{"product_id":"carboxypeptidase-a","title":"Carboxypeptidase A","description":"\u003cp\u003e\u003cmeta charset=\"UTF-8\"\u003e \u003cmeta name=\"viewport\" content=\"width=device-width, initial-scale=1.0\"\u003e\u003cmeta name=\"description\" content=\"Carboxypeptidase A from bovine pancreas (EC 3.4.17.1), zinc metalloexopeptidase for C-terminal Phe\/Tyr\/Trp cleavage. Protein sequencing. Optimal pH 7-8.\"\u003e \u003cmeta name=\"keywords\" content=\"carboxypeptidase A, carboxypeptidase A from bovine pancreas, CPA, 羧肽酶A, EC 3.4.17.1, zinc metalloexopeptidase, metalloenzyme, C-terminal aromatic amino acids, phenylalanine tyrosine tryptophan, protein sequencing, hippuryl-L-phenylalanine, 254 nm\"\u003e \u003clink rel=\"canonical\" href=\"https:\/\/www.example.com\/product\/carboxypeptidase-a-bovine-pancreas\"\u003e \u003clink rel=\"alternate\" hreflang=\"en\" href=\"https:\/\/www.example.com\/en\/product\/carboxypeptidase-a-bovine-pancreas\"\u003e \u003clink rel=\"alternate\" hreflang=\"zh\" href=\"https:\/\/www.example.com\/zh\/product\/carboxypeptidase-a-bovine-pancreas\"\u003e \u003clink rel=\"alternate\" hreflang=\"x-default\" href=\"https:\/\/www.example.com\/product\/carboxypeptidase-a-bovine-pancreas\"\u003e \u003cmeta property=\"og:type\" content=\"product\"\u003e \u003cmeta property=\"og:title\" content=\"Carboxypeptidase A from Bovine Pancreas, EC 3.4.17.1\"\u003e \u003cmeta property=\"og:description\" content=\"Carboxypeptidase A from bovine pancreas (EC 3.4.17.1), zinc metalloexopeptidase for C-terminal Phe\/Tyr\/Trp cleavage. Protein sequencing. Optimal pH 7-8.\"\u003e \u003cmeta property=\"og:url\" content=\"https:\/\/www.example.com\/product\/carboxypeptidase-a-bovine-pancreas\"\u003e \u003cmeta property=\"og:image\" content=\"https:\/\/www.example.com\/images\/carboxypeptidase-a-bovine-pancreas.jpg\"\u003e \u003cmeta property=\"og:image:alt\" content=\"Carboxypeptidase A from bovine pancreas, EC 3.4.17.1\"\u003e \u003cmeta property=\"og:locale\" content=\"en_US\"\u003e \u003cmeta property=\"og:locale:alternate\" content=\"zh_CN\"\u003e \u003cmeta property=\"og:site_name\" content=\"Example BioReagents\"\u003e \u003cmeta name=\"twitter:card\" content=\"summary_large_image\"\u003e \u003cmeta name=\"twitter:title\" content=\"Carboxypeptidase A from Bovine Pancreas, EC 3.4.17.1\"\u003e \u003cmeta name=\"twitter:description\" content=\"Carboxypeptidase A from bovine pancreas (EC 3.4.17.1), zinc metalloexopeptidase for C-terminal Phe\/Tyr\/Trp cleavage. Protein sequencing. Optimal pH 7-8.\"\u003e \u003cmeta name=\"twitter:image\" content=\"https:\/\/www.example.com\/images\/carboxypeptidase-a-bovine-pancreas.jpg\"\u003e \u003cscript type=\"application\/ld+json\"\u003e\n{\n  \"@context\": \"https:\/\/schema.org\",\n  \"@type\": \"Product\",\n  \"name\": \"Carboxypeptidase A from Bovine Pancreas\",\n  \"description\": \"Carboxypeptidase A from bovine pancreas (EC 3.4.17.1) is a zinc-containing pancreatic exopeptidase that preferentially hydrolyzes peptide bonds at C-terminal aromatic amino acids (phenylalanine, tyrosine, tryptophan). Molecular weight approximately 35,000 Da, optimal pH 7-8. One unit hydrolyzes 1 μmol of hippuryl-L-phenylalanine per minute at 25°C, pH 7.5, measured by increase in absorbance at 254 nm.\",\n  \"sku\": \"BF-2060050\",\n  \"mpn\": \"BF-2060050\",\n  \"category\": \"Biochemical Reagents \/ Enzymes\"\n}\n\u003c\/script\u003e \u003cscript type=\"application\/ld+json\"\u003e\n{\n  \"@context\": \"https:\/\/schema.org\",\n  \"@type\": \"FAQPage\",\n  \"mainEntity\": [\n    {\n      \"@type\": \"Question\",\n      \"name\": \"What is Carboxypeptidase A?