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Periodontal Ehlers-Danlos Syndrome in at least the great majority of cases results from specific classes of heterozygous mutations in C1R and C1S (show C1S Proteins).
We confirmed increased levels of C1R and VTN (show VTN Proteins) in sera from patients with Joint hypermobility syndrome by western blot analyses
C1q exists as the C1 complex (C1qC1r2C1s2), and C1q binding to ligands activates the C1r/C1s (show C1S Proteins) proteases. Incubation of nucleoli with C1 caused degradation of the nucleolar proteins nucleolin (show NCL Proteins) and nucleophosmin 1 (show NPM1 Proteins). T
C1r specificity is well suited to its cleavage targets and that efficient cleavage of C1s (show C1S Proteins) is achieved through both active site and exosite contributions.
Analysis of its interaction properties by surface plasmon resonance shows that rC1q retains the ability of serum C1q to associate with the C1s (show C1S Proteins)-C1r-C1r-C1s (show C1S Proteins) tetramer, to recognize physiological C1q ligands such as IgG and pentraxin 3 (show PTX3 Proteins)
a structural rearrangement as a switch between functional states of human C1r
These results provide further structural insights into the architecture of the C1 complex, and the interactions between C1r and C1s (show C1S Proteins).
The modular C1r protein is the first protease activated in the classical complement pathway, a key component of innate immunity.
Detailed mapping of C1q post-translational modifications and insights into the C1r/C1s (show C1S Proteins) binding sites.
Using a recombinant CUB2-CCP1 (show AGTPBP1 Proteins) domain pair and the individual CCP1 (show AGTPBP1 Proteins) module, we showed that binding of Ca(2 (show CA2 Proteins)+) induces the folding of the CUB2 domain and stabilizes its structure.
C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system.
complement C1r subcomponent
, complement C1r
, complement component 1, r subcomponent
, complement component 1 subcomponent r