Analytical Data
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Gene name
Complement factor I
- Application
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Alternative Names
C3B/C4B inactivator (If)
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Species
Rat
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Source
Baculovirus
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9WUW3
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Expression Region
19-604aa
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Molecular Weight
69.2
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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
Complement factor I (CFI) is a key regulatory protein in the complement system, which plays a crucial role in innate immunity by controlling the activation of complement pathways. Dysregulation of CFI activity is associated with various immune disorders, including autoimmune diseases and increased susceptibility to infections. Understanding the molecular mechanisms underlying CFI function is essential for developing therapeutic interventions aimed at modulating the complement system. The recombination of CFI protein allows for detailed structural and functional studies, facilitating insights into its enzymatic activity and interactions with other complement components. Moreover, recombinant CFI is valuable for experimental applications, including in vitro assays and potential therapeutic uses in complement-related diseases. Research in this area aims to enhance our understanding of CFI’s role in immune regulation and its potential as a target for novel treatments, particularly in conditions where complement dysregulation contributes to pathology. The ongoing investigations into the recombinant expression, purification, and characterization of CFI are critical for advancing our knowledge of complement biology and improving clinical outcomes for patients with complement-mediated diseases.
