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2000
Volume 10, Issue 2
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

An N-terminal polypeptide (XVAX2-P104) of the XVAX2 protein, which is involved in controlling the dorsoventral patterning of the retina in Xenopus laevis, was expressed and purified as a Histagged fusion protein (pHis-XVAX2-P104), and it was employed to generate an anti-XVAX2 antibody in New Zealand white rabbits. ELISA analysis shows that the titer of the antibody is as high as ∼1:100,000. The antibody could specifically recognize the full-length XVAX2 protein in extracts of Xenopus embryos, as determined by Western Blotting.

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/content/journals/ppl/10.2174/0929866033479086
2003-04-01
2025-05-06
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  • Article Type:
    Review Article
Keyword(s): anti-XVAX2; N-terminal polypeptide; Recombinant; Xenopus Laevis; Xvax2 Peptide
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