Analytical Data
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Gene name
HPR
- Application
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Alternative Names
HP
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Species
Human
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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
P00739
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Expression Region
Ser30~Pro85
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Molecular Weight
8kDa
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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
HPR (haptoglobin-related protein) is a member of the hemoglobin scavenger family, playing a key role in the immune response and tissue protection during hemolysis. Research on HPR has gained momentum due to its potential implications in various diseases, particularly those associated with inflammation and oxidative stress. Elevated levels of HPR have been linked to conditions such as cardiovascular diseases and certain cancers, suggesting its role as a biomarker for disease progression. The recombinant production of HPR allows for detailed functional studies and therapeutic applications, including its use in drug development and understanding its protective mechanisms at the cellular level. Advances in protein engineering techniques have enhanced our ability to produce a stable and active form of HPR, facilitating investigations into its structure-function relationships. Furthermore, the exploration of HPR's interaction with hemoglobin and other plasma proteins is crucial for elucidating its biological significance. As the understanding of its role in pathophysiology expands, HPR is being studied not only for its diagnostic potential but also for its therapeutic avenues in managing diseases characterized by dysregulated hemoglobin levels. Overall, the research on recombinant HPR is poised to contribute significantly to both fundamental biology and clinical medicine.
