ectonucleoside triphosphate diphosphohydrolase 6 isoform 1, CD39L2, dJ738P15.3, IL-6SAG, IL6ST2, NTPDase-6.
Greater than 80.0% as determined by SDS-PAGE.
ENTPD6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447amino acids (61-484a.a.) and having a molecular mass of 48.7kDa.
ENTPD6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ectonucleoside triphosphate diphosphohydrolase 6 isoform 1, CD39L2, dJ738P15.3, IL-6SAG, IL6ST2, NTPDase-6.
MGSSHHHHHH SSGLVPRGSH MGSKWHRATA TQAFFSITRA APGARWGQQA HSPLGTAADG HEVFYGIMFD AGSTGTRVHV FQFTRPPRET PTLTHETFKA LKPGLSAYAD DVEKSAQGIR ELLDVAKQDI PFDFWKATPL VLKATAGLRL LPGEKAQKLL QKVKEVFKAS PFLVGDDCVS IMNGTDEGVS AWITINFLTG SLKTPGGSSV GMLDLGGGST QIAFLPRVEG TLQASPPGYL TALRMFNRTY KLYSYSYLGL GLMSARLAIL GGVEGQPAKD GKELVSPCLS PSFKGEWEHA EVTYRVSGQK AAASLHELCA ARVSEVLQNR VHRTEEVKHV DFYAFSYYYD LAAGVGLIDA EKGGSLVVGD FEIAAKYVCR TLETQPQSSP FSCMDLTYVS LLLQEFGFPR SKVLKLTRKI DNVETSWALG AIFHYIDSLN RQKSPAS
The ENTPD6 gene is located on chromosome 20 and encodes a protein that is part of the NTPDase family. This family is characterized by the presence of four apyrase-conserved regions (ACRs), which are essential for the enzyme’s catalytic activity . The protein is a membrane-bound enzyme that can also be released from cells to function extracellularly .
ENTPD6 catalyzes the hydrolysis of nucleoside triphosphates and diphosphates in a calcium- or magnesium-dependent manner. It has a strong preference for nucleoside diphosphates, such as GDP, IDP, and UDP, and shows slower hydrolysis rates for CDP, ITP, GTP, CTP, ADP, and UTP. Interestingly, it exhibits virtually no hydrolysis of ATP . The enzyme’s activity is crucial for regulating the levels of extracellular nucleotides, thereby modulating purinergic signaling pathways .
The recombinant form of ENTPD6 is produced using genetic engineering techniques. The gene encoding ENTPD6 is cloned into an expression vector, which is then introduced into a suitable host cell, such as Escherichia coli or mammalian cells. The host cells are cultured under conditions that promote the expression of the recombinant protein. After expression, the protein is purified using various chromatographic techniques to obtain a highly pure and active enzyme .
Recombinant ENTPD6 has several applications in research and medicine. It is used to study the mechanisms of purinergic signaling and its role in various physiological and pathological processes. Additionally, it serves as a tool for screening potential therapeutic agents that target purinergic signaling pathways. The enzyme’s ability to hydrolyze extracellular nucleotides makes it a potential candidate for therapeutic interventions in conditions characterized by dysregulated purinergic signaling, such as chronic inflammation and cancer .
ENTPD6 has been implicated in several diseases, including Gaucher Disease Type IIIC and Endometrial Transitional Cell Carcinoma . Its role in these diseases is linked to its function in regulating extracellular nucleotide levels and purinergic signaling. Understanding the enzyme’s activity and regulation can provide insights into the pathophysiology of these conditions and aid in the development of targeted therapies .