protein

CYBB/Nox2 Protein, Human (His)

HY-P72161

20 μg;50 μg

260;450 USD

CYBB/Nox2 Protein, Human (His)

proteins

E. coli

20 μg;50 μg

260;450 USD

The CYBB/Nox2 protein is an important membrane-bound oxidase in phagocytes and is critical for superoxide production. As the terminal element of the respiratory chain, it transfers a single electron from NADPH to molecular oxygen. CYBB/Nox2 Protein, Human (His) is the recombinant human-derived CYBB/Nox2 protein, expressed by E. coli , with N-6*His labeled tag. The total length of CYBB/Nox2 Protein, Human (His) is 288 a.a., with molecular weight of ~37.2 kDa.

Human

CYBB/Nox2 protein serves as a crucial component of the membrane-bound oxidase found in phagocytes, playing a pivotal role in the generation of superoxide. As the terminal element of a respiratory chain, it facilitates the transfer of single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Additionally, CYBB/Nox2 operates as a voltage-gated proton channel, orchestrating H(+) currents in resting phagocytes. Its involvement extends to the regulation of cellular pH, and notably, this function is modulated by zinc, which serves as a blocking agent for the channel. The multifaceted activities of CYBB/Nox2 underscore its significance in the intricate cellular processes associated with oxidative and protonic regulation within phagocytes.

AMCBX2; CGD; CGD91-phox; CY24B_HUMAN; CYBB; Cytochrome b 245; beta polypeptide; Cytochrome b558; beta chain; Cytochrome b558; subunit beta; Cytochrome b-245 heavy chain; Cytochrome b558 subunit beta; GP91 PHOX; gp91-1; gp91-phox; GP91PHOX; Heme-binding membrane glycoprotein gp91phox;

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

Lyophilized from a 0.2 μm solution of 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.