Analytical Data
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Gene name
CFHR5
- Application
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Alternative Names
CFHL5; FHR-5; FHR5
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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
Q9BXR6
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Expression Region
Glu19~Glu569
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Molecular Weight
66kDa
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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
CFHR5 (Complement Factor H-Related 5) is a key protein involved in the regulation of the complement system, which plays a critical role in the immune response and maintaining homeostasis. Abnormalities in CFHR5 have been associated with various renal diseases, particularly those linked to atypical hemolytic uremic syndrome (aHUS) and age-related macular degeneration (AMD). Research into CFHR5 recombinant proteins has gained traction in recent years, owing to the need for better understanding its function and its role in disease pathology. The manipulation and characterization of CFHR5 enable scientists to investigate its interactions with other complement components and its impact on immune activation and regulation. Furthermore, studying CFHR5 can provide insights into the molecular mechanisms underlying complement dysregulation, which is crucial for the development of targeted therapies for related disorders. As protein engineering techniques have advanced, producing recombinant CFHR5 has become more feasible, allowing for detailed biochemical assays and structural studies. These investigations are not only essential for elucidating CFHR5's physiological roles but also for exploring its potential as a biomarker or therapeutic target in complement-related diseases.
