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Heme Oxygenase 2 Recombinant Protein | HMOX2 recombinant protein

Recombinant Human Heme Oxygenase 2

Gene Names
HMOX2; HO-2
Purity
Greater than 90% as determined by SDS-PAGE.
Synonyms
Heme Oxygenase 2; Recombinant Human Heme Oxygenase 2; HMOX2 Human; Heme Oxygenase-2 Human Recombinant; EC 1.14.99.3; HO2; Heme oxygenase 2; HO-2; HMOX2; HMOX2 recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
Greater than 90% as determined by SDS-PAGE.
Form/Format
HMOX2 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.
Sterile filtered colorless solution.
Sequence
SAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP MELHRKEALT KDMEYFFGEN WEEQVQCPKA AQKYVERIHY IGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA GSTLARETLE DGFPVHDGKG DMRK
Sequence Length
316
Preparation and Storage
HMOX2 Human Recombinant although stable at 4 degree C for 1 week, should be stored below -18 degree C. Please prevent freeze thaw cycles.
Related Product Information for HMOX2 recombinant protein
Description: HMOX2 Human Recombinant produced in E Coli is a single, non-glycosylated, polypeptide chain containing 264 amino acids (1-264 a.a.) and having a molecular mass of 30.5 kDa. HMOX2 is purified by proprietary chromatographic techniques.

Introduction: HMOX2 cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently transferred to bilirubin by biliverdin reductase. Under physiological conditions, the activity of HMOX2 is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. HMOX2 participates in the production of carbon monoxide in the brain where it operates as a neurotransmitter. HMOX2 is an essential enzyme in heme catabolism and is involved in cellular response to oxidative stress.
Product Categories/Family for HMOX2 recombinant protein

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
32,837 Da
NCBI Official Full Name
heme oxygenase 2 isoform b
NCBI Official Synonym Full Names
heme oxygenase (decycling) 2
NCBI Official Symbol
HMOX2
NCBI Official Synonym Symbols
HO-2
NCBI Protein Information
heme oxygenase 2
UniProt Protein Name
Heme oxygenase 2
Protein Family
UniProt Gene Name
HMOX2
UniProt Synonym Gene Names
HO2; HO-2
UniProt Entry Name
HMOX2_HUMAN

NCBI Description

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. Several alternatively spliced transcript variants encoding three different isoforms have been found for this gene. [provided by RefSeq, Oct 2013]

Uniprot Description

HMOX2: 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 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. 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: 16p13.3

Cellular Component: endoplasmic reticulum membrane; membrane; plasma membrane

Molecular Function: protein binding; metal ion binding; heme oxygenase (decyclizing) activity

Biological Process: heme catabolic process; cellular iron ion homeostasis; porphyrin metabolic process; heme oxidation; response to hypoxia; transmembrane transport

Research Articles on HMOX2

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Product Notes

The HMOX2 hmox2 (Catalog #AAA143697) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. The amino acid sequence is listed below: SAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP MELHRKEALT KDMEYFFGEN WEEQVQCPKA AQKYVERIHY IGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA GSTLARETLE DGFPVHDGKG DMRK. It is sometimes possible for the material contained within the vial of "Heme Oxygenase 2, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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