SULT1E1 Proteins, Antibodies, cDNA Clones, ELISA Kits Research Reagents

SULT1E1 (Sulfotransferase Family 1E Member 1) is a protein coding gene located on human chromosome 4q13.3. SULT1E1 is also known as EST, STE, EST-1 and ST1E1. The human SULT1E1 gene encodes a 35126 Da protein containing 294 amino acids. The SULT1E1 protein is biasedly expressed in small intestine, duodenum and other tissues. Among its related pathways are Photodynamic therapy-induced unfolded protein response and Estrogen metabolism. SULT1E1 is related to sulfotransferase activity and flavonol 3-sulfotransferase activity. SULT1B1 is an important paralog of SULT1E1 gene. SULT1E1 is associated with some diseases, including Endometrial Cancer and Skin Angiosarcoma.

SULT1E1 Protein (1)

    SULT1E1 Antibody (6)

      SULT1E1 ELISA キット(すぐに使用できます)& ELISA抗体ペアセット(すぐに使用できません)(1)

      SULT1E1 cDNA Clone (29)


      クローニングベクター cDNA 製品

      In lentiviral vector

      SULT1E1 qPCR Primer (1)

      SULT1E1 の背景知識

      Estrogen sulfotransferase, also known as Sulfotransferase, estrogen-preferring, Sulfotransferase 1E1, SULT1E1 and ST1E1, is a cytoplasm enzyme that belongs to the sulfotransferase 1 family. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. SULT1E1 may control the level of the estrogen receptor by sulfurylating free estradiol. SULT1E1 maximally sulfates beta-estradiol and estrone at concentrations of 2 nM. SULT1E1 also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, equalenin, diethylstilbesterol and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated. SULT1E1 is a key enzyme in estrogen homeostasis. It plays a central role in the prevention and development of human disease.

      SULT1E1 の参考文献

      • Bernier F, et al.,1994, J Biol Chem. 269 (45): 28200-5.
      • Strausberg RL, et al.,2003, Proc. Natl. Acad. Sci. 99 (26): 16899-903.
      • Cole,GB. et al., 2010, Proc Natl Acad Sci USA. 107 (14): 6222-7.

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