Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Heme oxygenase 1 (HO-1) (EC 1.14.14.18) (P32 protein)

 HMOX1_MOUSE             Reviewed;         289 AA.
P14901;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
07-JUN-2017, entry version 150.
RecName: Full=Heme oxygenase 1;
Short=HO-1;
EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
AltName: Full=P32 protein;
Name=Hmox1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Fibroblast;
PubMed=3409220;
Kageyama H., Hiwasa T., Tokunaga K., Sakiyama S.;
"Isolation and characterization of a complementary DNA clone for a Mr
32,000 protein which is induced with tumor promoters in BALB/c 3T3
cells.";
Cancer Res. 48:4795-4798(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8288554;
Alam J., Cai J., Smith A.;
"Isolation and characterization of the mouse heme oxygenase-1 gene.
Distal 5' sequences are required for induction by heme or heavy
metals.";
J. Biol. Chem. 269:1001-1009(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INDUCTION BY M.TUBERCULOSIS.
PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
Shiloh M.U., Manzanillo P., Cox J.S.;
"Mycobacterium tuberculosis senses host-derived carbon monoxide during
macrophage infection.";
Cell Host Microbe 3:323-330(2008).
[5]
INDUCTION IN MACROPHAGES AND LUNGS BY M.TUBERCULOSIS.
STRAIN=C3Heb/FeJ, and C57BL/6 X FVB; TISSUE=Lung, and Macrophage;
PubMed=18400743; DOI=10.1074/jbc.M802274200;
Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S.,
Kramnik I., Agarwal A., Steyn A.J.;
"Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
tuberculosis dormancy regulon.";
J. Biol. Chem. 283:18032-18039(2008).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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.
-!- CATALYTIC ACTIVITY: Protoheme + 3 [reduced NADPH--hemoprotein
reductase] + 3 O(2) = biliverdin + Fe(2+) + CO + 3 [oxidized
NADPH--hemoprotein reductase] + 3 H(2)O.
{ECO:0000250|UniProtKB:O48782}.
-!- SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum membrane
{ECO:0000250}; Peripheral membrane protein; Cytoplasmic side.
-!- INDUCTION: Heme oxygenase 1 activity is highly inducible by its
substrate heme and by various non-heme substances such as heavy
metals, bromobenzene, and endotoxin. It is also induced in
macrophages, liver and the lungs upon infection with
M.tuberculosis (at protein level). Data is conflicting as to
whether macrophage induction is independent of the nitric oxide
(NO) signaling pathway (PubMed:18400743), or dependent on NO
(PubMed:18474359). {ECO:0000269|PubMed:18400743,
ECO:0000269|PubMed:18474359}.
-!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M33203; AAA39872.1; -; mRNA.
EMBL; X13356; CAA31732.1; -; mRNA.
EMBL; X56824; CAA40159.1; -; Genomic_DNA.
EMBL; X56825; CAA40159.1; JOINED; Genomic_DNA.
EMBL; X56826; CAA40159.1; JOINED; Genomic_DNA.
EMBL; X56827; CAA40159.1; JOINED; Genomic_DNA.
EMBL; BC010757; AAH10757.1; -; mRNA.
CCDS; CCDS22423.1; -.
PIR; I48409; I48409.
RefSeq; NP_034572.1; NM_010442.2.
UniGene; Mm.276389; -.
ProteinModelPortal; P14901; -.
SMR; P14901; -.
IntAct; P14901; 3.
MINT; MINT-4097595; -.
STRING; 10090.ENSMUSP00000005548; -.
ChEMBL; CHEMBL4434; -.
iPTMnet; P14901; -.
PhosphoSitePlus; P14901; -.
SwissPalm; P14901; -.
EPD; P14901; -.
PaxDb; P14901; -.
PeptideAtlas; P14901; -.
PRIDE; P14901; -.
Ensembl; ENSMUST00000005548; ENSMUSP00000005548; ENSMUSG00000005413.
GeneID; 15368; -.
