PTPN6 is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling. Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported.
PTPN6 Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain containing 300 amino acids and having a molecular mass of 34.3 kDa. The protein coding region of the catalytic domain of PTPN6 (amino acids 243-541). The catalytic domain of PTPN6 was overexpressed as insoluble protein aggregates (inclusion bodies). The recombinant PTPN6 protein was purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. Additional amino acid(Met) is attached at N-terminus.
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