Lanosterol synthase/LSS, Human (P.pastoris, His)

LSS protein, a pivotal enzyme in cholesterol biosynthesis, catalyzes the cyclization of (S)-2,3 oxidosqualene into lanosterol, a crucial step in sterol nucleus formation. Beyond cholesterol biosynthesis, LSS may regulate lens protein aggregation, maintaining lens transparency. LSS's enzymatic action impacts fundamental and specialized cellular processes, underscoring its significance in diverse physiological contexts. Lanosterol synthase/LSS Protein, Human (P.pastoris, His) is the recombinant human-derived Lanosterol synthase/LSS protein, expressed by P. pastoris , with N-His labeled tag. The total length of Lanosterol synthase/LSS Protein, Human (P.pastoris, His) is 731 a.a., with molecular weight of ~86.0 kDa.

TEGTCLRRRG GPYKTEPATD LGRWRLNCER GRQTWTYLQD ERAGREQTGL EAYALGLDTK NYFKDLPKAH TAFEGALNGM TFYVGLQAED GHWTGDYGGP LFLLPGLLIT CHVARIPLPA GYREEIVRYL RSVQLPDGGW GLHIEDKSTV FGTALNYVSL RILGVGPDDP DLVRARNILH KKGGAVAIPS WGKFWLAVLN VYSWEGLNTL FPEMWLFPDW APAHPSTLWC HCRQVYLPMS YCYAVRLSAA EDPLVQSLRQ ELYVEDFASI DWLAQRNNVA PDELYTPHSW LLRVVYALLN LYEHHHSAHL RQRAVQKLYE HIVADDRFTK SISIGPISKT INMLVRWYVD GPASTAFQEH VSRIPDYLWM GLDGMKMQGT NGSQIWDTAF AIQALLEAGG HHRPEFSSCL QKAHEFLRLS QVPDNPPDYQ KYYRQMRKGG FSFSTLDCGW IVSDCTAEAL KAVLLLQEKC PHVTEHIPRE RLCDAVAVLL NMRNPDGGFA TYETKRGGHL LELLNPSEVF GDIMIDYTYV ECTSAVMQAL KYFHKRFPEH RAAEIRETLT QGLEFCRRQQ RADGSWEGSW GVCFTYGTWF GLEAFACMGQ TYRDGTACAE VSRACDFLLS RQMADGGWGE DFESCEERRY LQSAQSQIHN TCWAMMGLMA VRHPDIEAQE RGVRCLLEKQ LPNGDWPQEN IAGVFNKSCA ISYTSYRNIF PIWALGRFSQ LYPERALAGH P