Recombinant Human Nadph Oxidase 4 (NOX4) Protein (His)

Name: Recombinant Human Nadph Oxidase 4 (NOX4) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02212P
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Nadph Oxidase 4 (NOX4) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9NPH5
Target Symbol	NOX4
Synonyms	NOX4; RENOX; NADPH oxidase 4; Kidney oxidase-1; KOX-1; Kidney superoxide-producing NADPH oxidase; Renal NAD(PH-oxidase
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GGLLKYQTNLDTHPPGCISLNRTSSQNISLPEYFSEHFHEPFPEGFSKPAEFTQHKFVKICMEEPRFQANFPQTWLWISGPLCLYCAERLYRYIRSNKPVTIISVMSHPSDVMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLLPPSSQDSEILPFIQSRNYPKLYIDGPFGSPFEESLNYE
Expression Range	210-424aa
Protein Length	Partial
Mol. Weight	28.8 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Constitutive NADPH oxidase which generates superoxide intracellularly upon formation of a complex with CYBA/p22phox. Regulates signaling cascades probably through phosphatases inhibition. May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate insulin signaling cascade. May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB. May produce superoxide in the nucleus and play a role in regulating gene expression upon cell stimulation. Isoform 3 is not functional. Isoform 5 and isoform 6 display reduced activity.; Involved in redox signaling in vascular cells. Constitutively and NADPH-dependently generates reactive oxygen species (ROS). Modulates the nuclear activation of ERK1/2 and the ELK1 transcription factor, and is capable of inducing nuclear DNA damage. Displays an increased activity relative to isoform 1.
Subcellular Location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Cell junction, focal adhesion. Note=May localize to plasma membrane and focal adhesions. According to PubMed:15927447, may also localize to the nucleus.; [Isoform 4]: Nucleus. Nucleus, nucleolus.
Database References	HGNC: 7891 OMIM: 605261 KEGG: hsa:50507 STRING: 9606.ENSP00000263317 UniGene: PMID: 30087027 This genome-wide association study of severe diabetic retinopathy suggests new evidence for the involvement of the NOX4 gene. PMID: 30178632 These results suggest the specific involvement of Nox4 and Nox2 subunits as physiologically relevant endothelial sources of H2O2 generation that contribute to the endothelium-dependent vasodilatation of renal arteries and therefore have a protective role in kidney vasculature. PMID: 30125808 NOX4 is induced in early alcoholic liver injury and regulates CCR2/CCL2 mRNA stability thereby promoting recruitment of inflammatory cells and production of proinflammatory cytokines. PMID: 28383062 Study reveals the novel function of NOX4 in reprogramming aerobic glycolysis initiated by activated Kras and inactivated p16 in pancreatic ductal adenocarcinoma (PDAC), indicating its potential as a therapeutic target for PDAC and other cancers. PMID: 28232723 Human post-mortem and animal studies have identified elevated NOX2 and NOX4 levels in the injured brain, suggesting that these two NOXs are involved in the pathogenesis of Traumatic brain injury (TBI) PMID: 29571125 our data demonstrate that hypoxia strongly potentiates the peroxide-mediated induction of hepcidin via STAT3 signaling pathway. Moreover, oxidases such as NOX4 or artificially overexpressed urate oxidase (UOX) can induce hepcidin PMID: 29459227 Nox4 and its linked ER stress were shown to mainly contribute to eNOS uncoupling and its associated signaling in endothelial cells PMID: 28916474 Our data suggest that TGF-beta1-induced chemokinesis in PDAC cells is mediated through a RAC1/NOX4/ROS/p38 MAPK cascade. PMID: 29039574 GATA4 may inhibit diabetesinduced endothelial dysfunction by acting as a transcription factor for NOX4 expression. PMID: 29138836 The results demonstrate that the heightened sensitivity of the brain to ischemic damage is due to an organ-specific role of NOX4 in blood-brain barrier endothelial cells and neurons. PMID: 29087944 PTEN inhibits replicative senescence-induced MMP-1 expression by regulating NOX4-mediated reactive oxygen species in human dermal fibroblasts. PMID: 28557373 The NADPH-dependent reduction of cytochrome c or cytochrome b5 by purified Nox4 DH domain was found regulated by the H2O2 concentration, and C546L and C547L mutants showed lower rates of the hemeprotein reduction. PMID: 29365138 We demonstrated that small interfering RNA (siRNA)-mediated knockdown of PRR, Nox2 and Nox4 significantly reduced the HG-induced stimulation of VEGF. On the other hand, Nox4 overexpression significantly potentiated PRR-induced stimulation of VEGF under hyperglycemia in ARPE-19 cells. PMID: 28840773 Studies indicate that NADPH oxidase 4 (Nox4) is present in fibroblasts, a primary cell of the adventitia, and matches the adventitial location of ROS production in pulmonary arterial hypertension [Review]. PMID: 29047077 Serum Gal-3 and Nox4 levels were significantly elevated and correlated in 26 human pulmonary arterial hypertension patients when compared with 14 age- and sex-matched healthy controls. PMID: 28431936 we demonstrated that when NOX4 expression was knocked down by siRNAs, cell proliferation, cell-cycle and apoptosis, migration and invasion were significantly altered in CRC cell lines HCT116 and LOVO. Meanwhile, NOX4 promoted cancer cell proliferation and apoptosis, migration and invasion by regulating the expression of relevant genes. PMID: 28422720 Nox4 not only mediated TGF-beta1- induced collagen type I synthesis but also the expression of the myofibroblast markers alpha-SMA and fibronectin 1. PMID: 27576129 High NOX4 expression is associated with drug resistance in renal cell carcinoma. PMID: 29051480 Nox4 potentially mediates HGinduced HKC cell apoptosis. PMID: 28487945 Our results showed that lowering NOX4 oxidase below physiological level leads to cellular senescence of vascular smooth muscle cells PMID: 27655718 Extracellular advanced oxidative protein products accumulation triggered NOX4-dependent reactive oxygen species production, which activated ERK1/2 and p38 MAPK, and induced HaCaT cell apoptosis by activating caspase 3 and PARP-1. PMID: 27155970 The results establish a link between BRAF(V600E) and NOX4, which is confirmed by a comparative analysis of NOX4 expression in human (TCGA) and mouse thyroid cancers. PMID: 27401113 This study also showed that UCH-L1 promotes angiogenesis of HUVECs, as well as invasion in cancer cells, by up-regulating ROS by deubiquitination of NOX4, suggesting that UCH-L1 plays a key role in angiogenesis of HUVECS by regulating ROS levels by deubiquitination of NOX4. PMID: 29128359 The results reveal that NOX4 promotes glycolysis, contributing to non-small cell lung cancer cells growth, and supports glutaminolysis for oxidative resistance. PMID: 27989748 Metformin attenuates idiopathic lung fibrosis development via suppression of myofibroblast NOX4 expression. PMID: 27576730 Letter: airway smooth muscle cell NOX4 expression is increased in vivo and in vitro in COPD. PMID: 27435477 These data suggested that t-BHP induced both apoptosis and necroptosis in endothelial cells which was mediated by ROS and p38MAPK. ROS derived from NADPH oxidase and mitochondria contributed to t-BHPL and t-BHPH-induced apoptosis and necroptosis, respectively PMID: 28088644 These processes are mediated upstream by the reactive oxygen species (ROS)-producing enzyme Nox4. PMID: 28182006 data suggest that monocytic Nox4 is a central regulator of actin dynamics, and induction of Nox4 is the rate-limiting step in metabolic stress-induced monocyte priming and dysfunction associated with accelerated atherosclerosis and the progression of atherosclerotic plaques PMID: 23825596 findings demonstrate that manipulation of the host PI3K/Akt signaling pathway and Nox4 gene expression is a novel mechanism involved in T. gondii survival and proliferation PMID: 23824914 Loss of NOX4 increases actomyosin levels and favours an epithelial to amoeboid transition contributing to tumour aggressiveness. PMID: 27941881 NOX2, NOX4, and mitochondrial-derived reactive oxygen species contribute