Storage Condition: 0-5°C
Shipping Condition: Ambient temperature
Protein thiol is a major redox signaling in the
cellular processes. Modification of protein thiol by oxidative stress associates with the redox state in the cells. The approach of this kit is detecting the
number of thiol residues accurately in order to study the redox state in oxidative
Fig. 1 Redox States of Thiol group(s) in Protein
Mechanism of Thiol Modification with Protein-SHifter:
Fig. 2 Maleimide group of the
Protein-SHifter binds to a free thiol group of a protein. The conjugate consists
of a unique molecular weight that clearly visualized in electrophoresis.
Visualization of Redox State of Thiol Residues in a Protein:
Fig. 3 One molecule of Protein-SHifter binds to one molecule
of free-thiol in protein. The number of the conjugation is directly proportional to the number of free thiol as clear band-shift.
- Linearity of mobility shifts derived from Protein SHifter comparing with PEG-Maleimide (PEG-Mal)
*Conjugation with Thioredoxin
- Clear band-shift observed from Protein SHIfter comparing with PEG-Mal.
1)Satoshi Hara,Tatsuya Nojima,Kohji Seio, Masasuke Yoshida,Toru Hisabori."DNA-maleimide:
An improved maleimide compound for electrophoresis-based titration of reactive
thiols in a specificprotein"Biochimical
et Biophysical Acta,2013,1830(4)
2)Satoshi Hara,Yuki Tatenaka, Yuya Ohuchi, Toru Hisabori,"Direct determination of
the redox status of cysteine residues in proteins in vivo". Biochimical and Biophysical Research
Detection of Redox State of Thiols residues in GAPDH
1) S. Hara, T. Nojima, K. Seio, M. Yoshida and T. Hisabori, "DNA-maleimide: An improved maleimide compound for electrophoresis-based titration of reactive thiols in a specific protein" Biochim. Biophys. Acta, 2013, 1830(4), 3077.
2) S. Hara, Y. Tatenaka, Y. Ohuchi and T. Hisabori, "Direct determination of the redox status of cysteine residues in proteins in vivo", Biochem. Biophys. Res. Commun., 2015, 456, (1), 339.