{"id":326,"date":"2023-12-30T14:48:30","date_gmt":"2023-12-30T13:48:30","guid":{"rendered":"https:\/\/asa-enzyme.de\/?post_type=product&p=326"},"modified":"2026-03-02T15:51:48","modified_gmt":"2026-03-02T14:51:48","slug":"carboxypeptidase-b","status":"publish","type":"product","link":"https:\/\/asa-enzyme.de\/de\/produkt\/carboxypeptidase-b\/","title":{"rendered":"Carboxypeptidase B"},"content":{"rendered":"
\n

Carboxypeptidase B<\/h2>\n<\/div>\n
\n
EC 3.4.17.2<\/h6>\n
Exopeptidase<\/h6>\n
Aus<\/strong>\u00a0gen. mod.\u00a0Pichia pastoris<\/em><\/h6>\n

Anwendung:<\/strong>\u00a0Carboxypeptidase B ist eine rekombinante Exopeptidase, die die Hydrolyse der Aminos\u00e4uren Lysin, Arginin und Ornithin vom C-terminalen Ende von Polypeptiden katalysiert.<\/p>\n

Aktivit\u00e4t:<\/strong>\u00a0> 400 U\/mL<\/p>\n

Artikel Nr.:<\/strong>\u00a02500<\/p>\n<\/div>\n

Produktdatenblatt DE<\/strong> CPB-2500-DE<\/a><\/p>\n

Produktdatenblatt ENG <\/strong>CPB – 2500 – ENG<\/a><\/p>\n

Sicherheitsdatenblatt:<\/strong> Auf Anfrage<\/p>\n

Wissenschaftliche Literatur<\/strong><\/p>\n

High-activity recombinant human carboxypeptidaseB expression in Pichia pastoris through rational protein engineering and enhancing secretion from the Golgi apparatus to the plasma membrane<\/a> (By Jia Li,\u00a0<\/span><\/span>Qinan Shao, et al; 2024; Biotechnology Journal<\/em>, Volume 19, Issue 5, May 2024,\u00a0 DOI: <\/span>10.1002\/biot.202400098<\/a><\/span>)<\/span><\/p>\n

Molecular Characterization, Recombinant Expression, and Functional Analysis of CarboxypeptidaseB in <\/a>Litopenaeus vannamei (By <\/span>Hongmei Li, <\/span><\/span>Hai Lin, et al; 2025;\u00a0Genes 2025,\u00a0<\/em>Volume 16, Article 69, January 2025; DOI: 10.3390\/genes16010069<\/a>)<\/p>","protected":false},"excerpt":{"rendered":"

Carboxypeptidase B, EC 3.4.17.2<\/p>\n

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