Analytical Data
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Gene name
C4BPa
- Application
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Alternative Names
C4BPa；C4BP；C4b-binding Protein alpha chain
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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
P04003
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Expression Region
49-597aa
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AA Sequence
NCGPPPTLSFAAPMDITLTETRFKTGTTLKYTCLPGYVRSHSTQTLTCNSDGEWVYNTFCIYKRCRHPGELRNGQVEIKTDLSFGSQIEFSCSEGFFLIGSTTSRCEVQDRGVGWSHPLPQCEIVKCKPPPDIRNGRHSGEENFYAYGFSVTYSCDPRFSLLGHASISCTVENETIGVWRPSPPTCEKITCRKPDVSHGEMVSGFGPIYNYKDTIVFKCQKGFVLRGSSVIHCDADSKWNPSPPACEPNSCINLPDIPHASWETYPRPTKEDVYVVGTVLRYRCHPGYKPTTDEPTTVICQKNLRWTPYQGCEALCCPEPKLNNGEITQHRKSRPANHCVYFYGDEISFSCHETSRFSAICQGDGTWSPRTPSCGDICNFPPKIAHGHYKQSSSYSFFKEEIIYECDKGYILVGQAKLSCSYSHWSAPAPQCKALCRKPELVNGRLSVDKDQYVEPENVTIQCDSGYGVVGPQSITCSGNRTWYPEVPKCEWETPEGCEQVLTGKRLMQCLPNPEDVKMALEVYKLSLEIEQLELQRDSARQSTLDKEL
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Molecular Weight
63.7kDa
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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
C4BPa, or complement component 4 binding protein alpha, is a crucial regulatory protein involved in the complement system, an integral part of the immune response. It exists as a hetero-oligomeric complex that plays a significant role in modulating inflammation and immune responses by binding to and inactivating complement proteins, particularly C4b and C3b. The dysregulation of C4BPa has been associated with various pathological conditions, including autoimmune diseases, infections, and cardiovascular diseases, highlighting its potential as a therapeutic target. Recent studies have focused on the recombinant expression of C4BPa to better understand its structural and functional properties. Researchers aim to characterize the protein’s binding interactions and regulatory mechanisms, providing insights into its role in immune regulation. Understanding C4BPa's structure-function relationship could pave the way for novel therapeutic interventions, including the development of drugs that mimic or inhibit its activity to enhance immune responses in disease contexts. Additionally, the recombinant version of C4BPa offers a tool for further investigation into the complement system's dynamics, with the potential for application in diagnostic and therapeutic settings. Researchers are also exploring the implications of C4BPa in various diseases, making it a focal point for studies aimed at unraveling the complexities of immune regulation and the development of targeted therapies. Overall, ongoing research into C4BPa not only contributes to our understanding of complement regulation but also holds promise for advancing immune-related therapies and improving patient outcomes in a range of diseases.
