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Details of Functionality
Measured by its ability to inhibit proliferation in MC3T3‑E1 mouse preosteoblast cells. The ED50 for this effect is 1‑4 µg/mL. Optimal concentrations should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived human sFRP-3 protein Ala33-Asn325, with a C-terminal 10-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
35 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
38 kDa, reducing conditions
Publications
Read Publications using 192-SF/CF 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.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human sFRP-3 Protein, CF
FIZ
FREOS1
Frezzled
Fritz
Frizzled-related protein 1
frizzled-related protein
FRP
FRP-3
FRZB
Frzb1
FRZB-1
FRZB1sFRP-3
FRZB-PEN
FZRB
hFIZ
secreted frizzled-related protein 3
sFRP3
sFRP-3
SFRP3frezzled
SRFP3frizzled homolog-related
Background
Secreted Frizzled Related Protein 3 (sFRP-3) was originally identified in bovine cartilage for its chondrogenic ability. Human, mouse, chick and Xenopus clones have also been isolated. SFRP-3 is often referred to as FRZB, other names include Fritz, Frzb1, and FRP-3. At the amino acid sequence level, sFRP-3 is highly conserved. The human protein shares 77% identity with Xenopus, 92% with mouse, and 94% with bovine proteins. Human sFRP-3 is strongly expressed in the developing appendicular skeleton, and cartilage of craniofacial bones. As determined by Northern blot of adult tissues, it is strongly detected in heart and placenta, as well as the brain, skeletal muscle, kidney and pancreas.
The N-terminal portion of the protein shows 50% amino acid identity to the corresponding region of the Drosophila frizzled gene product, a receptor for Wg/Wnt signals. The similarity of sFRP-3 with frizzled proteins is restricted to the N-terminal cysteine-rich domain (CRD) that contains at least ten cysteine residues with highly conserved spacing between them. SFRP-3 was subsequently shown to be a soluble antagonist of Wnt signals. It lacks all transmembrane domains of frizzled proteins but retains the ability to bind Wnts. Ectopic expression of sFRP-3 mRNA has been shown to interfere with the induction of secondary axes in Xenopus embryos injected with Xwnt-8 mRNA.
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