10103233001
Roche
Carboxypeptidase B
from pig pancreas
form
solution
specific activity
~150 units/mg protein (at 25 °C with hippuryl-L-arginine as the substrate.)
shelf life
a decrease in activity of approximately 10% may occur within 6 months.
mol wt
Mr 34.6 kDa
packaging
pkg of 1 mL (5 mg)
manufacturer/tradename
Roche
storage condition
avoid repeated freeze/thaw cycles
optimum pH
7.0-9.0
General description
Peptidyl-L-lysine (-L-arginine) hydrolase. Carboxypeptidase B is secreted as a zymogen (pro-carboxypeptidase B) from the pancreas.
Application
Carboxypeptidase B has been used for the mass spectroscopy analysis ofanti-K11/K48 bispecific antibody.
Biochem/physiol Actions
Carboxypeptidase B is a Zn2+-metalloprotease, which catalyzes the hydrolysis of the basic amino acids L-Lys and L-Arg from the C-terminal position in polypeptides.
Preparation Note
Inhibitors: Chelating agents and basic amino acids
Store at -15–-25 °C. (Freeze only once in aliquots!)
Analysis Note
Contaminants: <5mU chymotrypsin/mg protein, < 0.007mU trypsin/mg, <2% carboxypeptidase A. Potential chymotrypsin and trypsin activities are eliminated by DFP treatment.
Other Notes
For life science research only. Not for use in diagnostic procedures.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
No data available
Flash Point(C)
No data available
Regulatory Information
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G A Scheele et al.
The Journal of biological chemistry, 250(7), 2660-2670 (1975-04-10)
An in vitro system of guinea pig pancreatic lobules convenient for the study of secretory processes is described in this paper. In this system: (a) the over-all glandular architecture of the tissue is preserved: lobules remain morphologically intact through 5
Louisette Basa
Methods in molecular biology (Clifton, N.J.), 1045, 285-293 (2013-08-06)
This chapter describes an LC-ESI-MS method for the DAR and drug load distribution analysis that is suitable for lysine-linked ADCs. The ADC sample is desalted using a reversed-phase LC column with an acetonitrile gradient prior to online MS analysis. The
Assembly and function of heterotypic ubiquitin chains in cell-cycle and protein quality control
Yau RG, et al.
Cell, 171(4), 918-933 (2017)
Christiane Jäger et al.
Methods in molecular biology (Clifton, N.J.), 901, 195-208 (2012-06-23)
Immunoglobulin (Ig) G is formed by two antigen-binding moieties termed Fabs and a conserved Fc -portion, which interacts with components of the immune systems. Within the Fc, N-linked carbohydrates are attached to each conserved asparagine residue at position 297 within
Zhilan Hu et al.
Biotechnology and bioengineering, 113(10), 2100-2106 (2016-03-19)
Heterogeneity of C-terminal lysine levels often observed in therapeutic monoclonal antibodies is believed to result from the proteolysis by endogenous carboxypeptidase(s) during cell culture production. Identifying the responsible carboxypeptidase(s) for C-terminal lysine cleavage in CHO cells would provide valuable insights
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