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 associate
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 Maleimido group of the Protein-SHifter
binds to a free thiol group of a protein. The conjugate consists of a unique
molecular weight that shifts properly in electrophoresis.
Photocleavage method enhances membrane transcription efficiency in western blotting.
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.
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"
et Biophysical Acta
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
3)Yuichiro J. Suzuki, Faisal Almansour, Camilla Cucinotta, Vladyslava Rybka, Lucia Marcocci,"Cell signaling promoting protein carbonylation does not cause sulfhydryl oxidation: Implications to the mechanism of redox signalingCell signaling promoting protein carbonylation does not cause sulfhydryl oxidation: Implications to the mechanism of redox signaling". F1000Research 2017, 6:455
Detection of the number of thiol on the GAPDH in HeLa cell lysate:
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.