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MilliporeSigma

C3888

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

lyophilized powder, ≥50 units/mg protein

Sinónimos:

Peptidyl-L-amino acid Hydrolase, Serine Carboxypeptidase

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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
Número CE:
MDL number:
Specific activity:
≥50 units/mg protein
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grade

Proteomics Grade

form

lyophilized powder

specific activity

≥50 units/mg protein

mol wt

61 kDa

composition

Protein, ≥75% E1%/280

shipped in

wet ice

storage temp.

−20°C

Application

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.

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.

Packaging

Package size based on protein content

Physical form

Lyophilized powder containing citric acid.

Analysis Note

amidase and esterase activities may be present

Other Notes

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.


pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable



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