Recombinant Rat Complement factor I(Cfi) Reference: CSB-BP005279RA_500 Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha-chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins. Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces. The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired complement activation, while in apoptotic cells or microbes, the absence of such cofactors leads to C3b-mediated complement activation and subsequent opsonization.
Recombinant Rat Complement factor I(Cfi) Reference: CSB-BP005279RA_100 Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha-chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins. Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces. The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired complement activation, while in apoptotic cells or microbes, the absence of such cofactors leads to C3b-mediated complement activation and subsequent opsonization.
Recombinant Rat Complement factor I(Cfi) Reference: CSB-BP005279RA_20 Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha-chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins. Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces. The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired complement activation, while in apoptotic cells or microbes, the absence of such cofactors leads to C3b-mediated complement activation and subsequent opsonization.
Recombinant Tetronarce californica Acetylcholine receptor subunit... Reference: CSB-BP005386TOT_1 After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Recombinant Tetronarce californica Acetylcholine receptor subunit... Reference: CSB-BP005386TOT_100 After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Recombinant Tetronarce californica Acetylcholine receptor subunit... Reference: CSB-BP005386TOT_20 After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Recombinant Human Neuronal acetylcholine receptor subunit... Reference: CSB-BP005389HU1_500 Bordetella pertussis is the causative agent of whooping cough. An essential step in the disease process is the attachment of the bacteria to the ciliated epithelium of the respiratory tract, enabling the organism to resist normal host-clearance mechanisms. It is unclear which bacterial cell surface component are responsible for adherence but the fimbriae of B.pertussis are prime candidates for being involved in this process.
Recombinant Human Neuronal acetylcholine receptor subunit... Reference: CSB-BP005389HU1_100 Bordetella pertussis is the causative agent of whooping cough. An essential step in the disease process is the attachment of the bacteria to the ciliated epithelium of the respiratory tract, enabling the organism to resist normal host-clearance mechanisms. It is unclear which bacterial cell surface component are responsible for adherence but the fimbriae of B.pertussis are prime candidates for being involved in this process.
Recombinant Human Neuronal acetylcholine receptor subunit... Reference: CSB-BP005389HU1_20 Bordetella pertussis is the causative agent of whooping cough. An essential step in the disease process is the attachment of the bacteria to the ciliated epithelium of the respiratory tract, enabling the organism to resist normal host-clearance mechanisms. It is unclear which bacterial cell surface component are responsible for adherence but the fimbriae of B.pertussis are prime candidates for being involved in this process.
Recombinant Human Cartilage intermediate layer protein 1(CILP),partial Reference: CSB-BP005437HU_500 Probably plays a role in cartilage scaffolding. May act by antagonizing TGF-beta1 (TGFB1) and IGF1 functions. Has the ability to suppress IGF1-induced proliferation and sulfated proteoglycan synthesis, and inhibits ligand-induced IGF1R autophosphorylation. May inhibit TGFB1-mediated induction of cartilage matrix genes via its interaction with TGFB1. Overexpression may lead to impair chondrocyte growth and matrix repair and indirectly promote inorganic pyrophosphate (PPi) supersaturation in aging and osteoarthritis cartilage.
Recombinant Human Cartilage intermediate layer protein 1(CILP),partial Reference: CSB-BP005437HU_100 Probably plays a role in cartilage scaffolding. May act by antagonizing TGF-beta1 (TGFB1) and IGF1 functions. Has the ability to suppress IGF1-induced proliferation and sulfated proteoglycan synthesis, and inhibits ligand-induced IGF1R autophosphorylation. May inhibit TGFB1-mediated induction of cartilage matrix genes via its interaction with TGFB1. Overexpression may lead to impair chondrocyte growth and matrix repair and indirectly promote inorganic pyrophosphate (PPi) supersaturation in aging and osteoarthritis cartilage.
Recombinant Human Cartilage intermediate layer protein 1(CILP),partial Reference: CSB-BP005437HU_20 Probably plays a role in cartilage scaffolding. May act by antagonizing TGF-beta1 (TGFB1) and IGF1 functions. Has the ability to suppress IGF1-induced proliferation and sulfated proteoglycan synthesis, and inhibits ligand-induced IGF1R autophosphorylation. May inhibit TGFB1-mediated induction of cartilage matrix genes via its interaction with TGFB1. Overexpression may lead to impair chondrocyte growth and matrix repair and indirectly promote inorganic pyrophosphate (PPi) supersaturation in aging and osteoarthritis cartilage.