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Hemoglobin Theta 1 consists of 142 amino acids and has a molecular mass of approximately 17.9 kDa . The recombinant form of this protein is often produced in E. coli and is fused to a His-tag at the N-terminus to facilitate purification . The protein’s structure allows it to bind oxygen with high affinity, which is essential for its role in oxygen transport.
Recombinant human HBQ1 is produced using conventional chromatography techniques. The protein is expressed in E. coli and purified to a high degree of purity, typically greater than 90% as determined by SDS-PAGE . The recombinant protein is often used in research to study hemoglobin function and structure.
Recombinant HBQ1 is used in various research applications, including studies on hemoglobin function, oxygen binding, and the effects of mutations on hemoglobin structure and function. It is also used in the development of therapeutic agents and in the study of hemoglobin-related diseases.