SULT1A2 Protein, Human (His)

Sulfotransferase 1A2 (SULT1A2) is a phenol sulfotransferase with thermostable enzyme activity. SULT1A2 utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. SULT1A2 is also responsible for the sulfonation and activation of minoxidil. SULT1A2 induces the mutagenicity and carcinogenicity of certain substrates by influencing DNA adduct formation. SULT1A2 Protein, Human (His) is the recombinant human-derived SULT1A2 protein, expressed by E. coli , with N-6*His labeled tag. The total length of SULT1A2 Protein, Human (His) is 295 a.a., with molecular weight of ~33.0 kDa.

Sulfotransferase 1A2 (SULT1A2) is a phenol sulfotransferase with thermostable enzyme activity. SULT1A2 utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. SULT1A2 is also responsible for the sulfonation and activation of minoxidil. SULT1A2 induces the mutagenicity and carcinogenicity of substrates, including nitrotoluenes, 3‑nitrobenzanthrone, aristolochic acids, aromatic hydroxyl‑amine and polycyclic aromatic hydrocarbons by influencing DNA adduct formation and plays a role in the chemical carcinogenesis of these substrates if SULT1A2 is expressed as a functional protein^[1][2][3].

Human

E. coli

N-6*His

AAI13728.1 (M1-L295)

6799  [NCBI]

MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDMIYQGGDLEKCHRAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLDQKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFKEMKKNPMTNYTTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL

Approximately 33.0 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.