Background
Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Carboxypeptidase-B sequentially cleaves C terminal K and R residues. Recombinant rat Carboxypeptidase-B is a 35.1 kDa protein consisting of 307 amino acids.
Specifications
Additional Names
Cpb1
Tested Application
n/a
Disclaimer
This product is for research use only.
Purity
Greater than 95% by SDS-PAGE gel and HPLC analyses.
Storage
The lyophilized Carboxypeptidase-B recombinant protein is stable for at least 2 years from date of receipt at -20ËšC. Reconstituted Carboxypeptidase-B stable for at least 3 months when stored in working aliquots with a carrier protein at -20ËšC. As with any protein, exposing Carboxypeptidase-B recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.
Preparation
Carboxypeptidase-B sequentially cleaves C terminal K and R residues. Endotoxin level is less than 0.1 ng per μg of Carboxypeptidase-B (1EU/μg).
Reactivity
n/a
Source
E.coli
Location
ASGHSYTKYN NWETIEAWIQ QVATDNPDLV TQSVIGTTFE GRNMYVLKIG KTRPNKPAIF IDCGFHAREW ISPAFCQWFV REAVRTYNQE IHMKQLLDEL DFYVLPVVNI DGYVYTWTKD RMWRKTRSTM AGSSCLGVDP NRNFNAGWCE VGASRSPCSE TYCGPAPESE KETKALADFI RNNLSTIKAY LTIHSYSQMM LYPYSYDYKL PENYEELNAL VKGAAKELAT LHGTKYTYGP GATTIYPAAG GSDDWSYDQG IKYSFTFELR DTGFFGFLLP ESQIRQTCEE TMLAVKYIAN YVREHLY
Species Reactivity
n/a
