Analytical Data
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Gene name
C1qA
- Application
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Alternative Names
C1qA；Complement C1q subcomponent subunit A
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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
P02745
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Expression Region
23-245aa
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AA Sequence
EDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIRTGIQGLKGDQGEPGPSGNPGKVGYPGPSGPLGARGIPGIKGTKGSPGNIKDQPRPAFSAIRRNPPMGGNVVIFDTVITNQEEPYQNHSGRFVCTVPGYYYFTFQVLSQWEICLSIVSSSRGQVRRSLGFCDTTNKGLFQVVSGGMVLQLQQGDQVWVEKDPKKGHIYQGSEADSVFSGFLIFPSA
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Molecular Weight
30.7 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
C1qA, a crucial component of the complement system, plays a significant role in innate immunity as it initiates the classical pathway for complement activation. The complement system is vital for immune surveillance, promoting opsonization, inflammation, and cell lysis, thereby aiding in pathogen clearance and maintaining homeostasis. Research has increasingly focused on C1qA due to its involvement not only in immune response but also in various pathological conditions, including autoimmune diseases and neurodegenerative disorders. Understanding the structure-function relationship of C1qA can elucidate its mechanisms and regulatory roles in immunity. Recombinant C1qA proteins have been developed to study these properties in vitro and in vivo, offering potential therapeutic applications for diseases characterized by complement dysregulation. The advancement of recombinant DNA technology facilitates the production of C1qA with specific modifications, enabling detailed exploration of its functional domains and interactions with other complement components and immune cells. This research not only enhances the understanding of complement biology but also opens avenues for novel treatment strategies targeting complement-mediated diseases.
