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抗Human C1S 抗体:
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Human Polyclonal C1S Primary Antibody for WB - ABIN2801901 : Mackinnon, Carter, Smyth, Dunbar, Fothergill: Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence. in European journal of biochemistry / FEBS 1988 (PubMed) Show all 4 Pubmed References
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 (PubMed)
Periodontal Ehlers-Danlos Syndrome in at least the great majority of cases results from specific classes of heterozygous mutations in C1R (显示 C1R 抗体) and C1S.
C1q exists as the C1 complex (C1qC1r2C1s2), and C1q binding to ligands activates the C1r (显示 C1R 抗体)/C1s proteases. Incubation of nucleoli with C1 caused degradation of the nucleolar proteins nucleolin (显示 NCL 抗体) and nucleophosmin 1 (显示 NPM1 抗体). T
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 (显示 C1R 抗体)-C1s tetramer, to recognize physiological C1q ligands such as IgG and pentraxin 3 (显示 PTX3 抗体)
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 (显示 F2 抗体) 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 (显示 C1R 抗体) and C1s.
Detailed mapping of post-translational modifications and insights into the C1r (显示 C1R 抗体)/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.
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.
C1 esterase , complement C1s subcomponent , complement component 1 subcomponent s , complement component C1s , complement component 1, s subcomponent , complement C1s subcomponent-like , basic proline-rich peptide IB-1 , complement C1s-A subcomponent , complement component 1 subcomponent s-A , complement component C1SA , serine protease