Analytical Data
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Gene name
HO2
- Application
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Alternative Names
HO2；HO2；Heme oxygenase 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P30519
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Expression Region
2-316aa
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AA 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 DMRKCPFYAA EQDKGALEGS SCPFRTAMAV LRKPSLQFIL AAGVALAAGL LAWYYM
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of the HO2 (Heme Oxygenase 2) recombinant protein is rooted in its critical role in cellular physiology and pathology. As a member of the heme oxygenase family, HO2 is responsible for the catabolism of heme into biliverdin, carbon monoxide (CO), and free iron, processes that are crucial for maintaining cellular homeostasis and protecting against oxidative stress. Unlike its counterpart HO1, which is highly inducible under stress conditions, HO2 is constitutively expressed in various tissues, particularly in the brain and vascular systems, suggesting its involvement in neuroprotection and vasodilation. The exploration of HO2 recombinant protein is significant for elucidating its enzymatic mechanisms and regulatory pathways, which can offer insights into its potential therapeutic applications. Dysregulation of HO2 has been linked to several diseases, including neurodegenerative disorders and cardiovascular diseases, making it a compelling target for drug development. By producing HO2 as a recombinant protein, researchers can study its structure-function relationships, assess its kinetic properties, and explore its interactions with various molecules, thereby advancing our understanding of its biological roles and therapeutic potential. The ability to generate HO2 in a controlled manner facilitates high-throughput screening and the development of novel therapeutic strategies aimed at modulating its activity for disease intervention. Overall, the research on HO2 recombinant protein not only enhances our understanding of heme metabolism but also opens avenues for exploring innovative treatments for conditions associated with its dysregulation.
