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 protein's N-terminus via a peptide bond. (Wiki)
Formulation
1 mg/ml in 1X PBS; BSA free, sodium azide free
Host
Mouse
Immunogen Region
A portion of amino acids 1-119 from the human protein was used as the immunogen for the Ubiquitin antibody.
Isotype
Mouse IgG1, kappa
Species Reactivity
Human
Note
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.
Uniprot
P0CG47, P0CG48, P62979, P62987, P62988
Format
Purified
Purity
Protein G affinity chromatography
Storage
Store the Ubiquitin antibody at 2-8oC (with azide) or aliquot and store at -20oC or colder (without azide).
Applications
WB, IHC-P
Description
Western blot: 1-2ug/ml,Immunohistochemistry (FFPE): 1-2ug/ml for 30 min at RT