KEGG; mmu:15368; -.
UCSC; uc009mhc.2; mouse.
CTD; 3162; -.
MGI; MGI:96163; Hmox1.
eggNOG; KOG4480; Eukaryota.
eggNOG; COG5398; LUCA.
GeneTree; ENSGT00390000017673; -.
HOGENOM; HOG000233221; -.
HOVERGEN; HBG005982; -.
InParanoid; P14901; -.
KO; K00510; -.
OMA; KKSHTMA; -.
OrthoDB; EOG091G0AS0; -.
PhylomeDB; P14901; -.
TreeFam; TF314786; -.
BRENDA; 1.14.99.3; 3474.
Reactome; R-MMU-189483; Heme degradation.
Reactome; R-MMU-917937; Iron uptake and transport.
PRO; PR:P14901; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000005413; -.
CleanEx; MM_HMOX1; -.
ExpressionAtlas; P14901; baseline and differential.
Genevisible; P14901; MM.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0020037; F:heme binding; ISO:MGI.
GO; GO:0004392; F:heme oxygenase (decyclizing) activity; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004630; F:phospholipase D activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0004871; F:signal transducer activity; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0006879; P:cellular iron ion homeostasis; ISO:MGI.
GO; GO:0071243; P:cellular response to arsenic-containing substance; IDA:MGI.
GO; GO:0071276; P:cellular response to cadmium ion; IDA:MGI.
GO; GO:0072719; P:cellular response to cisplatin; IMP:MGI.
GO; GO:0034605; P:cellular response to heat; ISO:MGI.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0031670; P:cellular response to nutrient; IEA:Ensembl.
GO; GO:0034101; P:erythrocyte homeostasis; ISO:MGI.
GO; GO:0042167; P:heme catabolic process; ISO:MGI.
GO; GO:0042168; P:heme metabolic process; IDA:MGI.
GO; GO:0006788; P:heme oxidation; ISO:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0055072; P:iron ion homeostasis; ISO:MGI.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IEA:Ensembl.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
GO; GO:0016242; P:negative regulation of macroautophagy; IMP:MGI.
GO; GO:0032764; P:negative regulation of mast cell cytokine production; IEA:Ensembl.
GO; GO:0043305; P:negative regulation of mast cell degranulation; IEA:Ensembl.
GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0016239; P:positive regulation of macroautophagy; IMP:MGI.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
GO; GO:0034395; P:regulation of transcription from RNA polymerase II promoter in response to iron; IDA:MGI.
GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; ISO:MGI.
GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
GO; GO:0002246; P:wound healing involved in inflammatory response; ISO:MGI.
CDD; cd00232; HemeO; 1.
Gene3D; 1.20.910.10; -; 1.
InterPro; IPR002051; Haem_Oase.
InterPro; IPR016053; Haem_Oase-like.
InterPro; IPR016084; Haem_Oase-like_multi-hlx.
InterPro; IPR018207; Haem_oxygenase_CS.
PANTHER; PTHR10720; PTHR10720; 1.
Pfam; PF01126; Heme_oxygenase; 1.
PIRSF; PIRSF000343; Haem_Oase; 1.
PRINTS; PR00088; HAEMOXYGNASE.
SUPFAM; SSF48613; SSF48613; 1.
PROSITE; PS00593; HEME_OXYGENASE; 1.
1: Evidence at protein level;
Apoptosis; Complete proteome; Endoplasmic reticulum; Heme; Iron;
Membrane; Metal-binding; Microsome; Oxidoreductase; Phosphoprotein;
Reference proteome.
CHAIN 1 289 Heme oxygenase 1.
/FTId=PRO_0000209688.
METAL 25 25 Iron (heme axial ligand). {ECO:0000250}.
BINDING 18 18 Heme. {ECO:0000250}.
BINDING 134 134 Heme. {ECO:0000250}.
BINDING 183 183 Heme. {ECO:0000250}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000250|UniProtKB:P09601}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000250|UniProtKB:P06762}.
