Recombinant Human Wnt-2/sFRP-1 Complex Protein, CF Summary
| Details of Functionality |
Measured by its ability to activate Wnt induced TCF reporter activity in HEK293 human embryonic kidney cells. The ED 50 for this effect is 10.0-150 ng/mL. |
| Source |
Chinese Hamster Ovary cell line, CHO-derived human Wnt-2 protein | Human Wnt-2 (Ser26-Thr360) Accession # P09544.1 | | Human sFRP-1 (Ser32-Lys314) Accession # AAB70793.1 | N-terminus | C-terminus | |
| N-terminal Sequence |
Ser26 (Wnt-2) & Ser32 (sFRP-1) |
| Structure / Form |
Non-covalent complex |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
38 kDa (Wnt-2) & 33 kDa (sFRP-1). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
| SDS-PAGE |
30-45 kDa, under reducing conditions. |
Packaging, Storage & Formulations
| Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution. |
| Buffer |
Lyophilized from a 0.2 μm filtered solution in MOPS and NaCl with Trehalose. |
| Purity |
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Reconstitution Instructions |
Reconstitute at 100 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Wnt-2/sFRP-1 Complex Protein, CF
Background
Wnt-2 is one of 19 vertebrate members of the Wingless-type MMTV integration site (Wnt) family of highly conserved cysteine-rich secreted glycoproteins that are important for normal developmental processes (1). Human Wnt-2 is a 35 kDa, secreted, glycosylated member of the Wnt family of developmental proteins. It is considered a class 1 Wnt based on its strong transforming activity on C57MG cells. Human Wnt-2 is synthesized as a 360 amino acid (aa) precursor that contains a 335 aa mature region. The mature region contains 24 cysteines and two potential N-linked glycosylation sites. Mature human Wnt-2 is 96% aa identical to mature mouse and rat Wnt-2. Wnt-2 is produced by mammary myoepithelial cells, endometrial epithelial cells, and breast fibroblasts (2, 3). Wnts bind to the cell surface Frizzled family receptors in conjunction with low-density lipoprotein receptor-related protein family receptors (LRP5 or 6) resulting in the stabilization of intracellular beta -catenin levels (4). As intracellular beta -catenin levels rise, beta -catenin binds to TCF/LEF transcription factors leading to expression of Wnt target genes (5). Wnt-2 is known to bind to sFRPs, a family of secreted molecules that contain an N-terminal cysteine-rich domain (CRD) highly similar to the CRDs of the Frizzled family receptors (6,7). More than one molecule of sFRP is suggested to participate in the interaction with each Wnt molecule (7). R&D Systems produces biologically active human Wnt-2 protein in a complex with human sFRP-1, and this Wnt-2/sFRP-1 complex is stable in the physiological buffer without detergent. Expression of Wnt-1, Wnt-2, E-cadherin, and beta -catenin is a common occurrence in non-small cell lung cancer (NSCLC) and is related to tumor histology and grade (8). Wnt-2 signaling is required for TGF-beta -mediated endothelial-to-mesenchymal transition (EndMT) of human aortic endothelial cells (HAECs), suggesting that Wnt-2 may contribute to atherosclerotic plaque development, and render Wnt-2 as a potential target for therapeutic intervention aiming at controlling atherosclerosis (9).
- Willert, K. and R. Nusse (2012) Cold Spring Harb. Perspect. Biol. 4:a007864.
- Van Ooyen, A. et al. (1985) EMBO J. 4:2905.
- Burrus, L.W. and A.P. McMahon (1995) Exp. Cell Res. 220:363.
- MacDonald, B.T. and X. He (2012) Cold Spring Harb. Perspect. Biol. 4:a007880.
- Korinek, V. et al. (1997) Science 275:1784.
- Dennis, S. et al. (1999) J. Cell Sci. 112:3815.
- Bafico, A. et al. (1999) J. Biol. Chem. 274:16180.
- Wrona, A. et al. (2021) Histochem. Cytochem. 69:711.
- Zhang, J. et al. (2021) Front. Cardiovasc. Med. 8:751720.
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