This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 27.6 kDa. The protein migrates as 40 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
RSPO1
Spezies: Human
Wirt: HEK-293 Cells
Recombinant
The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
RSPO1
Spezies: Ratte
Wirt: Escherichia coli (E. coli)
Recombinant
> 97 %
WB, SDS, Imm, PC
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Buffer
PBS, pH 7.4
Handhabung
Please avoid repeated freeze-thaw cycles.
Lagerung
-20 °C
Informationen zur Lagerung
No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
Park, Choi, Kim, Cheong, Jeong: "AhR activation by 6-formylindolo[3,2-b]carbazole and 2,3,7,8-tetrachlorodibenzo-p-dioxin inhibit the development of mouse intestinal epithelial cells." in: Environmental toxicology and pharmacology, Vol. 43, pp. 44-53, (2017) (PubMed).
Das, Png, Oancea, Hasnain, Lourie, Proctor, Eri, Sheng, Crane, Florin, McGuckin: "Glucocorticoids alleviate intestinal ER stress by enhancing protein folding and degradation of misfolded proteins." in: The Journal of experimental medicine, Vol. 210, Issue 6, pp. 1201-16, (2013) (PubMed).
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.