Recombinant Mouse Heme Oxygenase 1 (HMOX1) Protein (His-B2M)

Name: Recombinant Mouse Heme Oxygenase 1 (HMOX1) Protein (His-B2M)
Brand: Beta LifeScience
SKU: BLC-08632P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Heme Oxygenase 1 (HMOX1) Protein (His-B2M) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P14901
Target Symbol	HMOX1
Synonyms	Hmox1; Heme oxygenase 1; HO-1; EC 1.14.14.18; P32 protein
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-B2M
Target Protein Sequence	MERPQPDSMPQDLSEALKEATKEVHIQAENAEFMKNFQKGQVSREGFKLVMASLYHIYTALEEEIERNKQNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEIIPCTPATQHYVKRLHEVGRTHPELLVAHAYTRYLGDLSGGQVLKKIAQKAMALPSSGEGLAFFTFPNIDSPTKFKQLYRARMNTLEMTPEVKHRVTEEAKTAFLLNIELFEELQVMLTEEHKDQSPSQMASLRQRPASLVQDTAPAETPRGKPQISTSSSQTPLLQWVLTLSFLLATVAVGIYAM
Expression Range	1-289aa
Protein Length	Full Length
Mol. Weight	46.9 kDa
Research Area	Cell Biology
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	KEGG: mmu:15368 STRING: 10090.ENSMUSP00000005548 UniGene: PMID: 30327713 Ori might exhibit a protective role against H2O2-stimulated oxidative damage by the induction of HO-1 expression through the activation of the JNK- and PI3K/AKT-Nrf2 signaling pathways. PMID: 29959995 This is the first study to demonstrate the regulatory role of HO-1 in silicosis. PMID: 30068325 The HO-1-mediated pathway is involved in the suppressive effects of FNDC4 on inflammation and insulin resistance. PMID: 29787756 HO-1 enhanced STAT3 phosphorylation, which enriched to Il12b and Il23a loci and negatively regulated their transcription. These findings demonstrate the underlying mechanism through which a nutritional can interfere with the immune response. CUR silences IL-23/Th17-mediated pathology by enhancing HO-1/STAT3 interaction in dendritic cells. PMID: 28290522 HO-1 reduces HFD-induced AKT2 phosphorylation via ROS thresholding in mitochondria to reduce visceral adipose precursor proliferation. HO-1 influences adipogenesis in a cell-autonomous way by regulating events early in adipogenesis, during the process of mitotic clonal expansion, upstream of Cebpalpha and PPARgamma. PMID: 28102348 Involved in the Nrf2/HO-1 pathway. PMID: 29730008 Studied effect of Sargassum horneri (Turner) C. Agardh ethanol extract (SHE) on inflammation induced by fine dust in RAW 264.7 cells. Results suggest SHE protects the cells from oxidative stress in part by activating the nuclear factor erythroid derived 2 like 2 /heme oxygenase 1 (Nrf2/HO-1) signal pathway. PMID: 30200963 Our results reveal a previously unrecognized function of HO-1 in regulating SMC gene expressions during ESC-EB development. PMID: 29216542 HO-1 protects bone marrow mesenchymal stem cells from reactive oxygen species by secreting IL-10 upon iron overload. PMID: 29111167 Results show that renal myeloid cells upregulate HO-1 upon renal ischemia-reperfusion injury (IRI). Also, myeloid HO-1 mitigates both innate immune responses and oxidative stress upon renal IRI. PMID: 28298633 Findings demonstrate that myeloid HO-1 plays an anti-inflammatory role in the acute response to zymosan in vivo. PMID: 29599896 Genetic Hmox1 partial deficiency is sufficient to sensitize mice to the development of diabetic glomerular microvascular lesions. HO-1 exerts antioxidant effects in the kidney during diabetes mellitus. These have protective effects on the development of glomerular endothelial injury. PMID: 29359167 Inhibition of miR-92a attenuates oxidative stress and improves endothelial function through enhancing HO-1 expression and activity in db/db mouse aortas PMID: 28683566 n-propargyl caffeamide (PACA) attenuated LPS-induced NF-kB activation while activated Nrf2/HO-1 pathway. HO-1 inhibitor SnPP attenuated the effects of PACA on iNOS expression in LPS-challenged macrophages, possibly