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Cbz-2-Bromo-L-Phenylalanine is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

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  • 1270295-82-3 Structure
  • Basic information

    1. Product Name: Cbz-2-Bromo-L-Phenylalanine
    2. Synonyms: Cbz-2-Bromo-L-Phenylalanine;Cbz-L-2-Br-Phe-OH
    3. CAS NO:1270295-82-3
    4. Molecular Formula: C17H16BrNO4
    5. Molecular Weight: 378.21724
    6. EINECS: N/A
    7. Product Categories: N/A
    8. Mol File: 1270295-82-3.mol
  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: N/A
    3. Flash Point: N/A
    4. Appearance: /
    5. Density: N/A
    6. Refractive Index: N/A
    7. Storage Temp.: N/A
    8. Solubility: N/A
    9. CAS DataBase Reference: Cbz-2-Bromo-L-Phenylalanine(CAS DataBase Reference)
    10. NIST Chemistry Reference: Cbz-2-Bromo-L-Phenylalanine(1270295-82-3)
    11. EPA Substance Registry System: Cbz-2-Bromo-L-Phenylalanine(1270295-82-3)
  • Safety Data

    1. Hazard Codes: N/A
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany:
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 1270295-82-3(Hazardous Substances Data)

1270295-82-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 1270295-82-3 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,2,7,0,2,9 and 5 respectively; the second part has 2 digits, 8 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 1270295-82:
(9*1)+(8*2)+(7*7)+(6*0)+(5*2)+(4*9)+(3*5)+(2*8)+(1*2)=153
153 % 10 = 3
So 1270295-82-3 is a valid CAS Registry Number.

1270295-82-3Relevant articles and documents

Superiority of the carbamoylmethyl ester as an acyl donor for the kinetically controlled amide-bond formation mediated by α-chymotrypsin

Miyazawa, Toshifumi,Ensatsu, Eiichi,Yabuuchi, Nobuhiro,Yanagihara, Ryoji,Yamada, Takashi

, p. 390 - 395 (2007/10/03)

The superiority of the carbamoylmethyl ester as an acyl donor for the α-chymotrypsin-catalysed kinetically controlled peptide-bond formation is demonstrated in the couplings of an inherently poor amino acid substrate, Ala, with various amino acid residues as amino components and in the couplings of non-protein amino acids such as halogenophenylalanines as carboxylic components. Furthermore, this approach is applied to the amide-bond formation between an amino acid residue and a chiral amine, which is highly diastereoselective.

α-chymotrypsin-catalysed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in organic solvents with low water content: Incorporation of non-protein amino acids into peptides

Miyazawa, Toshifumi,Nakajo, Shin'ichi,Nishikawa, Miyako,Hamahara, Kazumi,Imagawa, Kiwamu,Ensatsu, Eiichi,Yanagihara, Ryoji,Yamada, Takashi

, p. 82 - 86 (2007/10/03)

The α-chymotrypsin-catalyzed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in orgnanic solvents with low water content was presented. The methyl esters of N-Z derivatives of racemic non-protein amino acids were chosen as carboxy components. They allowed the peptide-bond formation and optical resolution simultaneously to yield homochiral peptides. This method is useful for the incorporation of non-protein amino acids into peptides.

Remarkable effects of donor esters on the α-chymotrypsin-catalyzed couplings of inherently poor amino acid substrates

Miyazawa, Toshifumi,Tanaka, Kayoko,Ensatsu, Eiichi,Yanagihara, Ryoji,Yamada, Takashi

, p. 997 - 1000 (2007/10/03)

The extremely low efficiency during the α-chymotrypsin-catalyzed coupling of an inherently poor amino acid substrate, e.g., alanine, using the methyl ester as an acyl donor was significantly improved using esters such as the 2,2,2-trifluoroethyl or carbamoylmethyl ester. The ameliorating effect of the latter ester was especially significant.

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