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-SulfoBiotics- Protein Redox State Monitoring Kit Plus

Item # Unit Size
SB12-10
5 samples
SB12-12
20 samples

For Research Use Only Products

Redox State Visualization

∼ Feature ∼

  1. Monitor redox state of proteins in biological samples
  2. Visualize modification of thiol residues by electophoresis
  3. High transfer efficiency in Western Blotting




Storage Condition: 0-5°C
Shipping Condition: Ambient temperature


Product Description:

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 stress environment.


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.


References:

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) 3077.
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 Communications. 2014,In Press.
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.