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Carboxypeptidase P (Highly Pure)

$595.00

Catalog Number: B2012542 (1 mg)
Carboxypeptidase P (Highly Pure) is a high quality proteolytic enzyme that hydrolyzes the carboxyl terminus of the protein. This product has been used as molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request.

Live enquiry about this product via Text/SMS: 1-858-900-3210.

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SKU: B2012542 Categories: , Tag:

Description

Carboxypeptidase P (Highly Pure)
Catalog number: B2012542
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 1 mg
Molecular Weight or Concentration: 252.2 g/mol
Supplied as: Solution
Applications: molecular tool for various biochemical applications
Storage: -20°C
Keywords: protein, carboxypeptidase, amino, amino acid, sequence
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

References:
1: Barouch WW. Carboxypeptidase P cleaves Lys-Lys Pept Res. 1990 Mar-Apr;3(2):73-4.
2: Walter R, Simmons WH, Yoshimoto T. Proline specific endo- and exopeptidases Mol Cell Biochem. 1980 Apr 18;30(2):111-27.
3: Fukuda M, Shima H, Kunugi S. Kinetic study of carboxypeptidase P-catalyzed reaction. Pressure and temperature dependence of kinetic parameters J Biochem. 1985 Aug;98(2):517-25.
4: Thiede B, Wittmann-Liebold B, Bienert M, Krause E. MALDI-MS for C-terminal sequence determination of peptides and proteins degraded by carboxypeptidase Y and P FEBS Lett. 1995 Jan 2;357(1):65-9.
5: Yoshioka M, Erickson RH, Kim YS. Digestion and assimilation of proline-containing peptides by rat intestinal brush border membrane carboxypeptidases. Role of the combined action of angiotensin-converting enzyme and carboxypeptidase P J Clin Invest. 1988 Apr;81(4):1090-5.
6: Himeno S, Chittum HS, Burk RF. Isoforms of selenoprotein P in rat plasma. Evidence for a full-length form and another form that terminates at the second UGA in the open reading frame J Biol Chem. 1996 Jun 28;271(26):15769-75.
7: Furusawa H, Takano H, Okahata Y. Transient kinetic studies of pH-dependent hydrolyses by exo-type carboxypeptidase P on a 27-MHz quartz crystal microbalance Anal Chem. 2008 Feb 15;80(4):1005-11.
8: Cheng S, Guan F, Ma M, Zhang L, Cheng B, Qi X, Liang C, Li P, Kafle OP, Wen Y, Zhang F. An atlas of genetic correlations between psychiatric disorders and human blood plasma proteome Eur Psychiatry. 2020 Feb 20;63(1):e17.
9: Erickson RH, Song IS, Yoshioka M, Gulli R, Miura S, Kim YS. Identification of proline-specific carboxypeptidase localized to brush border membrane of rat small intestine and its possible role in protein digestion Dig Dis Sci. 1989 Mar;34(3):400-6.
10: Hedeager-Sørensen S, Kenny AJ. Proteins of the kidney microvillar membrane. Purification and properties of carboxypeptidase P from pig kidneys Biochem J. 1985 Jul 1;229(1):251-7.

Products Related to Carboxypeptidase P (Highly Pure) can be found at Enzymes

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