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Structural and Functional Characterization of a Single-Chain Form of . . . We report here, the first production of a single-chain recombinant form of human C1q globular region (C1q-scGR) The three monomers have been linked in tandem to generate a single continuous polypeptide, based on a strategy previously used for adiponectin, a protein structurally related to C1q
Structural and Functional Characterization of a Single-Chain Form of . . . We report here, the first production of a single-chain recombinant form of human C1q globular region (C1q-scGR) The three monomers have been linked in tandem to generate a single continuous polypeptide, based on a strategy previously used for adiponectin, a protein structurally related to C1q
structural and functional characterization of a single-chain form of . . . The three monomers have been linked in tandem to generate a single continuous polypeptide, based on a strategy previously used for adiponectin, a protein structurally related to C1q The resulting C1q-scGR protein was produced at high yield in stably transfected 293-F mammalian cells
Structural and functional anatomy of the globular domain of complement . . . C1q is the first subcomponent of the classical pathway of the complement system and a major connecting link between innate and acquired immunity As a versatile charge pattern recognition molecule, C1q is capable of engaging a broad range of ligands
Frontiers We report here the first production of a single-chain recombinant form of human C1q globular region (C1q-scGR) The three monomers have been linked in tandem to generate a single continuous polypeptide, based on a strategy previously used for adiponectin, a protein structurally related to C1q
Structural and functional characterization of a single-chain form of . . . Complement C1q is a soluble pattern recognition molecule comprising six heterotrimeric subunits assembled from three polypeptide chains (A, B, and C) Each heterotrimer forms a collagen-like stem prolonged by a globular recognition domain
Functional and Structural Characterization of a Potent C1q Inhibitor . . . Abstract The classical pathway of complement is important for protection against pathogens and in maintaining tissue homeostasis, but excessive or aberrant activation is directly linked to numerous pathologies We describe the development and in vitro characterization of C1qNb75, a single domain antibody (nanobody) specific for C1q, the pattern recognition molecule of the classical pathway
RCSB PDB - 5HKJ: Single Chain Recombinant Globular Head of the . . . We report here, the first production of a single-chain recombinant form of human C1q globular region (C1q-scGR) The three monomers have been linked in tandem to generate a single continuous polypeptide, based on a strategy previously used for adiponectin, a protein structurally related to C1q