Analytical Data
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Gene name
NOX4
- Application
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Alternative Names
NOX4；RENOX；NADPH oxidase 4
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NPH5
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Expression Region
1-578aa
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AA Sequence
MAVSWRSWLANEGVKHLCLFIWLSMNVLLFWKTFLLYNQGPEYHYLHQMLGLGLCLSRASASVLNLNCSLILLPMCRTLLAYLRGSQKVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVNYSEDFVELNAARYRDEDPRKLLFTTVPGLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSGGLLKYQTNLDTHPPGCISLNRTSSQNISLPEYFSEHFHEPFPEGFSKPAEFTQHKFVKICMEEPRFQANFPQTWLWISGPLCLYCAERLYRYIRSNKPVTIISVMSHPSDVMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLLPPSSQDSEILPFIQSRNYPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCMLHNKFWQENRPDYVNIQLYLSQTDGIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLSNQNNSYGTRFEYNKESFS
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
NADPH oxidase 4 (NOX4) is a member of the NOX family of enzymes, known for its role in generating reactive oxygen species (ROS) within cells. It has garnered significant attention in recent years due to its involvement in various physiological and pathological processes, including cellular signaling, inflammation, and tissue fibrosis. The prevalent expression of NOX4 in multiple tissues, including the heart, kidneys, and lungs, has implicated it in the progression of cardiovascular diseases, chronic kidney disease, and pulmonary disorders. Recent studies indicate that dysregulation of NOX4 activity can lead to oxidative stress, a condition linked to numerous diseases. As a result, NOX4 has emerged as a potential therapeutic target, sparking interest in the development of NOX4 recombinant proteins for research and clinical applications. The generation of these recombinant proteins allows for a deeper understanding of NOX4’s functional mechanisms, interactions with other cellular pathways, and its role in disease progression. The ongoing research on NOX4 recombinant proteins aims to elucidate its contributions to oxidative stress-related diseases and to explore potential strategies for modulating its activity for therapeutic benefits. By providing a platform to investigate the biochemical properties of NOX4, these studies may pave the way for novel interventions that can mitigate the detrimental effects of oxidative stress and improve patient outcomes in various conditions associated with NOX4 dysregulation.
