NOX4 Protein, Human (His)

When NOX4 protein complexes with CYBA/p22phox, superoxide is generated in cells. It regulates signaling cascades and inhibits phosphatases. NOX4 Protein, Human (His) is the recombinant human-derived NOX4, expressed by E. coli Cell-free , with N-10*His labeled tag. ,

NOX4 protein is a constitutive NADPH oxidase that generates superoxide within cells when it forms a complex with CYBA/p22phox. It is involved in regulating signaling cascades, potentially through inhibiting phosphatases. NOX4 may act as an oxygen sensor, influencing the activity of the KCNK3/TASK-1 potassium channel and HIF1A. It may also play a role in regulating insulin signaling, apoptosis, bone resorption, and lipolysaccharide-induced activation of NFKB. Additionally, NOX4 might produce superoxide in the nucleus, contributing to the regulation of gene expression following cell stimulation. Notably, isoform 3 is non-functional, while isoform 5 and isoform 6 exhibit reduced activity. NOX4 is implicated in redox signaling in vascular cells, generating reactive oxygen species (ROS) constitutively and NADPH-dependently. It modulates the activation of ERK1/2 and the ELK1 transcription factor in the nucleus and can induce nuclear DNA damage. Isoform 4, compared to isoform 1, demonstrates increased activity.

Human

E. coli Cell-free

N-10*His

Q9NPH5-1 (M1-S578)

50507

MAVSWRSWLANEGVKHLCLFIWLSMNVLLFWKTFLLYNQGPEYHYLHQMLGLGLCLSRASASVLNLNCSLILLPMCRTLLAYLRGSQKVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVNYSEDFVELNAARYRDEDPRKLLFTTVPGLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSGGLLKYQTNLDTHPPGCISLNRTSSQNISLPEYFSEHFHEPFPEGFSKPAEFTQHKFVKICMEEPRFQANFPQTWLWISGPLCLYCAERLYRYIRSNKPVTIISVMSHPSDVMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLLPPSSQDSEILPFIQSRNYPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCMLHNKFWQENRPDYVNIQLYLSQTDGIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLSNQNNSYGTRFEYNKESFS

Approximately 66 kDa

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

<1 EU/μg, determined by LAL method.