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Identification, expression, and purification of a unique stable domain from human HSPC144 protein.

Abstract：

:HSPC144 is a newly identified gene in human CD34(+) hematopoietic stem/progenitor cells. In this work, we have expressed and purified the 225-residue protein from Escherichia coli BL21 (DE3) and identified a stable fragment HSPC144-P (residues 44-225) by limited proteolysis method. The HSPC144-P fragment exhibits high stability with a little increase of secondary structure percentage as compared with the full-length protein. We anticipated that the N-terminally truncated protein possesses a more compact structure. By sequence analysis, the proteolytic fragment shares a great similarity with DUF589 domain, a previously identified domain with unknown function. This novel domain is highly conserved in Thy28 proteins and is worthy of structural and functional studies. We have subcloned this homologous domain from HSPC144 protein and purified to homogeneity for structure analysis. The (15)N and (15)N/(13)C-labeled DUF589 domain samples have been prepared successfully and determination of the NMR structure is in progress.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Song AX,Chang YG,Gao YG,Lin XJ,Shi YH,Lin DH,Hang QH,Hu HY

doi

10.1016/j.pep.2005.03.008

keywords:

subject

Has Abstract

pub_date

2005-07-01 00:00:00

pages

146-52

issue

1

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(05)00082-3

journal_volume

42

pub_type

杂志文章

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