SEQUENCE 289 AA; 32929 MW; 19DB0DCCD574044B CRC64;
MERPQPDSMP QDLSEALKEA TKEVHIQAEN AEFMKNFQKG QVSREGFKLV MASLYHIYTA
LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH WQEIIPCTPA TQHYVKRLHE
VGRTHPELLV AHAYTRYLGD LSGGQVLKKI AQKAMALPSS GEGLAFFTFP NIDSPTKFKQ
LYRARMNTLE MTPEVKHRVT EEAKTAFLLN IELFEELQVM LTEEHKDQSP SQMASLRQRP
ASLVQDTAPA ETPRGKPQIS TSSSQTPLLQ WVLTLSFLLA TVAVGIYAM


Related products :

Catalog number Product name Quantity
3391BP-50 Heme Oxygenase-1 Blocking Peptide target: Heme Oxygenase-1 50 μg
3392BP-50 Heme Oxygenase-2 Blocking Peptide target: Heme Oxygenase-2 50 μg
LF-MA10139 anti-Heme oxygenase 2 (1D8-1A8), Mouse monoclonal to Heme oxygenase 2, Isotype IgG1, Host Mouse 100 ug
LF-PA10009 anti-Heme Oxygenase 1, Mouse polyclonal to Heme Oxygenase 1, Isotype , Host Mouse 50 ug
SCH-4915-1050 RABBIT ANTI HUMAN HEME OXYGENASE 1, Product Type Polyclonal Antibody, Specificity HEME OXYGENASE 1, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications C, 50 µg
4915-1050 RABBIT ANTI HUMAN HEME OXYGENASE 1, Product Type Polyclonal Antibody, Specificity HEME OXYGENASE 1, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications C, 50 µg
18-272-195848 Heme Oxygenase 1 - Rabbit polyclonal to Heme Oxygenase 1 Polyclonal 0.1 ml
20-272-190816 Heme Oxygenase 1 - Mouse monoclonal [HO-1-1] to Heme Oxygenase 1; EC 1.14.99.3; HO-1 Monoclonal 0.05 mg
20-272-190754 Heme Oxygenase 1 - Mouse monoclonal [GTS - 1] to Heme Oxygenase 1 Monoclonal 0.05 mg
U1412Pl Plant Heme Heme Oxygenase CLIA KIT 96T
E1412Pl Plant Heme Heme Oxygenase ELISA Kit 96T
80R-1099 Heme oxygenase 1 protein (His tag), Conjugated Proteins 100 ug
orb90142 Human Heme Oxygenase 1 protein Enzymes 10
orb90143 Human Heme Oxygenase 2 protein Enzymes 5
HO26-R-25 Recombinant purified rat Heme Oxygenase 2 (HO-2) protein 25 ug
HO22-C Recombinant purified rat Heme Oxygenase 2 (HO-2) protein WB +ve control 100 ul
HO11-C Recombinant purified Rat Heme Oxygenase 1 (HO-1) protein WB +ve control 100 ul
abx108338 Polyclonal Rabbit Heme oxygenase 1 protein Antibody (HRP) 100 μg
HO26-R-25 Recombinant purified rat Heme Oxygenase 2 (HO_2) protein 25 ug
abx109856 Polyclonal Rabbit Heme oxygenase 1 protein Antibody 100 μg
bs-1238P Peptides: HO-2(Heme oxygenase 2) Protein Length:12-25 amino acids. 200ug lyophilized
HO12-C Recombinant purified Human Heme Oxygenase 1 (HO-1) protein WB +ve control 100 ul
U0584m CLIA Heme oxygenase 1,Hmox1,HO-1,Mouse,Mus musculus,P32 protein 96T
abx105499 Polyclonal Rabbit Heme oxygenase 1 protein Antibody (Biotin) 100 μg
abx106916 Polyclonal Rabbit Heme oxygenase 1 protein Antibody (FITC) 100 μg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur