Recombinant Human LEPR/CD295 protein (His tag)

A DNA sequence encoding the Human Ob-R protein (P48357) (Phe 22-Val 333) was expressed with a N-His tag.

The Recombinant Human LEPR/CD295 Protein (HIS TAG) is a highly purified and bioactive protein that has been produced using advanced recombinant DNA technology. This protein is designed to be used in various research applications, including but not limited to, the study of leptin receptor signaling pathways and the investigation of its role in various physiological and pathological processes.

The Recombinant Human LEPR/CD295 Protein (HIS TAG) is expressed in a mammalian cell expression system, ensuring its proper folding and post-translational modifications, which are crucial for its biological activity. The protein is then purified using a combination of chromatographic techniques, resulting in a highly pure and active protein product.

This protein is tagged with a histidine (HIS) tag, which allows for easy purification and detection using affinity chromatography and Western blotting techniques. The HIS tag does not interfere with the biological activity of the protein and can be easily removed if desired.

The Recombinant Human LEPR/CD295 Protein (HIS TAG) is provided as a lyophilized powder, which ensures its stability and long shelf life. It is recommended to reconstitute the protein in sterile water or aqueous buffer before use. The concentration of the protein can be adjusted according to the specific experimental requirements.

This product is intended for research use only and is not intended for diagnostic or therapeutic purposes. It is supplied for use by qualified personnel who are experienced in handling and working with recombinant proteins. Proper laboratory safety precautions should be followed when handling this protein.

In summary, the Recombinant Human LEPR/CD295 Protein (HIS TAG) is a highly pure and bioactive protein that is ideal for studying leptin receptor signaling pathways and its involvement in various physiological and pathological processes. Its advanced production technology, proper folding, and post-translational modifications ensure its biological activity and reliability in research applications.