ALDH1A2 Protein, Human (P.pastoris, His)

The ALDH1A2 protein catalyzes the NAD-dependent oxidation of aldehyde substrates, including all-trans -retinal and all-trans 13,14-dihydroretinal. ALDH1A2 Protein, Human (P.pastoris, His) is the recombinant human-derived ALDH1A2 protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of ALDH1A2 Protein, Human (P.pastoris, His) is 518 a.a., with molecular weight of 58.7 kDa.

ALDH1A2 protein plays a pivotal role in the NAD-dependent oxidation of various aldehyde substrates, such as all-trans-retinal and all-trans-13,14-dihydroretinal, converting them into their corresponding carboxylic acids, namely all-trans-retinoate and all-trans-13,14-dihydroretinoate. This enzymatic activity is essential for retinoate signaling, a process critical for the transcriptional control of numerous genes and notably crucial for the initiation of meiosis in both male and female organisms. ALDH1A2 can recognize retinal as a substrate, whether in its free form or when bound to cellular retinol-binding protein. While displaying the capability to metabolize octanal and decanal, ALDH1A2 exhibits only minimal activity with benzaldehyde, acetaldehyde, and propanal. Interestingly, it completely lacks activity with citral.

Human

P. pastoris

N-6*His

O94788 (M1-S518)

8854  [NCBI]

MTSSKIEMPGEVKADPAALMASLHLLPSPTPNLEIKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKIPQKNS

58.7 kDa

Greater than 90 % as determined by SDS-PAGE.

<1 EU/μg, determined by LAL method.