p67phox Protein, Human (sf9)

p67phox is central to activating NADPH oxidase, crucial for superoxide production. Forming a heterodimer with CYBA and CYBB, and interacting with NCF4 and NCF1, p67phox establishes vital connections within the complex. Its versatile associations include SYTL1, RAC1, NOXO1, S100A8, calprotectin (S100A8/9), and GBP7, highlighting its regulatory role. Enhanced interaction with CYBB in the presence of GBP7 underscores the dynamic nature of these protein-protein associations in orchestrating superoxide generation. p67phox Protein, Human (sf9) is the recombinant human-derived p67phox protein, expressed by Sf9 insect cells , with tag free. and with residual Gly-Pro in N-terminal (not related to functional changes) mutation. The total length of p67phox Protein, Human (sf9) is 526 a.a., with molecular weight of ~60 kDa.

The p67phox protein plays a pivotal role in the activation of the latent NADPH oxidase, a process essential for superoxide production. As a key component of the NADPH oxidase complex, it forms a heterodimer with the membrane proteins CYBA and CYBB, alongside the cytosolic subunits NCF1, NCF2, and NCF4. Notably, p67phox interacts with NCF4 and NCF1, establishing crucial connections within the complex through its C-terminal SH3 domain. Additionally, it engages with SYTL1 and RAC1 and may interact with NOXO1, highlighting its versatility in associating with regulatory elements. Further interactions with S100A8, calprotectin (S100A8/9), and GBP7 underscore the intricate network involved in the regulation of NADPH oxidase activity. The interaction with CYBB is enhanced in the presence of GBP7, emphasizing the dynamic nature of these protein-protein associations in orchestrating superoxide generation.

Human

Sf9 insect cells

Tag Free

P19878 (N-G&P, M1-V526)

4688  [NCBI]

Approximately 60 kDa

Greater than 85% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.