Cargando…
OX133, a monoclonal antibody recognizing protein-bound N-ethylmaleimide for the identification of reduced disulfide bonds in proteins
In vivo, enzymatic reduction of some protein disulfide bonds, allosteric disulfide bonds, provides an important level of structural and functional regulation. The free cysteine residues generated can be labeled by maleimide reagents, including biotin derivatives, allowing the reduced protein to be d...
Autores principales: | Holbrook, Lisa-Marie, Kwong, Lai-Shan, Metcalfe, Clive L., Fenouillet, Emmanuel, Jones, Ian M., Barclay, A. Neil |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5037987/ https://www.ncbi.nlm.nih.gov/pubmed/26986548 http://dx.doi.org/10.1080/19420862.2016.1152443 |
Ejemplares similares
-
Role of Disulfide Bonds and Sulfhydryl Blocked by N-Ethylmaleimide on the Properties of Different Protein-Stabilized Emulsions
por: Wu, Mangang, et al.
Publicado: (2021) -
Labile disulfide bonds are common at the leucocyte cell surface
por: Metcalfe, Clive, et al.
Publicado: (2011) -
Effect of N-Ethylmaleimide as a Blocker of Disulfide Crosslinks Formation on the Alkali-Cold Gelation of Whey Proteins
por: Lei, Zhao, et al.
Publicado: (2016) -
Interleukin-2 signalling is modulated by a labile disulfide bond in
the CD132 chain of its receptor
por: Metcalfe, Clive, et al.
Publicado: (2012) -
The impact of thioredoxin reduction of allosteric disulfide bonds on the therapeutic potential of monoclonal antibodies
por: Gurjar, Shalom A., et al.
Publicado: (2019)