详细说明
- Purity>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
- Endotoxin Level<1.0 EU per 1 μg of the protein by the LAL method.
- ActivityMeasured by its ability to neutralize Activin-mediated erythroid differentiation of K562 human chronic myelogenous leukemia cells. The ED 50 for this effect is 3-15 ng/mL in the presence of 7.5 ng/mL rhActivin A.
- SourceMouse myeloma cell line, NS0-derived Val24-Val256, with a C-terminal 6-His tag
- Accession #
- N-terminal Sequence
AnalysisVal24 - Predicted Molecular Mass26 kDa
- SDS-PAGE38 kDa, reducing conditions
| 1255-F3/CF | | 1255-F3 |
| Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | Formulation Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. | |
| Reconstitution Reconstitute at 100 μg/mL in sterile PBS. | Reconstitution Reconstitute at 10 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. | |
| Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | |
| Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
| Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
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).
- References:
- 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.
- Hill, J. et al. (2002) J. Biol. Chem. 277:40735.
- Bartholin, L. et al. (2001) Oncogene 20:5409.
- Entrez Gene IDs:10272 (Human); 83554 (Mouse)
- Alternate Names:FLRG; FLRGFSRP; follistatin-like 3 (secreted glycoprotein); Follistatin-like 3; Follistatin-like protein 3; Follistatin-related gene protein; follistatin-related protein 3; FSTL3
400-6226-992