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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About This Item
Número de CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Productos recomendados
grade
Proteomics Grade
Quality Level
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
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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
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
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
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