Analytical Data
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Gene name
C1qC
- Application
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Alternative Names
C1qC；C1QG；Complement C1q subcomponent subunit C
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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
P02747
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Expression Region
1-245aa
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AA Sequence
MDVGPSSLPHLGLKLLLLLLLLPLRGQANTGCYGIPGMPGLPGAPGKDGY DGLPGPKGEPGIPAIPGIRGPKGQKGEPGLPGHPGKNGPMGPPGMPGVPG PMGIPGEPGEEGRYKQKFQSVFTVTRQTHQPPAPNSLIRFNAVLTNPQGD YDTSTGKFTCKVPGLYYFVYHASHTANLCVLLYRSGVKVVTFCGHTSKTN QVNSGGVLLRLQVGEEVWLAVNDYYDMVGIQGSDSVFSGFLLFPD
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Molecular Weight
52 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
C1q is a crucial component of the classical complement pathway, playing a vital role in immune responses by recognizing and binding to various immune complexes, apoptotic cells, and pathogens. C1q serves as an initiator for the complement cascade, leading to opsonization, inflammation, and cell lysis. The research on C1q and its recombinant forms (C1qC) has gained significant attention due to its potential therapeutic applications, particularly in autoimmune diseases, where dysregulation of complement activation often contributes to disease pathology. Understanding the structure and function of C1qC can lead to the development of novel immunomodulatory therapies, enhancing our ability to target specific components of the immune system. Furthermore, recombinant C1q proteins can be engineered to improve their stability and efficacy, making them useful tools for both basic research and clinical applications. Investigating the interaction of C1qC with various ligands and its effects on complement activation could provide valuable insights into its role in immune regulation and its potential in treating complement-related disorders. Overall, the study of C1qC represents a promising area of research in immunology, with implications for improving therapeutic strategies in a range of diseases.
