Carboxypeptidase Y (Glyco-062CL)
Carboxypeptidase Y is a protease with that is able to cleave (release) any terminal amino acid including proline from the C-terminus of peptides.
Specifications
- Product Size
- 1 mg
- Contents & storage
- Store at -20°C.
BACKGROUND
- Description
- Carboxypeptidase Y is a glycoprotein exopeptidase of the serine class. Carboxypeptidase Y has a broad amino acid specificity, and is able to release every amino acid including proline from the carboxyl-terminus of peptides, although glycine and aspartic acid are released much more slowly than other residues. It is active in urea and SDS solutions and retains its activity under the denaturing conditions used for polypeptide sequencing.
- Properties
- • Alternative names: Proteinase C, yeast carboxypeptidase Y
• Specificity: Cleaves residues sequentially from the carboxy terminus
• Source: S. cerevisiae (bakers yeast)
• Molecular weight: 61,000
• Protease type: Serine exopeptidase
• Uses/applications: Peptide hydrolysis for sequencing
• Reaction conditions: pH 5.5-7.5, 25°C
• Inhibitors: PMSF and DFP
• Unit definition: One unit of carboxypeptidase Y hydrolyzes one µMol of benzyl-oxycarbonyl-L-phenylalanyl-L-leucine per minute at 25°C, pH 6.5
Immobilized carboxypeptidase Y can be substituted for free carboxypeptidase Y in any application, and is advantageous because it virtually eliminates autolysis, eliminates contamination of a sample with the protease and allows control of the digestion by removing the carboxypeptidase Y. Immobilized carboxypeptidase Y is also more stable against heat-induced denaturation, resulting in longer maintenance of activity.
For lab research use only, not for diagnostic, therapeutic or any in vivo human use.
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