Human R-Spondin 1 / RSPO1 Protein, His Tag

Source : 

Human R-Spondin 1, His Tag (RS1-H4221) is expressed from human 293 cells (HEK293). It contains AA Ser 21 - Ala 263 (Accession # Q2MKA7-1).

 

Molecule : R-Spondin 1

 

Synonyms : RSPO1,CRISTIN3,FLJ40906,RP11-566C13.1,R-spondin-1

 

Format : Powder

 

Category : Bio-Markers & CD Antigens

 

Accession : NP_001033722.1

 

Storage : -20℃

 

Shipping condition : Powder,RT

 

Molecular Weight : 28.7 kDa

 

Characteristics :

This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 28.7 kDa. The protein migrates as 38-42 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

 

Endotoxin Level : Less than 1.0 EU per μg by the LAL method.

 

Buffer : PBS, pH7.4

 

Description :

R-spondin-1 is also known as Roof plate-specific Spondin 1 (RSPO1) and cysteinerich and single thrombospondin domain containing protein 3 (Cristin 3), which is a secreted protein which belongs to the R-Spondin family and encodes a secreted activator protein with two cystein-rich, furin-like domains and one thrombospondin type 1 domain. All Rspondins regulate Wnt/β-catenin signaling, but have distinct expression patterns. Like other R-Spondins, R-Spondin-1 contains two adjacent cysteinerich furinlike domains (aa 34-135) with one potential N-glycosylation site, followed by a thrombospondin (TSP1) motif (aa 147-207) and a region rich in basic residues (aa 211-263). Only the furinlike domains are needed for β-catenin stabilization. A putative nuclear localization signal at the C-terminus may allow some expression in the nucleus.

 

References :

(1) Chen, JZ. et al. ,2002, Mol Biol Rep. 2002;29:287.
(2) Kim, K.A. et al., 2006, Cell Cycle. 2006;5:23–26.
(3) Nam, J.S. et al., 2007, Gene Expr. Patterns 7, 306–312.
(4) Kazanskaya, O. et al., 2004, Dev. Cell 7:525.
(5) Kamata, T. et al., 2004, Biochim. Biophys. Acta 1676 (1): 51–62.
(6) Binnerts, M.E. et al., 2007, Proc. Natl. Acad. Sci. U.S.A. 104 (37): 14700–5.
(7) Wei, Q. et al., 2007, J Biol Chem 282:15903–15911.