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characterization of the optimized c2 domain of protein g: finding its additional chicken igy-binding ability.the c2 domain of streptococcal protein g is a small (55 residue) peptide with immunoglobulin-binding activity. following codon optimization, the gene was divided into four oligonucleotide fragments and amplified by overlap pcr. the recombinant plasmid pet30a-c2 was transformed into escherichia coli rosetta (de3) plyss for expression. after purification by ni-nta, the fusion protein was identified by western-blotting, dot-elisa and elisa. his-tagged c2 bound to human, rabbit, cattle, pig, goat, m ...201323690033
cloning, expression and antiviral bioactivity of red-crowned crane interferon-α.interferon-α (ifn-α) genes have been cloned from a variety of animals, but information regarding crane ifn-α has not been reported to date. in this study, we cloned a full-length red-crowned crane interferon-α (crifn-α) gene sequence consisting of a 486bp partial 5' utr, 741bp complete orf and 559bp partial 3' utr. this gene encodes a protein of 246 amino acids and shares 60 to 80% identity with avian ifn-α and less than 45% identity with mammalian ifn-α. the expression of crifn-α with an n-term ...201424768181
generation and characterization of polyclonal antibody against part of immunoglobulin constant heavy υ chain of goose.immunoglobulin y (abbreviated as igy) is a type of immunoglobulin that is the major antibody in bird, reptile, and lungfish blood. igy consists of two light (λ) and two heavy (υ) chains. in the present study, polyclonal antibody against igyfc was generated and evaluated. rigycυ3/cυ4 was expressed in escherichia coli, purified and utilized to raise polyclonal antibody in rabbit. high affinity antisera were obtained, which successfully detected the antigen at a dilution of 1:204,800 for elisa assa ...201425171010
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