\",\n      \"acceptedAnswer\": {\n        \"@type\": \"Answer\",\n        \"text\": \"Carboxypeptidase A (EC 3.4.17.1), also known as peptidyl-L-amino acid hydrolase, is a zinc-containing pancreatic exopeptidase from bovine pancreas with a molecular weight of approximately 35,000 Da. It preferentially hydrolyzes peptide bonds at C-terminal aromatic amino acids.\"\n      }\n    },\n    {\n      \"@type\": \"Question\",\n      \"name\": \"What is the source of this Carboxypeptidase A?\",\n      \"acceptedAnswer\": {\n        \"@type\": \"Answer\",\n        \"text\": \"This Carboxypeptidase A is derived from bovine pancreas.\"\n      }\n    },\n    {\n      \"@type\": \"Question\",\n      \"name\": \"Which amino acids does Carboxypeptidase A cleave?\",\n      \"acceptedAnswer\": {\n        \"@type\": \"Answer\",\n        \"text\": \"Carboxypeptidase A preferentially hydrolyzes C-terminal aromatic amino acids — phenylalanine, tyrosine and tryptophan. Glycine, aspartic acid and glutamic acid are hydrolyzed slowly, while arginine, proline and hydroxyproline are not hydrolyzed.\"\n      }\n    },\n    {\n      \"@type\": \"Question\",\n      \"name\": \"What is the optimal pH of Carboxypeptidase A?\",\n      \"acceptedAnswer\": {\n        \"@type\": \"Answer\",\n        \"text\": \"The optimal pH range of Carboxypeptidase A is 7-8.\"\n      }\n    },\n    {\n      \"@type\": \"Question\",\n      \"name\": \"How is Carboxypeptidase A activity defined?\",\n      \"acceptedAnswer\": {\n        \"@type\": \"Answer\",\n        \"text\": \"One unit of Carboxypeptidase A hydrolyzes 1 μmol of hippuryl-L-phenylalanine per minute at 25°C and pH 7.5.\"\n      }\n    },\n    {\n      \"@type\": \"Question\",\n      \"name\": \"How is Carboxypeptidase A activity measured?\",\n      \"acceptedAnswer\": {\n        \"@type\": \"Answer\",\n        \"text\": \"Activity is measured by the increase in absorbance at 254 nm during hydrolysis of hippuryl-L-phenylalanine. The initial linear rate (ΔE254\/min) is used in the formula: Activity (U\/mg) = (ΔE254\/min × Total Vol. × Enz. Diln.) \/ (0.36 × mg Enz.\/ml).\"\n      }\n    },\n    {\n      \"@type\": \"Question\",\n      \"name\": \"Is Carboxypeptidase A a metalloenzyme?\",\n      \"acceptedAnswer\": {\n        \"@type\": \"Answer\",\n        \"text\": \"Yes. Carboxypeptidase A is a zinc-containing metalloenzyme; the zinc ion is tightly coordinated by two histidine imidazole rings and the carboxyl group of one glutamic acid residue.\"\n      }\n    },\n    {\n      \"@type\": \"Question\",\n      \"name\": \"How should the enzyme be prepared for the activity assay?\",\n      \"acceptedAnswer\": {\n        \"@type\": \"Answer\",\n        \"text\": \"Dissolve Carboxypeptidase A in 10% LiCl to 1-3 U\/ml, and add to a 1 mM hippuryl-L-phenylalanine solution in 50 mM Tris\/HCl buffer (containing 1.0 M NaCl), pH 7.5. Monitor the increase in absorbance at 254 nm over 5 minutes at 25°C.\"\n      }\n    }\n  ]\n}\n\u003c\/script\u003e \u003cscript type=\"application\/ld+json\"\u003e\n{\n  \"@context\": \"https:\/\/schema.org\",\n  \"@type\": \"Organization\",\n  \"name\": \"Example BioReagents\",\n  \"url\": \"https:\/\/www.example.com\"\n}\n\u003c\/script\u003e \u003cscript type=\"application\/ld+json\"\u003e\n{\n  \"@context\": \"https:\/\/schema.org\",\n  \"@type\": \"BreadcrumbList\",\n  \"itemListElement\": [\n    {\n      \"@type\": \"ListItem\",\n      \"position\": 1,\n      \"name\": \"Home\",\n      \"item\": \"https:\/\/www.example.com\"\n    },\n    {\n      \"@type\": \"ListItem\",\n      \"position\": 2,\n      \"name\": \"Products\",\n      \"item\": \"https:\/\/www.example.com\/products\"\n    },\n    {\n      \"@type\": \"ListItem\",\n      \"position\": 3,\n      \"name\": \"Carboxypeptidase A from Bovine Pancreas\",\n      \"item\": \"https:\/\/www.example.com\/product\/carboxypeptidase-a-bovine-pancreas\"\n    }\n  ]\n}\n\u003c\/script\u003e\u003c\/p\u003e\n\u003cstyle\u003e\n  * { box-sizing: border-box; }\n  body {\n    margin: 0;\n    padding: 0;\n    background: #ffffff;\n    color: #1f2937;\n    font-family: -apple-system, BlinkMacSystemFont, \"Segoe UI\", Roboto, \"Helvetica Neue\", Arial, sans-serif;\n    line-height: 1.7;\n  }\n  .product-detail {\n    max-width: 880px;\n    margin: 0 auto;\n    padding: 8px 20px 60px;\n  }\n  h2 {\n    font-size: 1.4rem;\n    color: #111827;\n    border-bottom: 2px solid #e5e7eb;\n    padding-bottom: 10px;\n    margin: 48px 0 18px;\n  }\n  .product-detail h2:first-of-type {\n    margin-top: 0;\n  }\n  p, li {\n    color: #374151;\n    line-height: 1.75;\n  }\n  .reaction {\n    margin: 16px 0;\n    font-family: \"SFMono-Regular\", Consolas, \"Liberation Mono\", Menlo, monospace;\n    font-size: 0.95rem;\n    color: #111827;\n  }\n  .table-wrap {\n    overflow-x: auto;\n    -webkit-overflow-scrolling: touch;\n    border: 1px solid #e5e7eb;\n    border-radius: 6px;\n  }\n  table {\n    width: 100%;\n    min-width: 600px;\n    border-collapse: collapse;\n    font-size: 0.95rem;\n  }\n  th, td {\n    border: 1px solid #e5e7eb;\n    padding: 10px 14px;\n    text-align: left;\n    vertical-align: top;\n  }\n  th {\n    background: #f3f4f6;\n    font-weight: 600;\n    color: #111827;\n    width: 40%;\n  }\n  ul.features, ul.applications {\n    padding-left: 22px;\n    margin: 12px 0;\n  }\n  ul.features li, ul.applications li {\n    margin-bottom: 10px;\n  }\n  details {\n    border: 1px solid #e5e7eb;\n    border-radius: 6px;\n    background: #fafafa;\n    padding: 14px 18px;\n    margin-bottom: 12px;\n  }\n  details summary {\n    cursor: pointer;\n    font-weight: 600;\n    color: #111827;\n    outline: none;\n  }\n  details p {\n    margin: 12px 0 4px;\n  }\n  .note {\n    font-size: 0.85rem;\n    color: #6b7280;\n    margin-top: 24px;\n  }\n\u003c\/style\u003e\n\u003carticle class=\"product-detail\"\u003e\u003c!-- ============ DESCRIPTION ============ --\u003e\n\u003csection id=\"description\"\u003e\n\u003ch2\u003eDescription\u003c\/h2\u003e\n\u003cp\u003eC-terminal aromatic amino acids — phenylalanine, tyrosine or tryptophan — can block protein sequencing, complicate peptide map interpretation, and obscure the true C-terminus of a peptide or protein. Removing or identifying these C-terminal residues cleanly and reproducibly with a well-characterized exopeptidase is a routine first step in protein analysis.\u003c\/p\u003e\n\u003cp\u003eCarboxypeptidase A from bovine pancreas (EC 3.4.17.1) is a zinc-containing pancreatic exopeptidase that preferentially hydrolyzes peptide bonds at C-terminal aromatic amino acids — phenylalanine, tyrosine and tryptophan:\u003c\/p\u003e\n\u003cp class=\"reaction\"\u003ePeptidyl-L-phenylalanine + H\u003csub\u003e2\u003c\/sub\u003eO → Peptide + L-Phenylalanine\u003c\/p\u003e\n\u003cp\u003eAlso known as peptidyl-L-amino acid hydrolase, this Carboxypeptidase A has a molecular weight of approximately 35,000 Da and an optimal pH range of 7-8. Glycine, aspartic acid and glutamic acid are hydrolyzed slowly, while arginine, proline and hydroxyproline are not hydrolyzed.\u003c\/p\u003e\n\u003cp\u003eThe enzyme activity is precisely defined: one unit hydrolyzes 1 µmol of hippuryl-L-phenylalanine per minute at 25°C and pH 7.5, and hydrolysis is followed directly by the increase in absorbance at 254 nm. For the assay, the enzyme is dissolved in 10% LiCl at 1-3 U\/ml and added to a 1 mM hippuryl-L-phenylalanine solution in 50 mM Tris\/HCl buffer (containing 1.0 M NaCl), pH 7.5. With this clear unit definition and simple spectrophotometric assay, Carboxypeptidase A delivers reproducible C-terminal digestion for protein analysis workflows.