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anti-Human C1S Antibodies:
anti-Mouse (Murine) C1S Antibodies:
anti-Rat (Rattus) C1S Antibodies:
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Human Monoclonal C1S Primary Antibody for IA, IHC (fro) - ABIN2191986
Matsumoto, Nagaki, Kitamura, Kuramitsu, Nagasawa, Seya: Probing the C4-binding site on C1s with monoclonal antibodies. Evidence for a C4/C4b-binding site on the gamma-domain. in Journal of immunology (Baltimore, Md. : 1950) 1989
Human Polyclonal C1S Primary Antibody for IHC, IHC (p) - ABIN4299881
Boufaied, Takhar, Nash, Erho, Bismar, Davicioni, Thomson: Development of a predictive model for stromal content in prostate cancer samples to improve signature performance. in The Journal of pathology 2019
The serine protease domains of C1r and C1s are at the periphery of the C1r2s2 tetramer both when alone or within the nonactivated C1 complex. The C1 complex adopts a conformation incompatible with intramolecular activation of C1. Instead, intermolecular proteolytic activation between neighboring C1 complexes bound to a complement-activating surface occurs. Many structurally unrelated molecular patterns can activate C1.
Periodontal Ehlers-Danlos Syndrome in at least the great majority of cases results from specific classes of heterozygous mutations in C1R and C1S.
C1q exists as the C1 complex (C1qC1r2C1s2), and C1q binding to ligands activates the C1r/C1s proteases. Incubation of nucleoli with C1 caused degradation of the nucleolar proteins nucleolin and nucleophosmin 1. T
TNT003, an inhibitor of the serine protease C1s, prevents complement activation induced by cold agglutinins.
Data indicate that complement C1s mRNA level was low in ICR-derived glomerulonephritis (ICGN) mice liver as compared with age-matched ICR mice.
Analysis of its interaction properties by surface plasmon resonance shows that rC1q retains the ability of serum C1q to associate with the C1s-C1r-C1r-C1s tetramer, to recognize physiological C1q ligands such as IgG and pentraxin 3
A molecular switch governs the interaction between the human complement protease C1s and its substrate, complement C4.
Four positively charged amino acids on the serine protease domain appear to form a catalytic exosite that is required for efficient cleavage of C4 in the classical pathway of complement.
These results provide further structural insights into the architecture of the C1 complex, and the interactions between C1r and C1s.
Detailed mapping of post-translational modifications and insights into the C1r/C1s binding sites.
Interaction with the prime side residues at the cleavage point in C1s enhances the affinity of the enzyme for complement 2 and complement 4 substrates; these prime subsite residues mediate positive cooperativity in the cleavage of the substrate.
full specificity of the enzyme using a randomized phage display library
There are splice variants of C1s mRNA transcripts in normal human cells
C1r and this gene are duplicated in mice; differential expression generates alternative isomorphs in the liver and in the male reproductive system.
This gene encodes a serine protease, which is a major constituent of the human complement subcomponent C1. C1s associates with two other complement components C1r and C1q in order to yield the first component of the serum complement system. Defects in this gene are the cause of selective C1s deficiency.
, basic proline-rich peptide IB-1
, complement C1s subcomponent
, complement component 1 subcomponent s
, complement C1s-A subcomponent
, complement component 1 subcomponent s-A
, complement component C1SA
, serine protease
, complement component C1s
, complement component 1, s subcomponent
, complement C1s subcomponent-like