protein

Carboxypeptidase A1/CPA1 Protein, Mouse (HEK293, His)

HY-P72868

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

65;110;290;490;1375;2200 USD

Carboxypeptidase A1/CPA1 Protein, Mouse (HEK293, His)

proteins

HEK293

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

65;110;290;490;1375;2200 USD

Carboxypeptidase A1 (CPA1) is an enzyme responsible for catalyzing the release of a C-terminal amino acid; however, it exhibits limited or no activity with residues such as -Asp, -Glu, -Arg, -Lys, or -Pro. This specificity in substrate recognition underscores its role as a carboxypeptidase with selectivity towards certain amino acid sequences at the C-terminus of peptides. Carboxypeptidase A1/CPA1 Protein, Mouse (HEK293, His) is the recombinant mouse-derived Carboxypeptidase A1/CPA1 protein, expressed by HEK293 , with C-His labeled tag. The total length of Carboxypeptidase A1/CPA1 Protein, Mouse (HEK293, His) is 403 a.a., with molecular weight of ~42-49 kDa.

Mouse

Carboxypeptidase A1 (CPA1) is an enzyme that plays a crucial role in catalyzing the release of C-terminal amino acids from peptides. However, its activity is limited or absent for peptides with C-terminal residues such as -Asp, -Glu, -Arg, -Lys, or -Pro. This substrate specificity indicates that CPA1 exhibits selectivity in its cleavage preferences, preferring certain amino acid residues at the C-terminus of peptides. The enzyme's action in releasing C-terminal amino acids contributes to various physiological processes, such as the digestion of proteins in the digestive system, highlighting its importance in the regulation of peptide and protein metabolism.

Carboxypeptidase A1; Cpa1

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of 20 mM Tris, 150 mM NaCl, pH 7.5 or 25 mM Tris-HCL, 150 mM NaCl, pH 7.5.

Room temperature in continental US; may vary elsewhere.