Recombinant Carboxypeptidase B
$190.00 - $695.00
All products have special prices for bulk purchase, please contact for more details if required.
Cat. No.: RCB-1 (for 1mg)
Cat. No.: RCB-10 (for 10mg)
Description
Recombinant Carboxypeptidase B is a zinc-dependent metalloprotease that catalyzes the hydrolysis of basic amino acids L-Lysine and L-Arginine from the C-terminal position in peptides. It has a molecular weight of 33.8 kDa, an isoelectric point of 6.0, and optimum pH range of 7.5-9.0. The activity of Carboxypeptidase B is competitively inhibited by arginine and lysine, and its enzymatic activity is inhibited by metal ion chelators such as EDTA.
Our recombinant Carboxypeptidase B is produced by expression in Escherichia coli. Its amino acid sequence is identical to that of rat pancreatic Carboxypeptidase B, exhibiting the same enzymatic properties as animal-sourced Carboxypeptidase B. It can be used as a substitute for animal-derived Carboxypeptidase B in various biotechnological processes.
Applications
- Production of recombinant insulin and its analogues
- Determination of protein C-terminal amino acids
- Production of other recombinant peptide substances
- Enzymatic synthesis of certain specific compounds
Physical Appearance
White, off-white, or light yellow powder
Biological Activity
≥170 units/mg pro.
Unit Definition
One unit of enzyme activity catalyzes the hydrolysis of 1 μmol of carbobenzoxy-L-arginine per minute at pH 7.6 and 25°C.
Purity
Single major band
Formulation
The protein is lyophilized with 100mM NaCl, mannitol, and 20mM Tris at pH 7.5.
Recommended Usage
Dissolve the recombinant Carboxypeptidase B in sterile water or 25mM Tris-HCl (pH 7.6) to achieve an enzyme concentration of 1-10 mg/ml. Enzyme-to-substrate ratio: Target protein (w:w) = 1:50-1:1000. Optimum pH range: 7.5-9.0.
Stability
The lyophilized recombinant Carboxypeptidase B is stable for 24 months when stored at 2-8°C. After dissolution in sterile water or 25mM Tris-HCl (pH 7.6), it can be stored at -20°C without any loss of activity even after 10 freeze-thaw cycles.
Amino Acid Sequence
The provided amino acid sequence is for reference only, and the actual length or sequence of amino acids may vary to some extent.
Advantages
- Non-animal sourced: Recombinant production without exogenous viral contamination and no use of animal-derived raw materials in the production process.
- Stable quality: Batch production ensures consistent and stable production across different batches without variations in quality.
- High purity: High specific activity with host protein residuals below the limit required for biological products.
- Lyophilized powder: Easy storage and transportation.
Storage
Store at 4°C or below for a shelf life of two years. Since each freeze-thaw cycle can cause partial inactivation of the protein, after the initial preparation of the corresponding concentration, it is recommended to aliquot and store at -20°C or below to avoid repeated freeze-thaw cycles.
Precautions
- This product is intended for scientific research use by professionals only. It should not be used for clinical diagnosis or treatment, nor for food or drug purposes. It should not be stored in a regular residential setting.
- For your safety and health, please wear laboratory attire and disposable gloves when handling.
Only for research and not intended for treatment of humans or animals
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