protein

CBR1 Protein, Human (P.pastoris, His)

HY-P72272

2 μg;10 μg;50 μg

35;78;220 USD

CBR1 Protein, Human (P.pastoris, His)

proteins

P. pastoris

2 μg;10 μg;50 μg

35;78;220 USD

CBR1 is an NADPH-dependent reductase with broad substrate specificity and plays a key role in the reduction of various carbonyl compounds, including quinones, prostaglandins, menadione, and xenobiotics. Crucially, CBR1 converts the anthracyclines doxorubicin and daunorubicin into their cardiotoxic forms doxorubicin and daunorubicin. CBR1 Protein, Human (P.pastoris, His) is the recombinant human-derived CBR1 protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of CBR1 Protein, Human (P.pastoris, His) is 276 a.a., with molecular weight of ~33.0 kDa.

Human

CBR1, an NADPH-dependent reductase, exhibits broad substrate specificity and plays a pivotal role in the reduction of diverse carbonyl compounds, encompassing quinones, prostaglandins, menadione, and various xenobiotics. Notably, CBR1 catalyzes the conversion of the antitumor anthracyclines doxorubicin and daunorubicin into their cardiotoxic counterparts, doxorubicinol and daunorubicinol. Moreover, it demonstrates the ability to transform prostaglandin E into prostaglandin F2-alpha, highlighting its versatility in substrate recognition. The enzyme's interaction with glutathione, evidenced by binding to glutathione-conjugated substrates, further elucidates its higher affinity for specific compounds. Additionally, CBR1 participates in glucocorticoid metabolism by facilitating the NADPH-dependent conversion of cortisol/corticosterone to 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b-DHB), both of which act as weak agonists for NR3C1 and NR3C2 in adipose tissue.

Carbonyl Reductase 1; SDR21C1

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from 0.2 μm filtered solution in 20 mM Tris-HC1, 0.5 M NaCl, 3% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.