Analytical Data
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Gene name
Haptoglobin
- Application
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Alternative Names
Liver regeneration-related protein LRRG173Zonulin
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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 90% as determined by SDS-PAGE.
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Uniprot
P06866
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Expression Region
19-346aa
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Molecular Weight
40.5 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
Haptoglobin is a crucial plasma protein that binds free hemoglobin released during hemolysis, preventing its oxidative damage and facilitating its clearance by macrophages. This protein exists in various genetic polymorphisms, with distinct isoforms exhibiting different functional properties. The study of recombinant haptoglobin has gained prominence due to its potential therapeutic applications in conditions such as hemolytic anemia, sepsis, and chronic inflammatory diseases, where free hemoglobin levels are elevated. Advancements in recombinant DNA technology have enabled the production of haptoglobin isoforms with controlled properties, allowing researchers to investigate their specific roles in oxidative stress responses and immune modulation. Furthermore, the characterization of recombinant haptoglobin can provide insights into its protective mechanisms against kidney injury and organ dysfunction related to hemolysis. High-throughput screening and structural studies of these isoforms may reveal new avenues for drug development. As such, the study of recombinant haptoglobin not only enhances our understanding of its biological function but also holds promise for innovative therapeutic strategies targeting diseases associated with hemolysis and oxidative damage.
