ALDH1A1 Protein, Human (His)

ALDH1A1 Protein, Human (His) is a human recombinant ALDH1A1 with an N-terminal Met and His tag produced in E. coli. ALDH1A1 Protein, Human (His) contains 501 amino acids (1-501 a.a.).

Aldehyde Dehydrogenase 1-A1 (ALDH1A1) is part of the aldehyde dehydrogenases family. Human ALDH1A1 is a cytosolic homotetramer expressed in several tissues (skin, eyes, liver, kidney, testis and brain). ALDH1A1oxidizes a broad range of aliphatic and aromatic aldehydes including those formed endogenously such as retinalsand 3,4-dihydroxyphenylacetaldehyde (DOPAL), xenobiotics such as benzaldehyde or those produced during lipid peroxidation^[1].

Measured by its ability to produce NADH during the oxidation of propionaldehyde. The specific activity is 77.63 pmol/min/µg, as measured under the described condition.

Human

E. coli

N-6*His

P00352 (M1-S501)

216  [NCBI]

MSSSGTPDLPVLLTDLKIQYTKIFINNEWHDSVSGKKFPVFNPATEEELCQVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLIERDRLLLATMESMNGGKLYSNAYLNDLAGCIKTLRYCAGWADKIQGRTIPIDGNFFTYTRHEPIGVCGQIIPWNFPLVMLIWKIGPALSCGNTVVVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVLADADLDNAVEFAHHGVFYHQGQCCIAASRIFVEESIYDEFVRRSVERAKKYILGNPLTPGVTQGPQIDKEQYDKILDLIESGKKEGAKLECGGGPWGNKGYFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTFYGLSAGVFTKDIDKAITISSALQAGTVWVNCYGVVSAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTVKISQKNS

Approximately 57 kDa

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

Solution.

Supplied as a 0.2 μm filter solution of 20 mM Tris-HCl, 150 mM NaCl, 20% Glycerol, 1 mM DTT, pH 8.0 or 50 mM Tris-HCL, 300 mM NaCl, pH 7.4, 20% Glycerol, 1 mM Dithiothreitol.

<1 EU/μg, determined by LAL method.

Stored at -80°C for 1 year. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.

• [1]. Calleja LF, et al. Omeprazole as a potent activator of human cytosolic aldehyde dehydrogenase ALDH1A1. Biochim Biophys Acta Gen Subj. 2020 Jan;1864(1):129451.  [Content Brief]