Analytical Data
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Gene name
Hemopexin
- Application
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Alternative Names
Haemopexin; Beta-1B-glycoprotein
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P20059
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Expression Region
Glu31~Thr242
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Molecular Weight
32kDa
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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
Hemopexin is a plasma glycoprotein primarily involved in heme transport and metabolism. It plays a crucial role in the body's response to oxidative stress and inflammation by binding free heme and facilitating its removal, thereby preventing tissue damage. Given its protective functions, recombinant hemopexin has gained attention in biomedical research and therapeutic development. Studies have shown its potential applications in treating conditions associated with heme toxicity, such as hemolytic anemia and certain neurodegenerative diseases. Additionally, hemopexin’s anti-inflammatory properties suggest its usefulness in managing various inflammatory disorders. The recombinant form of hemopexin allows for controlled studies of its biological functions and therapeutic effects, thereby enhancing our understanding of its mechanism of action and paving the way for novel treatment strategies. Furthermore, the advancement of recombinant protein technology facilitates the production of hemopexin in sufficient quantities for clinical research, enabling the exploration of its role in disease modulation and potential utility in precision medicine. Research into hemopexin not only highlights its physiological significance but also opens avenues for innovative therapeutic interventions that could improve patient outcomes in diseases characterized by heme overload and related inflammatory processes.
