公开(公告)号：US20210261629A1

公开(公告)日：2021-08-26

申请号：US17267891

申请日：2019-08-08

申请人： TOSOH CORPORATION ,  SAGAMI CHEMICAL RESEARCH INSTITUTE

发明人： Masahiro HAYASHI ,  Takahiro MARUYAMA ,  Hiroyuki ITO ,  Aya ASAGOSHI ,  Kouta HATAYAMA ,  Megumi HOYA

IPC分类号： C07K14/195 ,  B01J20/24 ,  B01J20/30 ,  C12N5/09 ,  C07H1/06 ,  B01D15/38

摘要： The present invention aims to provide a fucose-binding protein that shows improved productivity in cases of expression in a host such as Escherichia coli, improved binding affinity to a fucose-containing sugar chain such as a sugar chain containing a structure composed of Fucα1-2Galβ1-3GlcNAc and/or Fucα1-2Galβ1-3GalNAc, and/or improved thermal stability. The above object is achieved by deleting a plurality of amino acid residues in the C-terminal side of the amino acid sequence of the fucose-binding protein BC2LCN of SEQ ID NO: 1, and, when necessary, substituting the glycine residue at position 36 in SEQ ID NO: 1 with a cysteine residue, substituting the glutamine residue at position 39 in SEQ ID NO: 1 with a leucine residue or methionine residue, substituting the glutamine residue at position 65 in SEQ ID NO: 1 with a leucine residue, substituting the cysteine residue at position 72 in SEQ ID NO: 1 with a glycine residue or alanine residue, substituting the glutamic acid residue at position 81 in SEQ ID NO: 1 with a cysteine residue, glutamine residue, histidine residue, or methionine residue, and/or substituting the glycine residue identified as the residue at position 36 in SEQ ID NO: 1 with a cysteine residue.

公开(公告)号：US20190233499A1

公开(公告)日：2019-08-01

申请号：US16335519

申请日：2017-09-21

申请人： TOSOH CORPORATION ,  SAGAMI CHEMICAL RESEARCH INSTITUTE

发明人： Kouta HATAYAMA ,  Teruhiko IDE ,  Hiroyuki ITO ,  Yosuke TERAO ,  Naoki YAMANAKA ,  Satoshi ENDO

IPC分类号： C07K14/735 ,  C12N1/20 ,  C12P21/02 ,  C07K16/06 ,  C12N15/70 ,  C07K1/22

CPC分类号： C07K14/70535 ,  C07K1/22 ,  C07K16/065 ,  C12N1/20 ,  C12N15/70 ,  C12P21/02

摘要： The problem to be addressed by the present invention is to provide improved recombinant FcγRIIb and FcγRIIa that do not require refolding and exhibit high productivity and thermal stability, and to provide a method for producing the same. Said problem is solved by improved recombinant FcγRIIb comprising at least the amino acid residues of the extracellular domain of human FcγRIIb (No. 43 to No. 215 in UniProt No. P31994), wherein, in said amino acid residues, at least one amino acid substitution has occurred at a position corresponding to No. 82, 94, 98, 104, 105, or 139 in UniProt No. P31994. Said problem is also solved by improved recombinant FcγRIIa comprising at least the amino acid residues of the extracellular domain of human FcγRIIa (No. 34 to No. 206 in UniProt No. P12318-1), wherein, in said amino acid residues, at least one amino acid substitution has occurred at a position corresponding to No. 73, 85, 89, 95, 96, or 130 in UniProt No. P12318-1.