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Purification and characterization of the extracellular region of human receptor tyrosine kinase like orphan receptor 2 (ROR2).

Abstract：

:Receptor tyrosine kinase like orphan receptor 2 (ROR2) is a co-receptor for some Wnt proteins including Wnt5a that activate the noncanonical Wnt/planar cell polarity (PCP) signaling pathway. Upregulation of ROR2 is associated with several cancer forms. The extracellular region of ROR2, which contains an immunoglobulin (Ig)-like domain, a Frizzled like cysteine-rich domain (CRD) and a Kringle domain, is a potential anticancer drug target. The structural and biochemical properties of the ROR2 extracellular region remain largely unexplored. Here we describe the mapping and purification, using a baculovirus - insect cell system, of a near-full-length ROR2 extracellular fragment (residues 53-402), which is well-behaved and suitable for future structural and biochemical analysis. We show that the extracellular region of ROR2 per se is monomeric in solution. Different monoclonal antibodies raised against the purified ROR2 protein can specifically recognize the protein and can either inhibit or activate the PCP activity in a cell-based assay, and are thus potentially useful for future mechanistic and therapeutic/diagnostic studies. The biological relevance of these antibodies further demonstrates that the purified recombinant ROR2 protein is properly folded and biochemically active.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Li Y,Han X,Xu W,Rao Z,Li X

doi

10.1016/j.pep.2019.02.015

subject

Has Abstract

pub_date

2019-06-01 00:00:00

pages

74-80

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(19)30039-7

journal_volume

158

pub_type

杂志文章

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