Analytical Data
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Gene name
Cfi
- Application
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Alternative Names
Cfi；IF；Complement factor I
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05156
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Expression Region
239-316aa
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AA Sequence
KACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGCAGFASVTQEETEILTADMDAERR
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Molecular Weight
43.4 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
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Protein Description
Cfi, or Cyclophilin A, is a well-studied protein known for its role as a peptidyl-prolyl isomerase and its involvement in various cellular functions, including protein folding, trafficking, and regulation of immune responses. Research on Cfi has gained momentum due to its implications in several diseases, particularly in HIV, where it aids viral replication by interacting with viral proteins. Furthermore, Cfi has been implicated in cancer progression, neurodegenerative diseases, and inflammation, highlighting its potential as a therapeutic target. Advances in molecular biology and structural biology techniques have paved the way for the detailed study of Cfi and its interactions within cellular pathways. The re-engineering of Cfi to create recombinant proteins has enabled scientists to explore its structural dynamics and functional mechanisms more thoroughly. By producing Cfi in heterologous systems, researchers can generate large quantities of the protein for functional assays and high-resolution structural analyses, facilitating a deeper understanding of its role in disease pathology and paving the way for the development of small-molecule inhibitors or other therapeutics aimed at modulating its activity. Investigating the various isoforms and post-translational modifications of Cfi could also shed light on its multifaceted roles within the cell. Overall, the study of Cfi as a recombinant protein represents a significant avenue in biomedical research, promising novel insights into its functions and potential therapeutic applications.
