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875680-89-0

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875680-89-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 875680-89-0 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 8,7,5,6,8 and 0 respectively; the second part has 2 digits, 8 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 875680-89:
(8*8)+(7*7)+(6*5)+(5*6)+(4*8)+(3*0)+(2*8)+(1*9)=230
230 % 10 = 0
So 875680-89-0 is a valid CAS Registry Number.

875680-89-0Relevant articles and documents

Practical and scalable synthesis of orthogonally protected-2-substituted chiral piperazines

Chamakuri, Srinivas,Santini, Conrad,Shah, Manuj M.,Yang, David C. H.,Young, Damian W.

, p. 8844 - 8849 (2020)

A synthetic route to orthogonally protected, enantiomerically pure 2-substituted piperazines is described. Starting from α-amino acids, within four steps chiral 2-substituted piperazines are obtained. The key transformation involves an aza-Michael additio

α-methyl polyamines: Efficient synthesis and tolerance studies in vivo and in vitro. First evidence for dormant stereospecificity of polyamine oxidase

J?rvinen, Aki J.,Cerrada-Gimenez, Marc,Grigorenko, Nikolay A.,Khomutov, Alex R.,Veps?l?inen, Jouko J.,Sinervirta, Riitta M.,Kein?nen, Tuomo A.,Alhonen, Leena I.,J?nne, Juhani E.

, p. 399 - 406 (2007/10/03)

Efficient syntheses of metabolically stable α-methylspermidine 1, α-methylspermine 2, and bis-α,α-methylated spermine 3 starting from ethyl 3-aminobutyrate are described. The biological tolerance for these compounds was tested in wild-type mice and transgenic mice carrying the metallothionein promoter-driven spermidine/spermine N1- acetyltransferase gene (MT-SSAT). The efficient substitution of natural polyamines by their derivatives was confirmed in vivo with the rats harboring the same MT-SSAT transgene and in vitro with the immortalized fibroblasts derived from these animals. Enantiomers of previously unknown 1-amino-8-acetamido-5-azanonane dihydrochloride 4 were synthesized starting from enantiomerically pure (R)- and (S)-alaninols. The studies with recombinant human polyamine oxidase (PAO) showed that PAO (usually splits achiral substrates) strongly favors the (R)-isomer of 4 that demonstrates for the first time that the enzyme has hidden potency for stereospecificity.

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