CA1 E.Coli
Carbonate dehydratase, CAN, ECK0125, JW0122, yadF, CA 1, CA I, CA1, CAI, Car 1, Car1, Carbonate dehydratase I, Carbonic anhydrase 1, Carbonic anhydrase B.
Greater than 95.0% as determined by SDS-PAGE.
Description
CA1 E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (1-220) and having a molecular mass of 27.0 kDa.
CA1 E.Coli is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Carbonic anhydrase (CA) is an enzyme that catalyzes the reversible hydration of carbon dioxide (CO2) to bicarbonate (HCO3-) and protons (H+). This enzyme plays a crucial role in maintaining acid-base balance in the blood and other tissues. CA contains a zinc ion (Zn) at its active site, which is essential for its catalytic activity. One of the primary functions of CA is to facilitate the transport of CO2 from tissues to the lungs for exhalation. CA works in conjunction with Carbonic Anhydrase I to carry out this process.
Recombinant CA1 from E. coli is a single, non-glycosylated polypeptide chain. It consists of 240 amino acids, with amino acids 1-220 representing the CA1 protein, and has a molecular weight of 27.0 kDa. The protein is expressed in E. coli and purified using proprietary chromatographic methods. A 20 amino acid His-Tag is fused to the N-terminus to aid in purification.
CA1 E.Coli protein is supplied at a concentration of 1mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 1mM DTT, and 10% glycerol.
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein such as HSA or BSA (0.1%) is advised for long-term storage. Avoid repeated freezing and thawing of the product.
The purity of the CA1 E.Coli protein is greater than 95%, as determined by SDS-PAGE analysis.
Carbonate dehydratase, CAN, ECK0125, JW0122, yadF, CA 1, CA I, CA1, CAI, Car 1, Car1, Carbonate dehydratase I, Carbonic anhydrase 1, Carbonic anhydrase B.
MGSSHHHHHH SSGLVPRGSH MKDIDTLISN NALWSKMLVE EDPGFFEKLA QAQKPRFLWI GCSDSRVPAE RLTGLEPGEL FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG CGGVQAAVEN PELGLINNWL LHIRDIWFKH SSLLGEMPQE RRLDTLCELN VMEQVYNLGH STIMQSAWKR GQKVTIHGWA YGIHDGLLRD LDVTATNRET LEQRYRHGIS NLKLKHANHK.
Product Science Overview
CAs are divided into several classes: α, β, γ, δ, ζ, η, θ, and ι. Each class has evolved to perform specific functions in different organisms. For instance, in Escherichia coli (E. coli), β-CA (CynT) catalyzes the hydration of CO₂ generated by cyanase, thus preventing final HCO₃⁻ depletion in bacteria resulting from degradation of cyanate and/or other metabolic processes .
Expressing recombinant proteins, including CAs, in E. coli is a common practice due to the bacterium’s well-understood genetics, rapid growth, and ability to express foreign proteins. However, the expression of CAs in E. coli can be challenging due to the possible formation of insoluble protein aggregates, or inclusion bodies. This makes the production of soluble and active CA protein a prerequisite for downstream applications .
The ability to express CAs in E. coli has significant industrial implications, particularly for carbon capture, utilization, and storage (CCUS) processes. Identifying efficient and robust CAs and expressing them in model host cells like E. coli enables more efficient engineering of these enzymes for industrial CO₂ capture .
Recent studies have focused on streamlining the heterologous expression of top CAs in E. coli. For example, researchers have used bioinformatic tools to predict the solubility of various CA candidates and have successfully expressed high-solubility CAs in E. coli, leading to significantly higher protein yields . This approach not only enhances the efficiency of CA production but also provides insights into the phylogenetic clustering patterns of CA solubility and production yields .
In conclusion, the recombinant expression of Carbonic Anhydrase-1 in E. coli represents a promising avenue for both scientific research and industrial applications. The advancements in bioinformatics and experimental validation have paved the way for more efficient and robust production of these essential enzymes.
