protein

BPHL Protein, Human (His)

HY-P76177

5 μg;10 μg;50 μg;100 μg

45;70;185;295 USD

BPHL Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg

45;70;185;295 USD

The BPHL protein is a serine hydrolase that catalyzes the hydrolytic activation of amino acid ester prodrugs, such as nucleoside analogs such as valacyclovir and valganciclovir. It converts valacyclovir to acyclovir via hydrolysis. BPHL Protein, Human (His) is the recombinant human-derived BPHL protein, expressed by E. coli , with N-His labeled tag. The total length of BPHL Protein, Human (His) is 254 a.a., with molecular weight of ~30 KDa.

Human

BPHL protein, a serine hydrolase, serves as a catalyst for the hydrolytic activation of amino acid ester prodrugs, exemplified by nucleoside analogs like valacyclovir and valganciclovir. Notably, it facilitates the conversion of valacyclovir to acyclovir through hydrolysis. Beyond its role in drug activation, BPHL is implicated in potential detoxification processes. As a specific alpha-amino acid ester hydrolase, it displays a preference for small, hydrophobic, and aromatic side chains, without imposing strict requirements on the leaving group, except for a preference toward a primary alcohol. Existing as a monomer, BPHL may also engage in the formation of homodimers.

Biphenyl hydrolase like; Bph-rp; VACVase; Valacyclovirase; MCNAA

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris-HCL, 300 mM NaCl, pH 7.4.

Room temperature in continental US; may vary elsewhere.