Recombinant Human C1QA protein
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Recombinant Human C1QA protein is a Human Full Length protein, in the 23 to 245 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
Complement C1q subcomponent subunit A, C1QA
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human C1QA protein (AB157982)
ab157982 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
C1QA interacts with pathogens and modified host cells to trigger the complement cascade. This starts the activation of the classical pathway which enhances immune responses. C1QA together with C1QB and C1QC binds to Fc regions of antibodies attached to antigens. This binding leads to the subsequent activation of C1r and C1s proteases facilitating opsonization and clearance of immune complexes and apoptotic cells.
Pathways
The synthesis of C1QA plays an important role in the classical complement pathway and is part of the innate immunity. C1QA collaborates with proteins like C1QB and C1QC in this pathway. This pathway bridges innate and adaptive immunity by assisting in the removal of pathogens and cell debris. It also relates to the coagulation pathway where its activity can influence inflammation and tissue repair processes.
Specifications
Form
Liquid
General info
Function
C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
Post-translational modifications
O-linked glycans are assumed to be the Glc-Gal disaccharides typically found as secondary modifications of hydroxylated lysines in collagen-like domains.
Target data
Complementary Products
Product promise
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