CA1 Human, Active
CA1, CA-I, CAB.
Greater than 95.0% as determined by SDS-PAGE.
Description
CA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (1-261) and having a molecular mass of 31.0 kDa.
CA1 Humanis 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 to bicarbonate and protons (CO2 + H2O ↔ HCO3- + H+). CA contains a zinc ion in its active site and plays a crucial role in maintaining acid-base balance in the bloodstream and various tissues. Additionally, CA facilitates the transport of CO2 to and from tissues.
Recombinant human carbonic anhydrase 1 (CA1) was expressed in E. coli. The non-glycosylated polypeptide chain comprises 281 amino acids (residues 1-261), resulting in a molecular weight of 31.0 kDa.
The N-terminus of human CA1 is fused to a 20 amino acid His-Tag. Purification is achieved through proprietary chromatographic methods.
CA1 Human protein is supplied at a concentration of 1 mg/ml in a buffer solution containing 20mM Tris-HCl (pH 8.0), 1mM DTT, and 10% glycerol.
The purity of the protein is greater than 95.0% as determined by SDS-PAGE analysis.
The specific activity of the enzyme is greater than 300 pmol/min/µg. This is measured as the amount of enzyme required to hydrolyze 1.0 pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 8.0 and 37°C.
CA1, CA-I, CAB.
MGSSHHHHHH SSGLVPRGSH MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ PLKGRTVRAS F.
Product Science Overview
Carbonic Anhydrase-1 (CA1) is a crucial enzyme in the human body, playing a significant role in various physiological processes. The recombinant form of this enzyme, particularly the bioactive version, has been extensively studied for its applications in research and medicine.
Carbonic Anhydrase-1 is a single polypeptide chain metalloenzyme with a molecular weight of approximately 29-31 kDa . It is primarily expressed in erythrocytes (red blood cells) and is one of the twelve active carbonic anhydrase isozymes found in humans . The recombinant form is typically produced in E. coli and is often tagged with a His-tag for purification purposes .
The primary function of CA1 is to catalyze the reversible hydration of carbon dioxide (CO₂) to bicarbonate (HCO₃⁻) and protons (H⁺) . This reaction is vital for maintaining acid-base balance in blood and tissues. Additionally, CA1 plays a role in respiration by facilitating the transfer of CO₂ from tissues to the lungs .
Recombinant CA1 is widely used in biochemical and physiological research. Its ability to catalyze the hydration of CO₂ makes it a valuable tool for studying respiratory physiology, acid-base homeostasis, and various metabolic processes . The bioactive form of recombinant CA1 is particularly useful in assays and experiments that require high enzyme activity and stability .
Mutations or deficiencies in CA1 can lead to various medical conditions, although such cases are rare . The enzyme’s role in maintaining acid-base balance and facilitating CO₂ transport makes it a potential target for therapeutic interventions in conditions related to respiratory and metabolic dysfunctions.
