A DNA sequence encoding the human CHT protein (P32929) (Met 1-Ser 405) was expressed with a His tag at the C-terminus.
Accession
P32929
Protein construction
CHT (1-405)His
Source
E.coli
Bio Activity
Testing in progress.
Purity
>95% as determined by SDS-PAGE.
Endotoxin
Less than 1.0 EU per μg by the LAL method.
Formulation
Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4, 5% Trehalose, 5% mannitol.
Species
Human
Background
Catalyzes the last step in the trans-sulfuration pathway from L-methionine to L-cysteine in a pyridoxal-5'-phosphate (PLP)-dependent manner, which consists on cleaving the L,L-cystathionine molecule into L-cysteine, ammonia and 2-oxobutanoate. Part of the L-cysteine derived from the trans-sulfuration pathway is utilized for biosynthesis of the ubiquitous antioxidant glutathione. Besides its role in the conversion of L-cystathionine into L-cysteine, it utilizes L-cysteine and L-homocysteine as substrates (at much lower rates than L,L-cystathionine) to produce the endogenous gaseous signaling molecule hydrogen sulfide (H2S). In vitro, it converts two L-cysteine molecules into lanthionine and H2S, also two L-homocysteine molecules to homolanthionine and H2S, which can be particularly relevant under conditions of severe hyperhomocysteinemia (which is a risk factor for cardiovascular disease, diabetes, and Alzheimer's disease).
Usage guide
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped with blue ice. Bulk packages of recombinant proteins are provided as frozen liquid which are shipped with dry ice.
Storage
Please avoid repeated freeze-thaw cycles. Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃ It is recommended that aliquot the reconstituted solution to minimize freeze-thaw cycles.