Measured by its ability to synergize with Wnt-3a to induce Topflash reporter activity in HEK293T human embryonic kidney cells. The ED50 for this effect is 10-40 ng/mL in the presence of 20 ng/mL of Recombinant Mouse Wnt‑3a (Catalog # 1324-WN).
Source
Mouse myeloma cell line, NS0-derived human sFRP-2 protein Leu25-Cys295
>95%, 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
Bioactivity
Theoretical MW
31 kDa. 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
34-36 kDa, reducing conditions
Publications
Read Publications using 6838-FR in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS and NaCl with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 200 μg/mL in PBS containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human sFRP-2 Protein
FRP2
FRP-2secreted apoptosis related protein 1
SARP-1
SARP1sFRP-2
SDF-5
Secreted apoptosis-related protein 1
secreted frizzled-related protein 2
sFRP2
sFRP-2
Background
Secreted Frizzled Related Protein‑2 (sFRP‑2) belongs to a family of Wnt‑binding proteins with homology to the ligand‑binding domain of the Frizzled transmembrane Wnt receptors. The sFRP proteins are approximately 30‑35 kDa in size and contain an N-terminal Frizzled‑like domain with 10 conserved cysteines and a Netrin‑like C‑terminal domain (1, 2). Mature human sFRP‑2, also known as SARP‑1, SDF‑5, and FRP‑2, shares 99% aa sequence identity with mouse and rat sFRP‑2 (3). sFRP‑2 is widely expressed during embryogenesis and in the adult tissues including the eye, heart, lung, colon, intestine, smooth muscle, pancreas, prostate, testis, kidney, brain, teeth and joints, craniofacial mesenchyme, and preadipocytes (3‑6). Depending on the context, sFRP‑2 can exert either positive or negative effects on Wnt signaling (7‑9). It also inhibits BMP‑induced effects (8, 10). sFRP‑2 can be incorporated into the extracellular matrix through interactions with Fibronectin and Integrin alpha 5 beta 1 (11). sFRP‑2 plays a variety of roles during tissue morphogenesis including inhibition of the planar cell polarity pathway and myoblast and osteoblast differentiation (8, 10, 12, 13). sFRP‑2 is also expressed in multiple myeloma and glioma in which it promotes tumorigenicity (10, 14). At physiological concentrations sFRP‑2 enhances BMP‑1 mediated proteolysis of Pro‑Collagen I, whereas at higher concentrations it inhibits BMP‑1 activity (15, 16). This difference is significant considering that sFRP‑2 is up‑regulated in fibrotic areas of the heart following myocardial infarction (15, 16). Elevated levels of sFRP‑2 then promote the recovery of cardiac function by reducing collagen deposition, remodeling, and calcification and by promoting the engraftment of mesenchymal stem cells into the heart (8, 15).
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