You Searched For: L-Tryptophan+benzyl+ester

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Ethyl-2-benzylacetoacetate ≥97%

Catalog Number: (L01573.22)

Supplier: Thermo Fisher Scientific

Description: Ethyl-2-benzylacetoacetate ≥97%

UOM: 1 * 100 g

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Boc-D-Glu(Obzl)-OH

Supplier: Apollo Scientific

Description: Boc-D-Glu(Obzl)-OH

Bovine alpha-Chymotripsin (from Pancreas), MP Biomedicals

Supplier: MP Biomedicals

Description: Preparation Method
Produced from 3× crystallised chymotrypsinogen

α-Chymotrypsin is used for treating pancreatic insufficiency and in traumatology.

Chymotrypsin preferentially catalyses the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine, and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. In addition to bonds involving aromatic amino acids, chymotrypsin catalyses at a high rate the hydrolysis of bonds of leucyl, methionyl, asparaginyl, and glutamyl residues. a-Chymotrypsin is a protein consisting of 241 amino acid residues. The molecule has three peptide chains: an A chain of 13 residues, a B chain of 131 residues, and a C chain of 97 residues.

2-(Carbobenzoxyamino)-1-ethanol 98%

Catalog Number: (APOSOR480631-100G)

Supplier: Apollo Scientific

Description: 2-(Carbobenzoxyamino)-1-ethanol 98%

UOM: 1 * 100 g

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1-N-Cbz-4-aminopiperidine 97%

Catalog Number: (H64424.06)

Supplier: Thermo Fisher Scientific

Description: 1-N-Cbz-4-aminopiperidine 97%

UOM: 1 * 5 g

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Boc-Hyp-OBZL 95%

Supplier: Thermo Fisher Scientific

Description: Boc-Hyp-OBZL 95%

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Human recombinant Carboxypeptidase A2 (from Cells)

Catalog Number: (PRSI91-529)

Supplier: ProSci Inc.

Description: Carboxypeptidase A2 (CPA) is a secreted pancreatic procarboxy-peptidase that cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan. CPA2 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. Three different forms of human pancreatic procarboxypeptidase A have been isolated, and the A1 and A2 forms are always secreted as monomeric proteins with different biochemical properties. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E, and is involved in zymogen inhibition.

UOM: 1 * 50 µG

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