Measured by its ability to neutralize Activin-mediated erythroid differentiation of K562 human chronic myelogenous leukemia cells. The ED50 for this effect is 3-15 ng/mL in the presence of 7.5 ng/mL recombinant human Activin A.
Source
Mouse myeloma cell line, NS0-derived human Follistatin-related Gene Protein/FLRG protein Met27-Val263, with a C-terminal 6-His tag
>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
Bioactivity
Theoretical MW
26 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 1288-F3/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
>90%, 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 FLRG Protein, CF
FLRG
FLRGFSRP
follistatin-like 3 (secreted glycoprotein)
Follistatin-like 3
Follistatin-like protein 3
Follistatin-related gene protein
follistatin-related protein 3
FSTL3
Background
Follistatin-related gene protein (FLRG), also known as follistatin-like 3 (FSTL3) is a glycoprotein belonging to the follistatin-module protein family. Human FLRG cDNA encodes a 263 amino acid (aa) residue protein with a putative 26 aa signal peptide, an N-terminal domain, two cysteine-rich follistatin-like domains (FS) and a C‑terminal acidic domain. Compared to follistatin, FLRG lacks the third FS domain found in follistatin. In addition, FLRG also lacks the heparin-binding domain found within the first amino-terminal FS domain of follistatin. Mouse and human FLRG share approximately 83% aa sequence homology. Like follistatin, FLRG has been shown to bind and inhibit the activities of TGF-beta family ligands including activin, BMP-2, -6, -7 and GDF-8/myostatin. While both FLRG and follistatin are located in a wide and overlapping range of adult and fetal tissue, their sites of peak expression differ: FLRG most highly in heart, lung, kidney, placenta and testis, while follistatin is highest in ovary and pituitary. The expression of FLRG is upregulated by TGF-beta and activin signaling through Smad proteins. Although FLRG is a secreted protein in many cell types, it has also been localized to the nuclear compartment in HeLa, 293 and CHO cells (1 - 5).
Tsuchida, K. et al. (2000) J. Biol. Chem. 275:40778.
Sidis, Y. et al. (2002) Endocrinology 143:1613.
Tortoriello, D.V. et al. (2001) Endocrinology 142:3426.
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