by regulating the cross-talk between HO-1 and NF-kB pathways. PMID: 29996121 Ablation of adipose tissue-HO-1 abridged PGC1 expression promoted mitochondrial dysfunction and contributed to an increase of pro-inflammatory visceral fat and abrogated beige-cell like phenotype. PMID: 28763300 These results suggested that schisandrin A has a protective effect against LPS-induced inflammatory and oxidative responses in RAW 264.7 cells by inhibiting the NF-kappaB, MAPK and PI3K/Akt pathways; these effects are mediated, at least in part, by the activation of the Nrf2/HO-1 pathway PMID: 29115385 Newborns appear to be protected from the pro-oxidative effects of free heme (FH), which may be mediated by heme binding and a higher absolute HO activity at baseline and after FH-mediated induction. PMID: 28926834 Rosiglitazone Regulates TLR4 and Rescues HO-1 and NRF2 Expression in Myometrial and Decidual Macrophages in Inflammation-Induced Preterm Birth. PMID: 28322133 this study shows that induction of heme oxygenas-1 attenuates NLRP3 inflammasome activation in lipopolysaccharide-induced mastitis in mice PMID: 28938188 DADLE was able to significantly improve hepatic I/R injury in mice, and the specific mechanism may be associated with the Nrf2/HO1 signaling pathway. PMID: 28901476 HO-1 role in the feedback response to blood carbon monoxide depletion PMID: 27057920 Pretreatment with Zinc L-carnosine was able to activate Nrf2/HO-1 signaling pathway, thus suppressing the expression of inflammatory mediators, such as NO and iNOS in LPS-induced RAW 264.7 cells. PMID: 28697633 Study demonstrated that a higher level of HO-1 associated with higher levels of injury severity, histological lesions and behavioral deficits in males than in females was induced by striatal ferrous citrate-infusion, which simulates iron overload in the striatum after intracerebral hemorrhage. PMID: 27198537 these results indicate that MaR 1 protects against lung I/R injury through suppressing oxidative stress. The mechanism is partially explained by activation of the Nrf-2-mediated HO-1 signaling pathway. PMID: 28751936 Splenic Ly6C(hi) monocytes contribute to adverse late post-ischemic left ventricular remodeling in heme oxygenase-1 deficient mice. PMID: 28534119 findings suggest that HO-1 protects against I/R-induced hepatic injury via regulation of mitochondrial QC by PGAM5 signaling. PMID: 29524517 this study shows that heme oxygenase 1 affects granulopoiesis in mice through control of myelocyte proliferation PMID: 28576353 HO-1(pos) /CD169(neg) macrophages in jejunal serosa and at Auerbach's plexus up-regulated by lipopolysaccharide PMID: 27860408 The results demonstrated that restoration of Brg1 during reperfusion could enhance Nrf2-mediated inducible expression of HO-1 during hepatic ischemia-reperfusion injury to effectively increase antioxidant ability to combat against hepatocytes damage. PMID: 28569786 report that TLR signaling involving MyoD88 has a negative role in egress of HSPCs from BM into PB as TLR signaling enhances expression of HO-1 in hematopoietic cells PMID: 27560112 Taken together, these findings suggest that 2,3,5,4'-Tetrahydroxystilbene-2-O-beta-D-glucoside (TSG) enhances mitochondrial biogenesis and function mainly via activation the HO-1. TSG can be developed as a potential drug for treatment of inflammatory diseases. PMID: 28473878 The in vitro study illustrated that the anti-inflammatory effects of RA-XII were partially reversed following Nrf2 and HO-1 inhibition. Together, these findings strongly suggested that RA-XII is a potential agent against acute kidney injury. PMID: 29277609 mRNA and protein levels of heme oxygenase-1 (HO-1)aresignificantly increased by Melaleuca alternifolia oil via p38 and JNK MAPK activation. PMID: 29121804 Together with results