Analytical Data
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Gene name
HO1
- Application
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Alternative Names
HO1；HO；Heme oxygenase 1
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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
P09601
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Expression Region
1-288aa
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AA Sequence
MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLV MASLYHIYVA LEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYG PRWQEVIPYTPAMQRYVKRLHE VGRTEPELLVAHAYTRYLGDLSGGQV LKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQ LYRSRMNSLEMTPA VRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRA SN KVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
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Molecular Weight
32 kDa
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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
HO1, or heme oxygenase-1, is an important enzyme that plays a crucial role in heme catabolism, converting heme into biliverdin, carbon monoxide, and free iron. This enzyme is part of the body’s response to oxidative stress and inflammation, and its expression is regulated by various stimuli, including cytokines and hypoxia. The significance of HO1 has been particularly highlighted in various pathological conditions, such as cardiovascular diseases, neurodegenerative disorders, and cancer, where it exhibits cytoprotective, anti-inflammatory, and anti-apoptotic properties. Research on recombinant HO1 protein has gained momentum due to its potential therapeutic applications. By producing HO1 in recombinant systems, researchers can obtain large quantities of the enzyme for detailed biochemical studies, therapeutic enzyme replacement, or exploration of its roles in disease models. Additionally, understanding the structure-function relationships of HO1 through recombinant protein studies may reveal novel targets for drug development and biomarker identification. The ongoing research aims to elucidate the mechanisms by which HO1 exerts its protective effects and to explore its therapeutic potential in clinical settings. Overall, HO1 recombinant protein research is pivotal for advancing our knowledge of its biological functions and therapeutic implications in various diseases.
