Recombinant Human PTPN6, N-His

Description of Recombinant Human PTPN6, N-His

The Structure of Recombinant Human PTPN6, N-His

Recombinant Human PTPN6, N-His is a protein that is produced through genetic engineering techniques. It is a variant of the human protein tyrosine phosphatase non-receptor type 6 (PTPN6), which is also known as SHP-1 (Src homology 2 domain-containing protein tyrosine phosphatase 1). PTPN6 is a key regulator of cell signaling and is involved in a variety of cellular processes such as cell growth, differentiation, and immune response.

The recombinant version of PTPN6, N-His contains a histidine tag at the N-terminus, which allows for easy purification and detection of the protein. The protein has a molecular weight of approximately 68 kDa and is composed of 595 amino acids. It has a conserved catalytic domain, which is responsible for its phosphatase activity, and two SH2 domains, which are involved in protein-protein interactions.

The Activity of this protein

The main function of PTPN6 is to dephosphorylate tyrosine residues on target proteins, thereby regulating their activity. This is achieved through the catalytic domain of the protein, which removes phosphate groups from tyrosine residues on target proteins. PTPN6 has been shown to have a wide range of substrates, including receptors, kinases, and adaptor proteins, making it a key regulator of various signaling pathways.

One of the most well-studied functions of PTPN6 is its role in immune response. It is expressed in immune cells such as T cells, B cells, and natural killer cells, and has been shown to regulate the activation and differentiation of these cells. PTPN6 is also involved in the regulation of cytokine signaling and has been linked to various autoimmune diseases and cancers.

Application of Recombinant Human PTPN6, N-His

The unique structure and activity of Recombinant Human PTPN6, N-His make it a valuable tool in both basic research and drug discovery. Its ability to specifically dephosphorylate tyrosine residues on target proteins allows for the study of various signaling pathways and the identification of potential drug targets.

In addition, PTPN6 has been identified as a potential drug target itself. Mutations in the PTPN6 gene have been linked to various diseases, and its dysregulation has been observed in many cancers. Therefore, the development of PTPN6 inhibitors or activators could have therapeutic potential for these conditions.

Recombinant Human PTPN6, N-His is also used in protein-protein interaction studies. Its SH2 domains allow for specific binding to phosphorylated proteins, making it a useful tool for studying protein complexes and signaling networks.

Furthermore, the histidine tag on PTPN6, N-His allows for easy purification and detection of the protein, making it a valuable tool for protein purification and analysis.

In conclusion, Recombinant Human PTPN6, N-His is a versatile protein with a unique structure and activity that makes it a valuable tool in scientific research. Its involvement in various cellular processes and potential as a drug target make it an important protein to study in the field of drug discovery.