Todas as fotos(1)

Documentos Principais

COO/COA

Visualizar Toda a Documentação

C1877

Z-Ile-Leu

Name: Z-Ile-Leu
Brand: SIGMA

Sinônimo(s):

N-CBZ-Ile-Ieu

Faça loginpara ver os preços organizacionais e de contrato

Todas as fotos(1)

About This Item

Fórmula empírica (Notação de Hill):

C₂₀H₃₀N₂O₅

Número CAS:

38972-95-1

Peso molecular:

378.46

Número MDL:

MFCD00056158

Código UNSPSC:

12352200

ID de substância PubChem:

24892443

temperatura de armazenamento

−20°C

cadeia de caracteres SMILES

CCC(C)C(NC(=O)OCc1ccccc1)C(=O)NC(CC(C)C)C(O)=O

InChI

1S/C20H30N2O5/c1-5-14(4)17(18(23)21-16(19(24)25)11-13(2)3)22-20(26)27-12-15-9-7-6-8-10-15/h6-10,13-14,16-17H,5,11-12H2,1-4H3,(H,21,23)(H,22,26)(H,24,25)

chave InChI

BSRAGXJNZJMFMY-UHFFFAOYSA-N

Ações bioquímicas/fisiológicas

N-CBZ-Ile-Ieu (Z-Ile-Ieu) (CBZ-isoleucylleucine) is an N-terminal protected Cbz-dipeptide substrate used to differentiate, characterize and kinetically analyze various carboxypeptidase(s).

Código de classe de armazenamento

13 - Non Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

Já possui este produto?

Encontre a documentação dos produtos que você adquiriu recentemente na biblioteca de documentos.

Visite a Biblioteca de Documentos

Cathepsin A-like activity is possibly the main acidic carboxypeptidase in human platelets.

H Ostrowska

Platelets, 8(5), 355-360 (2006-06-24)

Human platelets were investigated for activity of the acidic carboxypeptidases: cathepsin A, lysosomal carboxypeptidase B and prolyl-carboxypeptidase. It was found that the main acidic carboxypeptidase in human platelets had cathepsin A activity. No activity of lysosomal carboxypeptidase B and prolyl-carboxypeptidase

Characterization of a bifunctional aminoacylase/carboxypeptidase from radioresistant bacterium Deinococcus radiodurans R1.

Long-Liu Lin et al.

Journal of biotechnology, 128(2), 322-334 (2006-11-30)

The gene encoding a Deinococcus radiodurans R1 bifunctional aminoacylase/carboxypeptidase (DR_ACY/CP) was amplified by polymerase chain reaction and cloned into pQE-30 to generate pQE-DRAC. The cloned gene consists of an open reading frame of 1197 bp encoding a protein with a

Amphipathic property of free thiol group contributes to an increase in the catalytic efficiency of carboxypeptidase Y.

Joji Mima et al.

European journal of biochemistry, 269(13), 3220-3225 (2002-06-27)

Cys341 of carboxypeptidase Y, which constitutes one side of the solvent-accessible surface of the S1 binding pocket, was replaced with Gly, Ser, Asp, Val, Phe or His by site-directed mutagenesis. Kinetic analysis, using Cbz-dipeptide substrates, revealed that polar amino acids

Debittering effect of Actinomucor elegans peptidases on soybean protein hydrolysates.

Li Li et al.

Journal of industrial microbiology & biotechnology, 35(1), 41-47 (2007-10-19)

Effects of the enzymes in Actinomucor elegans extract and the enzyme Alcalase 2.4L on debittering the soybean protein hydrolysates were investigated. When the protein was treated only with the latter, a strong bitterness formed; but it decreased if the protein

Nossa equipe de cientistas tem experiência em todas as áreas de pesquisa, incluindo Life Sciences, ciência de materiais, síntese química, cromatografia, química analítica e muitas outras.

Entre em contato com a assistência técnica