Mouse R-Spondin 1 / RSPO1 Protein (His Tag)
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Mouse R-Spondin 1 / RSPO1 Protein (His Tag) PDF Download

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R-spondin homolog (Xenopus laevis) Protein Datasheet


R-Spondin 1 / RSPO1 Protein Price Inquiry ( Available Sizes )

R-Spondin 1 / RSPO1 Protein Product Information

Synonym : RP23-325M14.2, R-spondin, Rspondin
Protein Construction:

A DNA sequence encoding the full length of mouse RSPO1 (NP_619624.2) (Met 1-Gln 265) was fused with a polyhistidine tag at the C-terminus.

Source: Mouse
Expression Host: CHO Stable Cell

R-Spondin 1 / RSPO1 Protein QC Testing

Purity: > 95 % as determined by SDS-PAGE SDS-PAGE:

R-Spondin 1 / RSPO1 protein


Measured by its ability to induce activation of β-catenin response in a Topflash Luciferase assay using HEK293T human embryonic kidney cells.
The ED50 for this effect is typically 50-200 ng/ml in the presence of 50 ng/ml recombinant mouse Wnt3a.
Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
Stability: Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal: Ser 21
Molecular Mass:

The secreted recombinant mouse RSPO1 comprises 256 amino acids with a predicted molecular mass of 28.5 kDa. As a result of glycosylation, the apparent molecular mass of the protein is approximately 44 kDa in SDS-PAGE under reducing conditions.

Formulation: Lyophilized from sterile PBS, pH7.4.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.

R-Spondin 1 / RSPO1 Protein Usage Guide

Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

R-Spondin 1 / RSPO1 Protein Related Products & Topics

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Molecule Species Description //For Detailed Info. and Price------CLICK! Cat. No
RSPO1 Human RSPO1 Protein, Recombinant 11083-H08H
RSPO1 Human RSPO1 (aa 1-146) Protein, Recombinant 11083-H08H1
RSPO1 Mouse RSPO1 Protein, Recombinant 50316-M08H
RSPO1 Mouse R-Spondin 1 / RSPO1 Protein, Recombinant 50316-M08S


Molecule Application Description //For Detailed Info. and Price------CLICK! Cat. No
WB RSPO1 Antibody, Rabbit MAb 11083-R010
ELISA RSPO1 Antibody, Rabbit MAb 11083-R106
WB, ELISA Rabbit Polyclonal Antibody 11083-RP01
WB, ELISA Rabbit Polyclonal Antibody (Antigen Affinity Purified) 11083-RP02

R-Spondin 1 / RSPO1 Protein Description

R-Spondin 1 ( Roof plate-specific Spondin 1 ), also known as RSPO1 and Cristin 3, is a secreted protein which belongs to the R-Spondin family. The R-Spondin (RSPO) family of secreted proteins act as potent activators of the Wnt/beta-catenin signaling pathway. R-Spondin1 regulates cellular responsiveness to Wnt ligands by modulating the cell-surface levels of the coreceptor LRP6. R-Spondin1 activity critically depends on the presence of canonical Wnt ligands and LRP6. R-Spondin1 does not directly activate LRP6, it interferes with DKK1/Kremen-mediated internalization of LRP6 through an interaction with Kremen, resulting in increased LRP6 levels on the cell surface. Mature human R-Spondin1 is 27 kDa and 243 amino acids (aa) in length. It contains a cysteine-rich furin repeat domain followed by a type I TSP domain. This form is apparently retained intracellularly. Human R-Spondin1 shares 89%, 87%, 92%, 91%, 91%, and 89% aa identity with mouse, rat, equine, canine, caprine and bovine R-Spondin1, respectively. Human RSPO1 disruption results in a recessive syndrome characterized by XX sex reversal, palmoplantar hyperkeratosis and predisposition to squamous cell carcinoma of the skin. It has been shown that the complete female-to-male sex reversal is due to the absence of the testis-determining gene, SRY.


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  2. Capel, B., 2006, Nature genetics. 38 (11) :1233-4.
  3. Binnerts, ME. et al., 2007, Proc Natl Acad Sci. 104 (37): 14700-5.
  4. Wilhelm, D., 2007, Bioessays. 29 (4): 314-8.
  5. Zhao, J. et al., 2009, Proc Natl Acad Sci. 106 (7) :2331-6.