• Call +1.858.633.0165 or Fax +1.858.633.0166 or Contact Us

Heme Oxygenase 1 (HMOX1) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS954223

He oxygenase cleaves the he ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of he oxygenase is highest in the spleen, where senescent… More details

$315 / 0.02 mg (E-Coli) +1 FREE 8GB USB
Product Documentation
PDF
Sample Manual Insert View PDF
PDF
Testing Data View PDF
PDF
Certificate of Analysis (COA) View PDF
PDF
QC Report View PDF
PDF
Material Safety Data Sheet View PDF
PDF
Technical Datasheet View PDF
PDF
Protocol View PDF

Product Overview

Online Datasheet in PDF
Product Name
Heme oxygenase 1 (HMOX1), Recombinant Protein
Full Product Name
Recombinant Human Heme oxygenase 1
Product Gene Name
Product Synonym Gene Name
HO; HO1
Sequence
RPQPDSMPQD LSEALKEATK EVHTQAENAE FMRNFQKGQV TRDGFKLVMA SLYHIYVALE EEIERNKESP VFAPVYFPEE LHRKAALEQD LAFWYGPRWQ EVIPYTPAMQ RYVKRLHEVG RTEPELLVAH AYTRYLGDLS GGQVLKKIAQ KALDLPSSGE GLAFFTFPNI ASATKFKQLY RSRMNSLEMT PAVRQRVIEE AKTAFLLNIQ LFEELQELLT HDTKDQSPSR APGLRQRASN KVQDSAPVET PRGKPPLNTR SQAPLLRWVL TLSFLVATVA VGLYAM
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
36.6 kDa
Sequence Positions
3-288aa; Partial
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
141250
3D Structure
ModBase 3D Structure for P09601

Product Categories/Family for HMOX1 recombinant protein

ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for HMOX1 recombinant protein

Human heme oxygenase cDNA and induction of its mRNA by hemin.Yoshida T., Biro P., Cohen T., Mueller R.M., Shibahara S.Eur. J. Biochem. 171:457-461(1988) A genome annotation-driven approach to cloning the human ORFeome.Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.Genome Biol. 5:R84.1-R84.11(2004) SeattleSNPs variation discovery resourceThe DNA sequence of human chromosome 22.Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.Nature 402:489-495(1999) Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite.Keyse S.M., Tyrrell R.M.Proc. Natl. Acad. Sci. U.S.A. 86:99-103(1989) Structural organization of the human heme oxygenase gene and the function of its promoter.Shibahara S., Sato M., Muller R.M., Yoshida T.Eur. J. Biochem. 179:557-563(1989) Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency.Yachie A., Niida Y., Wada T., Igarashi N., Kaneda H., Toma T., Ohta K., Kasahara Y., Koizumi S.J. Clin. Invest. 103:129-135(1999) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) Mechanisms of cell protection by heme oxygenase-1.Gozzelino R., Jeney V., Soares M.P.Annu. Rev. Pharmacol. Toxicol. 50:323-354(2010) CXCR3-B can mediate growth-inhibitory signals in human renal cancer cells by down-regulating the expression of heme oxygenase-1.Datta D., Banerjee P., Gasser M., Waaga-Gasser A.M., Pal S.J. Biol. Chem. 285:36842-36848(2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) Endoplasmic reticulum anchored heme-oxygenase 1 faces the cytosol.Gottlieb Y., Truman M., Cohen L.A., Leichtmann-Bardoogo Y., Meyron-Holtz E.G.Haematologica 97:1489-1493(2012) Crystal structure of human heme oxygenase-1.Schuller D.J., Wilks A., Ortiz de Montellano P.R., Poulos T.L.Nat. Struct. Biol. 6:860-867(1999) Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1 catalytic implications.Lad L., Wang J., Li H., Friedman J., Bhaskar B., Ortiz de Montellano P.R., Poulos T.L.J. Mol. Biol. 330:527-538(2003)

Other Notes

Small volumes of HMOX1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for HMOX1 purchase

MBS954223 is a recombinant protein targeting HMOX1. Also known as Recombinant Human Heme oxygenase 1. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for HMOX1. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Related Accession #
GenBank Nucleotide #
NCBI Official Full Name
heme oxygenase 1
NCBI Official Synonym Full Names
heme oxygenase 1
NCBI Official Symbol
HMOX1
NCBI Official Synonym Symbols
HO-1; HSP32; HMOX1D; bK286B10
UniProt Protein Name
Heme oxygenase 1
Protein Family
UniProt Gene Name
HMOX1
UniProt Synonym Gene Names
HO; HO1; HO-1
UniProt Entry Name
HMOX1_HUMAN
NCBI Protein Information
heme oxygenase 1

NCBI Summary for HMOX1

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family. [provided by RefSeq, Jul 2008]
Show more

UniProt Comments for HMOX1

HMOX1: 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. Heme oxygenase 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. Expressed at higher levels in renal cancer tissue than in normal tissue. Belongs to the heme oxygenase family.

Protein type: Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; Oxidoreductase; EC 1.14.99.3

Chromosomal Location of Human Ortholog: 22q13.1

Cellular Component: caveola; cytosol; endoplasmic reticulum; endoplasmic reticulum membrane; extracellular space; membrane; nucleolus; nucleus; perinuclear region of cytoplasm

Molecular Function: enzyme binding; heme binding; heme oxygenase (decyclizing) activity; metal ion binding; phospholipase D activity; protein binding; protein homodimerization activity; signal transducer activity

Biological Process: angiogenesis; cell death; cellular iron ion homeostasis; cellular response to nutrient; DNA damage response, signal transduction resulting in induction of apoptosis; endothelial cell proliferation; erythrocyte homeostasis; excretion; healing during inflammatory response; heme catabolic process; heme oxidation; iron ion homeostasis; negative regulation of DNA binding; negative regulation of leukocyte migration; negative regulation of mast cell cytokine production; negative regulation of mast cell degranulation; negative regulation of neuron apoptosis; negative regulation of smooth muscle cell proliferation; negative regulation of transcription factor activity; porphyrin metabolic process; positive regulation of angiogenesis; positive regulation of chemokine biosynthetic process; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of smooth muscle cell proliferation; positive regulation of vasodilation; protein homooligomerization; regulation of angiogenesis; regulation of blood pressure; regulation of transcription factor activity; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; response to estrogen stimulus; response to hydrogen peroxide; response to nicotine; response to oxidative stress; small GTPase mediated signal transduction; smooth muscle hyperplasia; transmembrane transport

Disease: Heme Oxygenase 1 Deficiency; Pulmonary Disease, Chronic Obstructive
Show more

Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

Request a Quote

Please fill out the form below and our representative will get back to you shortly.

MBS000000
Contact Us

Please fill out the form below and our representative will get back to you shortly.

MBS000000