to angiopoietin-1 signaling and angiogenic responses in endothelial cells. PMID: 28351775 Mechanistically, HO-1 induction by all CRLPs requires NADPH oxidase 4, with PUFA-containing particles additionally dependent upon mitochondrial reactive oxygen species.These studies define new molecular pathways coupling endothelial cell activation by model CMRs with adaptive regulation of Nrf2-dependent HO-1 expression PMID: 27185859 NOX4 knockout cell lines showed reduced cell proliferation with an increase of sub-G1 cell population and the decrease of S/G2/M population, and resulted in a dramatic decrease in invadopodium formation and the invasive activity. NOX4 deficiency caused a decrease in focal adhesions and cell migration in HeLa cells. The results suggest that NOX4 is required for both efficient proliferation and invasion of HeLa cells. PMID: 28099519 Thioredoxin attenuates oxidized low-density lipoprotein induced oxidative stress in human umbilical vein endothelial cells by reducing NOX2-NOX4 activity. PMID: 28688762 Nox4-derived H2O2 in part activates Nox2 to increase mitochondrial ROS via pSer36-p66Shc, thereby enhancing VEGFR2 signaling and angiogenesis in endothelial cells. PMID: 28424170 TGF-beta1 increases NADPH oxidase 4 (NOX4) mRNA and protein expression in normal human lung fibroblasts (NHLFs) and causes nuclear export of HDAC4. PMID: 28336812 Nox4 should contribute to the pathological processes insubarachnoid hemorrhage(SAH)-induced early brain injury (EBI), and there was not an overlay effect of Nox2 inhibition and Nox4 inhibition on preventing SAH-induced EBI. PMID: 28330417 TGFbeta1 was found to induce Nox4 mRNA expression and total collagen release by these cells (P < 0.05; n = 4), and both responses are blocked by Smad3 inhibitor SIS3. Suppressing Nox4 gene transcription with Adv-Nox4i completely attenuated TGFbeta1-stimulated H2O2 release and collagen production by conjunctival fibroblasts PMID: 28605812 CD44V6 is part of a positive-feedback loop with TGFbeta1/TGFbetaRI signaling that acts to increase NOX4/ROS production, which is required for myofibroblast differentiation, myofibroblast differentiation, myofibroblast extracellular matrix production, myofibroblast invasion, and myofibroblast contractility. PMID: 28389561 Endoplasmic reticulum stress triggers a localized signaling module on the ER surface involving Nox4-dependent calcium mobilization, which directs local Ras activation through ER-associated, calcium-responsive RasGRF. PMID: 27856453 PI3K/AKT signaling only occurs when FLT3-ITD is expressed at the plasma membrane and is required for the production of NOX-generated ROS. ER retention of FLT3-ITD resulted in NOX4 deglycosylation and p22(phox) protein degradation. PMID: 27870947 NOX4 upregulation confers anoikis resistance. PMID: 28081539 these data demonstrate that increased expression and activation of NOX4, which might result from increased TGFbeta1 levels seen during aging, induces a proinflammatory phenotype in VSMCs, enhancing atherosclerosis. PMID: 27986445 The ROS levels of the study group decreased obviously before irradiation (P<0.01), however, the radiation-induced ROS of the study group was at a high level even when irradiation had been terminated for 2 h (P<0.01). Moreover, NOX2 and NOX4 levels and total SOD activity decreased (P<0.01), while the levels of SOD1 were stably maintained (P>0.05). PMID: 28260074 alkali burns markedly upregulated the transcription and expression of Nox2 and Nox4 in human or mouse corneas. PMID: 27221536 The NOX4 and TLR2 pathways played important roles in the biological effects mediated by Bletilla striata polysaccharide b. PMID: 27151672 it was demonstrated that elevated uric acid promoted ROSinduced tubular cell apoptosis by upregulating Nox4 expression. PMID: 27052425 expression of MATER and NOX4 proteins are closely related to the follicular development and ovulation with particular regard for ovarian aging PMID: 27515505

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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