/substrate sensitivity.
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