Preparation and Analysis of Biological Activity of the Secreted
Proteins of the Noggin Family

F. M. Eroshkin, A. V. Bairamov, O. V. Aver’yanova, E. A. Solov’eva,
M. V. Serebryakova, A. G. Zaraiskii, and N. Yu. Martynova¹

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences,
ul. Miklukho-Maklaya 16/10, Moscow, 117997 Russia

Received November 2, 2012; in final form, November 7, 2012

Abstract—Methods for preparation of recombinant physiologically active proteins of the Noggin family
(Noggin1 and Noggin2) of the clawed frog Xenopus laevis that are capable of interaction with BMP factors of
the TGF-beta superfamily have been developed. Structures were designed for the expression of Noggin1 and
Noggin2 proteins allowing us to produce them from the directly microinjected synthetic mRNA in the cells of
developing embryos of the clawed frog, as well as in the prokaryotic expression system. Target proteins con-
tained three Myc-epitopes at the N-terminal. Introduction of these ‘tags’ allowed comparison of the expression
level of the Noggin1 and Noggin2 proteins, isolation on the affinity immunosorbent, and demonstration of bio-
logical activity of the isolated Noggin-proteins through the analysis of their ability to bind the BMP4 factor of
the TGF-beta superfamily with coimmunoprecipitation method.

Keywords: Noggin1, Noggin2, signaling cascade, luciferase reporter, embryogenesis

DOI: 10.1134/S1068162013020040

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