Rspondin 1 Recombinant Protein His Tag Lyophilized from Innovative Research has been recombinantly produced in HEK293 cells. This is a Lyophilized protein buffered in PBS, pH7.4 with a purity of >95% as determined by SDS-PAGE..

More Details:

• Species: Human
• Target: RSPO1
• Purity: >95% as determined by SDS-PAGE.
• Source: HEK293 cells
• Storage Conditions: Lyophilized Protein should be stored at -20°C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20°C or -70°C. Avoid repeated freeze-thaw cycles.

Additional Information:

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/?-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 ?-catenin stabilization. A putative nuclear localization signal at the C-terminal may allow some expression in the nucleus.

This recombinant protein can be used for WB. For research use only.. At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.

This material is sold for in-vitro use only for manufacturing and research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herin are offered for informational purposes only to be used solely for your consideration, investigation, and verification.

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