Recombinant Human HO-1 Protein

Name: Recombinant Human HO-1 Protein
Brand: Beta LifeScience
SKU: BL-2040NP
Availability: InStock

BL-2040NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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

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Product Overview

Description	Recombinant Human Heme Oxygenase 1 is produced by our E.coli expression system and the target gene encoding Met1-Thr261 is expressed.
Accession	P09601
Synonym	Heme Oxygenase 1; HO-1; HMOX1; HO; HO1
Gene Background	Heme Oxygenase 1 (HO-1) is an enzyme in endoplasmic reticulum that belongs to the heme oxygenase family. HO-1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is subsequently converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HO-1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. HO-1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA. HO-1 is involved in the regulation of cardiovascular function and response to a variety of stressors. Defects in HO-1 are the cause of Heme Oxygenase 1 deficiency, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues.
Molecular Mass	29.86 KDa
Apmol Mass	30 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 1mM EDTA, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Subcellular Location	Microsome. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Protein Families	Heme oxygenase family
Database References	HGNC: 5013 OMIM: 141250 KEGG: hsa:3162 STRING: 9606.ENSP00000216117 UniGene: PMID: 30159103 HO-1 is over-expressed in sera of psoriasis patients and is correlated with psoriasis extent and severity. PMID: 30105448 Pregnant women who subsequently develop severe preeclampsia show higher expression of HO-1. PMID: 30363976 Our findings identify survivin as a target of HO-1 and a mediator of adipocyte-induced survival in the metastatic niche. PMID: 29311669 the role of HO-1 in nervous system pointing out different molecular mechanisms possibly responsible for HO-1 up-regulation in nervous system homeostasis and neurodegeneration. PMID: 30071692 HO-1 may serve as a prognostic marker and a new target to modulate chemotherapeutic effects in patients with small-intestinal adenocarcinomas PMID: 29537718 The T allele of heme oxygenase 1 gene SNP polymorphism (rs2071746) is a risk factor for esophageal varices development in cirrhotics. PMID: 29877949 Data show that the ferroptotic process induced by heme oxygenase-1 (HO-1). overexpression indicated that HO-1 is a key mediator of BAY 11-7085 (BAY)-induced ferroptosis that operates through cellular redox regulation and iron accumulation. PMID: 29274359 Heme oxygenase activity increases after exercise in healthy volunteers. PMID: 29343136 Results show that HO-1 is overexpressed in pancreatic cancer (PC) cells, induces cell proliferation and SHH signaling pathway activation as well as resistance to anticancer therapy. PMID: 29620188 the expression of hsa_circRNA0054633 has a protective effect against high glucoseinduced endothelial cell dysfunction by targeting ROBO1 and HO1. PMID: 29693114 the 14 kDa HO-1 is shown to promote cell proliferation and an increase in relative telomere lengths in vivo and in vitro. PMID: 29660345 HO-1 plays a key role in protecting tumor cells from apoptosis, in a process that involves Smad7 and HDAC4/5 in apoptosis of B-ALL cells PMID: 29886060 HO-1 might be a potential marker for prediction of ovarian cancer prognosis and a target for ovarian cancer treatment PMID: 28808929 HO-1 was an important cellular factor against Dengue virus replication. PMID: 27553177 our results demonstrate that Pc-induced expression of HO-1 is mediated by the PKCA-Nrf-2/HO-1 pathway, and inhibits UVB-induced apoptotic cell death in primary skin cells. PMID: 29470442 HO-1 regulates macrophage activation via the SIRT1-p53 signaling network and regulates hepatocellular death in liver ischemia-reperfusion injury. PMID: 28842295 In light of a pivotal role of NRF2 and BACH1 in response to oxidative stress and regulation of HO-1, we examined if smoke-induced HO-1 expression is modulated through the NRF2/BACH1 axis. We demonstrated that smoke causes significant nuclear translocation of NRF2, but only a slight decrease in nuclear BACH1. PMID: 29125538 downregulation of HO-1 gene expression in patients with inflammatory bowel disease. PMID: 28770550 This study demonstrated that HO-1 plays a vital role in the development of gastric cancer and may serve as a therapeutic target of this type of cancer PMID: 29048628 Overexpression of HO-1 inhibited the increase in nucleus pulposus cell apoptosis after IL-1beta treatment and simultaneously inhibited the expression of p-P65. PMID: 29617687 We also found a subset of prostate cancer patient-derived xenografts and prostate cancer patient samples with mild HO-1 and low Gal-1 expression levels. These results highlight a novel function of a human-used drug as a means of boosting the antitumor response PMID: 28512172 Our data suggest that HO-1 exerts its inhibitory effect on Th17 cell differentiation by directly associating and blocking STAT3 phosphorylation. We speculate that hemin may be a potential therapeutic candidate for the treatment of other types of immune and pulmonary inflammatory-related