Analytical Data
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Gene name
CFD
- Application
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Alternative Names
CFD；DF；PFD；Complement factor D
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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
P00746
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Expression Region
26-253aa
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AA Sequence
ILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGK VQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKAT LGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLD RATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSG SRVCGNRKKPGIYTRVASYAAWIDSVLA
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Molecular Weight
26 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
The study of recombinant proteins using Computational Fluid Dynamics (CFD) has gained significant traction in recent years, primarily due to their pivotal role in biotechnology and pharmaceutical applications. Recombinant proteins are artificially produced by inserting specific genes into host cells, allowing for the large-scale production of proteins with therapeutic or industrial importance. However, the process of producing these proteins often encounters challenges such as poor solubility, aggregation, and misfolding, which can hinder their efficacy. CFD provides a powerful tool for simulating and analyzing the fluid dynamics involved in the production and purification processes of recombinant proteins. By modeling how the proteins behave in various bioreactor conditions and purification setups, researchers can optimize these processes, enhance protein yield, and improve overall product quality. Additionally, CFD can aid in visualizing and understanding the interactions between proteins and their environments at a molecular level, contributing to the design of more efficient bioprocesses. As the demand for biopharmaceuticals continues to rise, the integration of CFD into recombinant protein research holds promise for accelerating the development and optimization of bioproduction strategies, thereby addressing the challenges inherent in the field and pushing the boundaries of what is achievable in protein engineering and biotechnology.