\u003c\/p\u003e\n\u003c\/section\u003e\n\u003c!-- ============ SPECIFICATION ============ --\u003e\n\u003csection id=\"specification\"\u003e\n\u003ch2\u003eSpecification\u003c\/h2\u003e\n\u003cdiv class=\"table-wrap\"\u003e\n\u003ctable\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003cth\u003eProduct Name\u003c\/th\u003e\n\u003ctd\u003eCarboxypeptidase A\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003cth\u003eSynonyms\u003c\/th\u003e\n\u003ctd\u003ePeptidyl-L-amino acid hydrolase\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003cth\u003eCatalog Number\u003c\/th\u003e\n\u003ctd\u003eBF-2060050\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003cth\u003eEC Number\u003c\/th\u003e\n\u003ctd\u003e3.4.17.1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003cth\u003eBiological Source\u003c\/th\u003e\n\u003ctd\u003eBovine pancreas\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003cth\u003eMolecular Weight\u003c\/th\u003e\n\u003ctd\u003eApproximately 35,000 Da\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003cth\u003eOptimal pH\u003c\/th\u003e\n\u003ctd\u003e7-8\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003cth\u003eUnit Definition\u003c\/th\u003e\n\u003ctd\u003eOne unit hydrolyzes 1 µmol hippuryl-L-phenylalanine per minute at 25°C, pH 7.5\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003cth\u003eAssay Method\u003c\/th\u003e\n\u003ctd\u003eIncrease in absorbance at 254 nm during hydrolysis of hippuryl-L-phenylalanine\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e\n\u003c\/div\u003e\n\u003c\/section\u003e\n\u003c!-- ============ FEATURES ============ --\u003e\n\u003csection id=\"features\"\u003e\n\u003ch2\u003eFeatures\u003c\/h2\u003e\n\u003cul class=\"features\"\u003e\n\u003cli\u003ePreferential hydrolysis of C-terminal aromatic amino acids — phenylalanine, tyrosine and tryptophan\u003c\/li\u003e\n\u003cli\u003eZinc-containing metalloexopeptidase from bovine pancreas with a molecular weight of approximately 35,000 Da\u003c\/li\u003e\n\u003cli\u003eZinc ion tightly coordinated by two histidine imidazole rings and the carboxyl group of one glutamic acid residue\u003c\/li\u003e\n\u003cli\u003eOptimal pH range of 7-8\u003c\/li\u003e\n\u003cli\u003eSlow hydrolysis of glycine, aspartic acid and glutamic acid; no hydrolysis of arginine, proline or hydroxyproline\u003c\/li\u003e\n\u003cli\u003eWell-defined unit: 1 U hydrolyzes 1 µmol hippuryl-L-phenylalanine per minute at 25°C, pH 7.5\u003c\/li\u003e\n\u003cli\u003eSimple spectrophotometric activity monitoring at 254 nm\u003c\/li\u003e\n\u003cli\u003eAssay-ready: dissolved in 10% LiCl to 1-3 U\/ml for the activity assay\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c\/section\u003e\n\u003c!-- ============ APPLICATION ============ --\u003e\n\u003csection id=\"application\"\u003e\n\u003ch2\u003eApplication\u003c\/h2\u003e\n\u003cp\u003eCarboxypeptidase A is used in protein analysis workflows:\u003c\/p\u003e\n\u003cul class=\"applications\"\u003e\n\u003cli\u003eProtein C-terminal amino acid determination and sequencing\u003c\/li\u003e\n\u003cli\u003eRemoval of C-terminal aromatic amino acids (phenylalanine, tyrosine, tryptophan) from peptides and proteins\u003c\/li\u003e\n\u003cli\u003ePeptide mapping and proteomics sample preparation\u003c\/li\u003e\n\u003cli\u003eCharacterization of C-terminal residues of peptides and proteins\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003c\/section\u003e\n\u003c!