Analytical Data
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Gene name
C4BPb
- Application
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Alternative Names
C4BP-B; C4-BP; Complement Component 4 Binding Protein, Beta
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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
P20851
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Expression Region
Ser18~Leu252
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Molecular Weight
31kDa
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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
C4b-binding protein (C4BPb) is a crucial regulatory protein involved in the complement system, which plays a significant role in the immune response. Research on C4BPb has gained attention due to its dual function as a regulator of complement activation and as a carrier of vitamin K-dependent proteins. It is primarily known for binding to activated C4b, thereby preventing excessive complement activation that can lead to tissue damage and inflammatory diseases. Given its significant involvement in various pathological conditions, including autoimmune diseases, infections, and cancer, understanding the structure, function, and interactions of C4BPb is essential for elucidating its role in human health and disease. Advances in recombinant protein technology have facilitated the production of C4BPb, allowing researchers to investigate its biochemical properties and develop potential therapeutic applications. Studies on C4BPb not only enhance our understanding of the complement system but also pave the way for innovative strategies in managing diseases that involve complement dysregulation. As such, further exploration of C4BPb's mechanism of action and its interactions with other complement components and immune regulators remains a vital area of research in immunology and therapeutic development.
