Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | 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 rhActivin A. |
Source | Mouse myeloma cell line, NS0-derived mouse Follistatin-related Gene Protein/FLRG protein Val24-Val256, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Val24 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Fstl3 |
Purity | >90%, 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. |
Dilutions |
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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 |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
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. |
Follistatin-Related Gene Protein (FLRG), also known as follistatin-like 3 (FSTL3) is a glycoprotein belonging to the follistatin-module protein family. Mouse FLRG cDNA encodes a 256 amino acid (aa) residue protein with a putative 23 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).
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