Recombinant Human RSPO1 Protein (His Tag)

Name: Recombinant Human RSPO1 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-4097
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	NP_001033722.1
Synonym	CRISTIN3, R-Spondin 1, RSPO
Background	RSPO1 gene is a member of the R-spondin family. It encodes RSPO1 which is known as a secreted activator protein with two cystein-rich, furin-like domains and one thrombospondin type 1 domain. In mice, RSPO1 induces the rapid onset of crypt cell proliferation and increases intestinal epithelial healing, providing a protective effect against chemotherapy-induced adverse effects. This protein is an activator of the beta-catenin signaling cascade, leading to TCF-dependent gene activation. RSPO1 acts both in the canonical Wnt/beta-catenin-dependent pathway and in non-canonical Wnt signaling pathway, probably by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. It also acts as a ligand for frizzled FZD8 and LRP6.
Description	A DNA sequence encoding the human RSPO1 (NP_001033722.1) (Met 1-Ala 263) was expressed, fused with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Ser 21
AA Sequence	Met 1-Ala 263
Molecular Weight	The secreted recombinant human RSPO1 comprises 254 a.a. with a predicted molecular mass of 28.2 kDa. As a result of glycosylation, rhRSPO1 migrates as an approximately 42 kDa band in SDS-PAGE under reducing conditions.
Purity	>95% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	1. Measured by its binding ability in a functional ELISA. Immobilized human RSPO1 at 20 ug/ml (100 ul/well) can bind human LIMPII with a linear ranger of 32-800 ng/ml.2. Measured by its binding ability in a functional ELISA. Immobilized human RSPO1 at 20 ug/ml (100 ul/well) can bind mouse CD36 with a linear ranger of 6.4-800 ng/ml.3. Measured by its ability to induce activation of βcatenin response in a Topflash Luciferase assay using HEK293T human embryonic kidney cells. The ED50 for this effect is typically 0.1-0.9 ug/mL in the presence of 5 ng/mL recombinant mouse Wnt3a.
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.