Recombinant Human Heme Oxygenase 1 (HMOX1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04427P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Heme Oxygenase 1 (HMOX1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04427P
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Product Overview

Description Recombinant Human Heme Oxygenase 1 (HMOX1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P09601
Target Symbol HMOX1
Synonyms 32 kD; bK286B10; D8Wsu38e; heat shock protein 32 kD; heat shock protein 32kD; Heat shock protein; Heme oxygenase (decycling) 1; Heme oxygenase 1; Hemox; HMOX 1; Hmox; Hmox1; HMOX1_HUMAN; HO 1; HO; HO-1; HO1 ; Hsp32
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His
Target Protein Sequence RPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
Expression Range 3-288aa
Protein Length Partial
Mol. Weight 36.6kDa
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 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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    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.

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