-- ============ FAQ ============ --\u003e\n\u003csection id=\"faq\"\u003e\n\u003ch2\u003eFAQ\u003c\/h2\u003e\n\u003cdetails\u003e\n\u003csummary\u003eWhat is Carboxypeptidase A?\u003c\/summary\u003e\n\u003cp\u003eCarboxypeptidase A (EC 3.4.17.1), also known as peptidyl-L-amino acid hydrolase, is a zinc-containing pancreatic exopeptidase from bovine pancreas with a molecular weight of approximately 35,000 Da. It preferentially hydrolyzes peptide bonds at C-terminal aromatic amino acids.\u003c\/p\u003e\n\u003c\/details\u003e\n\u003cdetails\u003e\n\u003csummary\u003eWhat is the source of this Carboxypeptidase A?\u003c\/summary\u003e\n\u003cp\u003eThis Carboxypeptidase A is derived from bovine pancreas.\u003c\/p\u003e\n\u003c\/details\u003e\n\u003cdetails\u003e\n\u003csummary\u003eWhich amino acids does Carboxypeptidase A cleave?\u003c\/summary\u003e\n\u003cp\u003eCarboxypeptidase A preferentially hydrolyzes C-terminal aromatic amino acids — phenylalanine, tyrosine and tryptophan. Glycine, aspartic acid and glutamic acid are hydrolyzed slowly, while arginine, proline and hydroxyproline are not hydrolyzed.\u003c\/p\u003e\n\u003c\/details\u003e\n\u003cdetails\u003e\n\u003csummary\u003eWhat is the optimal pH of Carboxypeptidase A?\u003c\/summary\u003e\n\u003cp\u003eThe optimal pH range of Carboxypeptidase A is 7-8.\u003c\/p\u003e\n\u003c\/details\u003e\n\u003cdetails\u003e\n\u003csummary\u003eHow is Carboxypeptidase A activity defined?\u003c\/summary\u003e\n\u003cp\u003eOne unit of Carboxypeptidase A hydrolyzes 1 µmol of hippuryl-L-phenylalanine per minute at 25°C and pH 7.5.\u003c\/p\u003e\n\u003c\/details\u003e\n\u003cdetails\u003e\n\u003csummary\u003eHow is Carboxypeptidase A activity measured?\u003c\/summary\u003e\n\u003cp\u003eActivity is measured by the increase in absorbance at 254 nm during hydrolysis of hippuryl-L-phenylalanine. The initial linear rate (ΔE\u003csub\u003e254\u003c\/sub\u003e\/min) is used in the formula: Activity (U\/mg) = (ΔE\u003csub\u003e254\u003c\/sub\u003e\/min × Total Vol. × Enz. Diln.) \/ (0.36 × mg Enz.\/ml).\u003c\/p\u003e\n\u003c\/details\u003e\n\u003cdetails\u003e\n\u003csummary\u003eIs Carboxypeptidase A a metalloenzyme?\u003c\/summary\u003e\n\u003cp\u003eYes. Carboxypeptidase A is a zinc-containing metalloenzyme; the zinc ion is tightly coordinated by two histidine imidazole rings and the carboxyl group of one glutamic acid residue.\u003c\/p\u003e\n\u003c\/details\u003e\n\u003cdetails\u003e\n\u003csummary\u003eHow should the enzyme be prepared for the activity assay?\u003c\/summary\u003e\n\u003cp\u003eDissolve Carboxypeptidase A in 10% LiCl to 1-3 U\/ml, and add to a 1 mM hippuryl-L-phenylalanine solution in 50 mM Tris\/HCl buffer (containing 1.0 M NaCl), pH 7.5. Monitor the increase in absorbance at 254 nm over 5 minutes at 25°C, using the initial linear rate for calculation.\u003c\/p\u003e\n\u003c\/details\u003e\n\u003c\/section\u003e\n\u003cp class=\"note\"\u003eFor research use only. Not for use in diagnostic or therapeutic procedures.\u003c\/p\u003e\n\u003c\/article\u003e","brand":"calzyme","offers":[{"title":"1 g","offer_id":52985275482293,"sku":"BF-2060050","price":0.0,"currency_code":"USD","in_stock":true},{"title":"10 g","offer_id":52985275515061,"sku":"BF-2060051","price":0.0,"currency_code":"USD","in_stock":true},{"title":"100 g","offer_id":52985275547829,"sku":"BF-2060052","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0521\/5312\/2997\/files\/carboxypeptidase-a-aqueous-suspension-1500x1500.jpg?v=1787117982","url":"https:\/\/biofargo.com\/products\/carboxypeptidase-a","provider":"Biofargo","version":"1.0","type":"link"}