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Purification and characterization of a recombinant human IgE Fcε fragment lacking the C4 domain
[摘要]

Complementary DNA of human lgE Icε fragment (residues 226–480) lacking the Cϕ domain was expressed in Escherichia coli and the product was purified by immunoaffinity chromatography on a monoclonal antibody (E12 0.02)-Affi-Gel 10 column. About 1.8 mg of an apparent dimer and 5.9 mg of a monomer were obtained from 65 g E. coli cells with 9.3% recovery. The purified products were found to lack more than half of the COOH-terminal portion of the Cε3 domain. The apparent dimer showed high immunological specific activity (3.6 × 106 U/mg protein) comparable to that of natural human IgE when measured by commercial human IgE determination kits.

[发布日期]  [发布机构] 
[效力级别]  [学科分类] 生物化学/生物物理
[关键词] Recombinant IgE Fcε fragment;Immunoaffinity chromatography;(Escherichia coli);FcεR;Fc receptor for IgE;PBS;phosphate-buffered saline;SDS-PAGE;SDS-polyacrylamide gel electrophoresis [时效性] 
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