Analytical Data
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Gene name
HMOX1
- Application
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Alternative Names
HMOX1；HO；HO1；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
3-288aa
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AA Sequence
RPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
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Molecular Weight
36.6 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
Heme oxygenase-1 (HMOX1) is an enzyme that plays a crucial role in heme catabolism, converting heme into biliverdin, free iron, and carbon monoxide. This enzymatic process not only regulates the levels of heme, which can be toxic in excess, but also produces biliverdin, a potent antioxidant, and carbon monoxide, which has signaling functions in various biological systems. Research on HMOX1 has gained momentum due to its involvement in various physiological and pathological conditions, including inflammation, oxidative stress, and cellular responses to injury. Additionally, HMOX1 is known for its cytoprotective properties, making it a potential therapeutic target for diseases such as cardiovascular disorders, neurodegenerative conditions, and cancer. The recombinant expression of HMOX1 provides a valuable tool for investigating its function and regulatory mechanisms, as well as for exploring potential therapeutic applications. By studying the biochemical characteristics and biological effects of recombinant HMOX1, researchers aim to understand its role in disease pathways and to develop novel strategies for clinical intervention. Overall, the exploration of HMOX1 and its recombinant protein forms holds significant promise in the fields of molecular biology, medicine, and therapeutic development, fostering a deeper understanding of its complex roles in human health and disease.
