|Related Categories||3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Carboxypeptidase W,|
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One unit will hydrolyze 1.0 μmole of N-CBZ-
Suplied as a suspension in sodium acetate with 2.5 M NaCl, pH 4.0
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.
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(Type II-PMSF treated), ≥50 units/mg protein, aqueous suspension
lyophilized powder, ≥3 units/mg protein
lyophilized powder, ≥50 units/mg protein
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Keywords: Cell culture, Cell disruption, Cell signaling, Diagnostic, Digestions, Drug discovery, Functional genomics, Gene expression, Genomics, Metabolic Pathways, Molecular biology, Neuroscience, Proteomics
Structure determination of the human protective protein: twofold averaging reveals the three-dimensional structure of a domain which was entirely absent in the initial model. Rudenko, G., et al. Acta Crystallogr. D, Biol. Crystallogr. 52, 923-36, (1996)
Immunohistochemical localization and comparison of carboxypeptidases D, E, and Z, alpha-MSH, ACTH, and MIB-1 between human anterior and corticotroph cell "basophil invasion" of the posterior pituitary. Fan X, Olson SJ, and Johnson MD J. Histochem. Cytochem. 49(6), 783-90, (2001)
A short sequence within domain C of duck carboxypeptidase D is critical for duck hepatitis B virus binding and determines host specificity. Spangenberg HC, Lee HB, Li J, et al. J. Virol. 75(22), 10630-42, (2001)
Relative quantitation of peptides in wild-type and Cpe(fat/fat) mouse pituitary using stable isotopic tags and mass spectrometry. Che FY, Biswas R, and Fricker LD J. Mass Spectrom. 40(2), 227-37, (2005)
Septal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment. Potluri L, Karczmarek A, Verheul J, et al. Mol. Microbiol. 77(2), 300-23, (2010)
Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and alpha-factor precursor processing. Dmochowska A, Dignard D, Henning D, et al. Cell 50(4), 573-84, (1987)
End-binding proteins and Ase1/PRC1 define local functionality of structurally distinct parts of the microtubule cytoskeleton. Duellberg C, Fourniol FJ, Maurer SP, et al. Trends Cell Biol. 23(2), 54-63, (2013)
Serine-type carboxypeptidase KexA of Aspergillus oryzae has broader substrate specificity than Saccharomyces cerevisiae Kex1 and is required for normal hyphal growth and conidiation. Morita H, Tomita S, Maeda H, et al. Appl. Environ. Microbiol. 78(22), 8154-7, (2012)
Gene cloning, molecular modeling, and phylogenetics of serine protease P32 and serine carboxypeptidase SCP1 from nematophagous fungi Pochonia rubescens and Pochonia chlamydosporia. Larriba E, Martín-Nieto J, and Lopez-Llorca LV Can. J. Microbiol. 58(7), 815-27, (2012)
Reaction pathway and free energy profile determined for specific recognition of oligosaccharide moiety of carboxypeptidase Y. Senkara-Barwijuk E, Kobiela T, Lebed K, et al. Biosens. Bioelectron. 36(1), 103-9, (2012)
Nitrogen source and growth stage of Candida albicans influence expression level of vacuolar aspartic protease Apr1p and carboxypeptidase Cpy1p. Bauerová V, Pichová I, and Hrušková-Heidingsfeldová O Can. J. Microbiol. 58(5), 678-81, (2012)
Structure and function of a serine carboxypeptidase adapted for degradation of the protein synthesis antibiotic microcin C7. Agarwal V, Tikhonov A, Metlitskaya A, et al. Proc. Natl. Acad. Sci. U. S. A. 109(12), 4425-30, (2012)
Simultaneous screening of multiple mutations by invader assay improves molecular diagnosis of hereditary hearing loss: a multicenter study. Usami S, Nishio SY, Nagano M, et al. PLoS ONE 7(2), e31276, (2012)
Identification of interaction site of propeptide toward mature carboxypeptidase Y (mCPY) based on the similarity between propeptide and CPY inhibitor (IC). Nagayama M, Kuroda K, and Ueda M Biosci. Biotechnol. Biochem. 76(1), 153-6, (2012)
Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates. Grubb S, Guo L, Fisher EA, et al. Mol. Biol. Cell 23(4), 520-32, (2012)
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