showing involvement of TTF-1 in the TNF-alpha-induced increase in interleukin 1 beta and monocyte chemotactic protein 1 production, this study suggests that TTF-1 plays an important role in the mouse hypothalamus TNF-alpha-induced inflammatory response for regulating HO-1 gene expression. PMID: 29305861 Curtailment of glial HO-1 transduction at strategic points of the life course may confer neuroprotection in human degenerative and developmental central nervous system disorders. PMID: 28746897 Results indicate the essential roles of heme oxygenase-1 (HO-1) in suppressing the pathogenesis of abdominal aortic aneurysm (AAA), suggesting targeting HO-1 might be a promising therapeutic strategy for AAA. PMID: 27626316 inadequate HO-1 in striatal astrocytes might contribute to the limited antioxidant defense and dopaminergic neuron degeneration in PD, and preferential HO-1 activation in striatal astrocytes might be neuroprotective. PMID: 26385576 results indicate that high expression of HO-1 may reduce the severity of acute graft-versus-host disease by regulation of the TH17/Treg balance PMID: 27168057 YZH-106 induced p38 MAPK and ERK1/2 phosphorylation, which led to the activation of erythroid 2-related factor 2 (Nrf2) that up-regulated heme oxygenase-1 (HO-1) expression in addition to other genes. PMID: 27107768 our data indicate that luteolin diminishes the proinflammatory mediators NO, inflammatory cytokines and the expression of their regulatory genes, iNOS and COX-2, in PRV-infected RAW264.7 cells by inhibiting STAT1/3 dependent NF-kappaB activation and inducing Nrf2mediated HO-1 expression. PMID: 27016074 we demonstrate that RG induces HO-1 expression by promoting phosphorylation of Nrf2 at Ser40 through activation of the ERK1/2 and JNK cascade in macrophages. PMID: 28257879 We conclude that 1) CIH induces expression of HO-1 in the C1 and pre-BotC regions within 1 day and 2) HO-1 is necessary for hypoxia respiratory response and contributes to the maintenance of the hypoxic sigh responses and baseline sympathetic activity during CIH. PMID: 27609199 this study demonstrates that ammonia stimulates the expression of HO-1 in endothelial cells via the ROS-Nrf2 pathway, and that the induction of HO-1 contributes to the cytoprotective action of ammonia by generating carbon monoxide. Moreover, it identifies ammonia as a potentially important signaling gas in the vasculature that promotes endothelial cell survival. PMID: 27867098 HO-1 influences granulopoiesis through regulation of myelocyte proliferation. It is accompanied by changes in expression of transcriptionally active C/EBPbeta protein. PMID: 27817989 EET-mediated increase in HO-1 levels require PGC-1alpha expression PMID: 27418542 Downregulation of inducible NO synthetase (iNOS) resulted in downregulation of heme oxygenase 1 (HO-1), and, conversely, upregulation of iNOS enhanced HO-1 activity. PMID: 27752990 Data suggest the a decrease in migration of hematopoietic stem progenitor cells (HSPCs) can be explained by impaired calcium release in phospholipase C-beta2 (PLC-beta2) knockout (KO) mice and a high baseline level of heme oxygenase 1 (HO-1), an enzyme that negatively regulates cell migration. PMID: 27704316 HO-1 expression is upregulated by hydrogen-rich water in a mouse model of in fl ammatory bowel disease, which also inhibits inflammatory factors, and oxidative stress and ER stress PMID: 28293084 study demonstrates that human respiratory syncytial virus (hRSV) infection can be modulated by the expression of HO-1 both in vitro and in vivo; thus, HO-1 activity may play a critical role during hRSV infection PMID: 28566367

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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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