PHYH Protein, Human

PHYH protein catalyzes 2-hydroxylation of various mono-branched and straight-chain acyl-CoA esters, including racemic phytanoyl-CoA and isomers of 3-methylhexadecanoyl-CoA. It acts on acyl-CoAs with a chain length of at least seven carbon atoms, excluding long, very long straight-chain, and 2-methyl or 4-methyl-branched acyl-CoAs. PHYH Protein, Human is the recombinant human-derived PHYH protein, expressed by E. coli , with tag free. The total length of PHYH Protein, Human is 308 a.a., with molecular weight of 32 kDa.

PHYH protein plays a crucial role in cellular metabolism by catalyzing the 2-hydroxylation of various acyl-CoA esters, including racemic phytanoyl-CoA, isomers of 3-methylhexadecanoyl-CoA, and a diverse array of other mono-branched 3-methylacyl-CoA esters with a chain length of at least seven carbon atoms, as well as straight-chain acyl-CoA esters with a chain length longer than four carbon atoms. Notably, PHYH does not hydroxylate long and very long straight-chain acyl-CoAs or 2-methyl- and 4-methyl-branched acyl-CoAs, showcasing its substrate specificity. These enzymatic activities contribute to the regulation of lipid metabolism and cellular homeostasis, highlighting the importance of PHYH in maintaining metabolic balance.

Human

E. coli

Tag Free

O14832-1 (S31-L338)

5264  [NCBI]

SGTISSASFHPQQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL

Approximately 32 kDa

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

<1 EU/μg, determined by LAL method.