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SDS-Page

Heme oxygenase1 Recombinant Protein | HMOX1 recombinant protein

Heme oxygenase1,1-266aa, Human, His tag, E Coli

Gene Names
HMOX1; HO-1; HSP32; HMOX1D; bK286B10
Applications
SDS-Page
Purity
> 95% by SDS-PAGE
Synonyms
Heme oxygenase1; 1-266aa; Human; His tag; E Coli; HO-1; Heat shock protein 32; HSP32; bK286B10; D8Wsu38e; Heme oxygenase (decycling) 1; Heme oxygenase 1; Hemox; Hmox; HMOX 1; HMOX1; HO; HO 1; HO1.; HMOX1 recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
> 95% by SDS-PAGE
Form/Format
Liquid. In 20 mM Tris-HCl Buffer (pH 8.0) containing 50mM NaCl, 0.1mM PMSF, 10% glycerol
Concentration
1 mg/ml (determined by Absorbance at 280nm) (varies by lot)
Sequence
MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQ LYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHH HHHH
Sequence Length
288
Applicable Applications for HMOX1 recombinant protein
SDS-PAGE
Endotoxin Level
< 1.0 EU per 1 ug of protein (determined by LAL method)
Preparation and Storage
Can be stored at 4°C short term (1-2 weeks).
For long term storage, aliquot and store at -20°C or -70°C.
Avoid repeated freezing and thawing cycles.

SDS-Page

SDS-Page
Related Product Information for HMOX1 recombinant protein
Heme oxygenase 1 belongs to the heme oxygenase family and is an essential enzyme in heme catabolism. It cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Also this protein is known to play an important role in the regulation of cardiovascular function and its adaptive response to a variety of stressors. Recombinant human Heme oxygenase 1 protein, fused to His-tag at C-terminus, was expressed in E Coli and purified by using conventional chromatography techniques.
Product Categories/Family for HMOX1 recombinant protein
References
Vareille M., et al. (2008). J Immunol. 180 (8):5720-6.; Soares MP., et al. (2001). Immunol Rev.184:275-85;

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
31.4 kDa (274 aa), confirmed by MALDI-TOF.
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
NCBI Protein Information
heme oxygenase 1
UniProt Protein Name
Heme oxygenase 1
UniProt Gene Name
HMOX1
UniProt Synonym Gene Names
HO; HO1; HO-1

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. [provided by RefSeq, Jul 2008]

Uniprot Description

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.

Research Articles on HMOX1

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Product Notes

The HMOX1 hmox1 (Catalog #AAA203285) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. AAA Biotech's Heme oxygenase1 can be used in a range of immunoassay formats including, but not limited to, SDS-PAGE. Researchers should empirically determine the suitability of the HMOX1 hmox1 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. The amino acid sequence is listed below: MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQ LYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHH HHHH. It is sometimes possible for the material contained within the vial of "Heme oxygenase1, 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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