Characterization of Recombinant Extracellular Domain of Human Interleukin-10 Receptor
نویسندگان
چکیده
منابع مشابه
Recombinant Expression of the Non-glycosylated Extracellular Domain of Human Transforming Growth Factorβ Type II Receptor Using the Baculovirus Expression System in Sf21 Insect Cells
Transforming growth factor beta (TGFβ1, β2, and β3) are 25 kDa disulfide-linked homodimers that regulate many aspects of cellular functions, consist of proliferation, differentiation, adhesion and extracellular matrix formation. TGFβs mediate their biological activities by binding of growth factor ligand to two related, functionally distinct, single-pass transmembrane receptor kinases, known as...
متن کاملConstruction of recombinant Pichia pastoris expressing single-chain antibody fragment against extracellular domain of EpCAM
Introduction: Epithelial cell adhesion molecule (EpCAM) is highly expressed on epithelial tumors. So, EpCAM is a valuable antigen for targeted therapy. Using monoclonal antibodies (mabs) is an attractive approach for targeted cancer therapy. Importantly, limitations of intact mabs including large size led to the development of antibody fragments such as single chain fragment variable (scfv). Pi...
متن کاملCloning, Expression and Characterization of Recombinant Human Fc Receptor Like 1, 2 and 4 Molecules
Background: The Fc receptor like (FCRL) molecules belong to the immunoglobulin (Ig) superfamily with potentially immunoregulatory <span style="font-va...
متن کاملCharacterization of the recombinant extracellular domains of human interleukin-20 receptors and their complexes with interleukin-19 and interleukin-20.
The soluble extracellular domains of human interleukin-20 (IL-20) receptors I and II (sIL-20R1 and sIL20R2), along with their ligands IL-19 and IL-20, were expressed in Drosophila S2 cells and purified to homogeneity. Formation of the receptor/receptor and ligand/receptor complexes was studied by size exclusion chromatography. Both ligands and soluble receptors were found to be monomeric in sol...
متن کاملPurification and characterization of the recombinant extracellular domain of human nerve growth factor receptor expressed in a baculovirus system.
To obtain the large quantities of the extracellular domain of the nerve growth factor receptor (NGF-R) necessary for structural analyses, we produced this protein in the baculovirus expression system. A cDNA coding for the extracellular domain of the human NGF-R was first introduced into transfer vector pVL941. Recombinant baculovirus was produced by cotransfecting Spodoptera frugiperda cells w...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.21.12906