C6742
Carboxypeptidase W from wheat
≥50 units/mg protein
form
suspension
specific activity
≥50 units/mg protein
shipped in
dry ice
storage temp.
−20°C
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Application
Carboxypeptidase W from wheat has been used in a study to assess the proteolytic activities in dormant rye (Secale cereale L.) grain. Carboxypeptidase W from wheat has also been used in a study to investigate the structure determination of the human protective protein.
Physical form
One unit will hydrolyze 1.0 μmole of N-CBZ-L-Phe-L-Ala to N-CBZ-L-Phe and L-Ala per minute at pH 4.0 at 30 °C
Suplied as a suspension in sodium acetate with 2.5 M NaCl, pH 4.0
Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Regulatory Information
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Adam Drzymała et al.
Acta biochimica et biophysica Sinica, 41(1), 69-78 (2009-01-09)
Carboxypeptidase III from germinating triticale grains was purified 434.2-fold with a six-step procedure including: homogenization, ammonium sulfate precipitation, cation-exchange chromatography on CM-cellulose, gel filtration chromatography on Sephadex G-150, cation-exchange chromatography on SP8HR column (HPLC), and affinity chromatography on CABSSepharose 4B.
Galyna Sidyelyeva et al.
The Journal of biological chemistry, 277(51), 49613-49620 (2002-10-24)
Metallocarboxypeptidase D (CPD), is a 180-kDa protein that contains three carboxypeptidase-like domains, a transmembrane domain, and a cytosolic tail and which functions in the processing of proteins that transit the secretory pathway. An initial report on the Drosophila melanogaster silver
Elena Kalinina et al.
Journal of cellular biochemistry, 99(3), 770-783 (2006-05-06)
Carboxypeptidase D (CPD) functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates examined as well as Drosophila. Several forms of CPD mRNA were previously found in Drosophila that resulted from differential splicing
K Brijs et al.
Journal of agricultural and food chemistry, 47(9), 3572-3578 (1999-12-20)
Endoproteolytic, exoproteolytic, carboxypeptidase, aminopeptidase, and N-alpha-benzoyl-arginine-p-nitroanilide hydrolyzing activities were detected in 0.05 M sodium acetate buffer (pH 5.0) extracts of whole meal of the rye (Secale cereale L.) varieties Amando, Halo, and Humbolt. The proteolytic enzymes of Humbolt, the variety
Fa-Yun Che et al.
Journal of mass spectrometry : JMS, 40(2), 227-237 (2005-02-12)
Cpe(fat/fat) mice have a point mutation in the coding region of the carboxypeptidase E gene that renders the enzyme inactive. As a result, these mice have reduced levels of several neuropeptides and greatly increased levels of the peptide processing intermediates
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