diseases. PMID: 28580587 recipient promoter region (GT)n genotype may contribute to cardiac allograft vasculopathy development PMID: 28186648 study implies that DJ-1 may protect endothelial progenitor cells against Ang II-induced dysfunction by activating the PPARgamma/HO-1. PMID: 28600848 These results revealed that hemin treatment increased HMOX1 expression and inhibited TGFbetainduced epithelial-mesenchymal transition in MCF7 cells. PMID: 28627599 There was no association between HMOX1 gene promoter polymorphism and manifestation of Fabry Disease. PMID: 28951772 Most published Newborn studies demonstrated no effect of HO-1 promoter polymorphisms on the Neonatal Hyperbilirubinemia. PMID: 28206992 Genetic mutations within MAPK1 (rs6928, rs9340, rs11913721), HIF-1 (rs1087314, rs2057482), and HO-1 (rs2071746) could alter susceptibility to perimenopausal coronary artery disease in Chinese population. PMID: 28444966 The overexpression of HO1 alleviated oxidative damage through inhibition of the PI3K/AKT signaling pathway and downregulation of the expression of cMyc. PMID: 28713890 Study shows that heme degradation by HO-1 is required for aggresome-like induced structures (ALIS) formation, and that the free iron released on heme degradation is necessary and sufficient to induce ALIS. PMID: 27821769 co-expression patterns of NGF and heme oxygenase-1 might be used as prognostic indicators for gastric carcinoma patients PMID: 28679437 These results suggest that HO-1 is involved in oxygen-glucose deprivation-evoked upregulation of apical junctional complex proteins, which is partly mediated by MMP9 pathway. PMID: 29425821 HMOX-1, an anti-oxidase, is a bona fide transcriptional target gene of HSF4 in HLECs (human lens epithelial cells). HSF4 directly binds to the HSE element in HMOX-1 promoter to mediate its mRNA transcription and protein accumulation. PMID: 29454088 The regulated HO-1 expression of Bone marrow stromal cells provides a new putative target for chronic myeloid leukemia therapy. PMID: 28445830 Dihydromyricetin (DMY) protects HUVECs from ox-LDL-induced oxidative injury by activating Akt and ERK1/2, which subsequently activates Nrf2/HO-1 signaling, thereby up-regulating antioxidant enzymes and anti-apoptotic proteins. PMID: 28612103 review of non-canonical functions of the HO isoforms: protein-protein interaction, intracellular compartmentalization, and extracellular secretion [review] PMID: 27626166 The interaction between ALAD rs1800435 and the HMOX1 rs2071746, HMOX1 rs2071747 was not associated with essential tremor. PMID: 28276576 Docosahexaenoic acid (DHA) activates Nrf2, possibly through modification of critical Keap1 cysteine 288 residue and PKCdelta-mediated phosphorylation of Nrf2, leading to upregulation of HO-1 and NQO1 expression. PMID: 28604588 These results suggest that RYR extract serves as alternative and complementary medicine in the treatment of these diseases, by inducing HO-1, thereby decreasing the vascular complications of diabetes PMID: 28555162 These results indicate that TNFRI-Fc and hHO-1 overexpression may apparently induce free iron in the liver and exert oxidative stress by enhancing reactive oxygen species production and block normal postneonatal liver metabolism. PMID: 28503569 Mice overexpressing human HO-1 specifically in astrocytes are protected from collagenase-induced intracerebral hemorrhage, as examined by striatal cell viability, neurological deficits and mortality. PMID: 28323022 HMOX1 negatively regulates MMP-9 expression in chronic lymphocytic leukemia cells in response to arsenic trioxide, through modulation of the p38 MAPK/AP-1 signaling pathway. PMID: 27829220 Review/Meta-analysis: both the HO-1(GT)n repeat length polymorphism and the T(-413)A SNP are associated with decreased risk of coronary heart disease. The (GT)n repeat length polymorphism was associated with coronary restenosis following PCI. PMID: 27825138 These data suggest that heme oxygenase-1 is induced during acute HIV-1 infection, likely mediating anti-inflammatory effects and driving expansion of heme oxygenase-1-specific CD8 regulatory T cells capable of suppressing HIV-1-specific immune responses in vitro. PMID: 28060008 Among myelodysplastic syndromes patients only, CD163 + macrophage density and HO1 and H-ferritin expression by CD163 + macrophages increased in tandem with marrow iron. High HO1 was significantly associated with shorter overall survival. PMID: 26758041 elevated HMOX1 expression is associated with stemness in Glioblastoma multiforme and can be modulated through TGFbeta. PMID: 27354342 Fetal GTn Repeat in the Heme Oxygenase 1 Promoter Is Associated With Severe and Early-Onset Preeclampsia. PMID: 29203625 CAL suppresses the expression of pro-inflammatory cytokines via p62/Nrf2-linked HO-1 induction in RASFs. PMID: 27678042 Findings indicate the importance of nuclear heme oxygenase-1 (HO-1) post-translational modification in the induction of cancer progression. PMID: 28846111

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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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Recombinant Human HO-1 Protein

Recombinant Human HO-1 Protein

Product Overview

Target Details

FAQs