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Carboxypeptidase Y from baker's yeast (S. cerevisiae)

lyophilized powder, ≥50 units/mg protein

Peptidyl-L-amino acid Hydrolase, Serine Carboxypeptidase
CAS Number:
Enzyme Commission number:
MDL number:


Proteomics Grade

Quality Level


lyophilized powder

specific activity

≥50 units/mg protein

mol wt

61 kDa


Protein, ≥75% E1%/280

shipped in

wet ice

storage temp.


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Carboxypeptidase Y has a broad specificity and is stable in urea. Hence, this enzyme is not like other carboxypeptidases and can be used for sequence analysis. Due to its amidase action, this enzyme might be applied to the sequence analysis of peptides having amidated COOH-terminal groups such as oxytocin and vasopressin.


1, 2, 5, 10 mg
Package size based on protein content

Biochem/physiol Actions

The glycoprotein has a molecular weight of about 61,000, has a nitrogen content of 12.74%. It is a single polypeptide chain of 442 residues with 16 residues of glucosamine in the carbohydrate moiety. Lysine is at the NH2 terminus and -Asp-Ser-Thr-Leu is the COOH-terminal sequence. The principal action of the enzyme is to remove COOH-terminal residues from polypeptide chains. It is used as a vacuolar marker enzyme for studies on protein transport and localization.

Unit Definition

One unit will hydrolyze 1.0 μmole of N-CBZ-Phe-Ala to N-CBZ-L-phenylalanine and L-alanine per min at pH 6.75 at 25°C, based on EM/230 = 191.5.

Physical form

Lyophilized powder containing citric acid.

Analysis Note

amidase and esterase activities may be present


Exclamation markHealth hazard

Signal Word


Hazard Statements

Precautionary Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

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Certificate of Origin

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Technical Information

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