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Benzene, 1,1'-[2-butene-1,4-diylbis(thio)]bis- is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

49824-79-5

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49824-79-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 49824-79-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 4,9,8,2 and 4 respectively; the second part has 2 digits, 7 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 49824-79:
(7*4)+(6*9)+(5*8)+(4*2)+(3*4)+(2*7)+(1*9)=165
165 % 10 = 5
So 49824-79-5 is a valid CAS Registry Number.

49824-79-5Downstream Products

49824-79-5Relevant academic research and scientific papers

Vortex Fluidic Ethenolysis, Integrating a Rapid Quench of Ruthenium Olefin Metathesis Catalysts

Pye, Scott J.,Chalker, Justin M.,Raston, Colin L.

, p. 1138 - 1143 (2020/08/27)

Ruthenium-catalysed ethenolysis occurs in a vortex fluidic device (VFD)-a scalable, thin-film microfluidic continuous flow process. This process takes advantage of the efficient mass transfer of gaseous reagents into the dynamic thin film of liquid. Also reported is the rapid quenching of the ruthenium-based olefin metathesis catalyst by the addition of a saturated solution of N-acetyl-l-cysteine in MeCN, as a convenient alternative to previously reported quenching methods.

Allyl sulfides are privileged substrates in aqueous cross-metathesis: Application to site-selective protein modification

Lin, Yuya A.,Chalker, Justin M.,Floyd, Nicola,Bernardes, Goncalo J. L.,Davis, Benjamin G.

supporting information; experimental part, p. 9642 - 9643 (2009/02/04)

Allyl sulfides undergo efficient cross-metathesis in aqueous media with Hoveyda-Grubbs second generation catalyst 1. The high reactivity of allyl sulfides in cross-metathesis was exploited in the first examples of cross-metathesis on a protein surface. S-Allylcysteine was incorporated chemically into the protein, providing the requisite allyl sulfide handle. Preliminary efforts to genetically incorporate S-allylcysteine into proteins are also reported. Copyright

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