Recombinant Human FLRG Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human FLRG Protein, CF Summary

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 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
Accession #
N-terminal Sequence
Met27
Protein/Peptide Type
Recombinant Proteins
Gene
FSTL3
Purity
>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:

Packaging, Storage & Formulations

Storage
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).

  1. Tsuchida, K. et al. (2000) J. Biol. Chem. 275:40778.
  2. Sidis, Y. et al. (2002) Endocrinology 143:1613.
  3. Tortoriello, D.V. et al. (2001) Endocrinology 142:3426.
  4. Hill, J. et al. (2002) J. Biol. Chem. 277:40735.
  5. Bartholin, L. et al. (2001) Oncogene 20:5409.

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Publications for Follistatin-related Gene Protein/FLRG/Fstl3 (1288-F3/CF)(5)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 2 applications: Bioassay, ELISA (Standard).


Filter By Application
Bioassay
(3)
ELISA (Standard)
(2)
All Applications
Filter By Species
Human
(3)
All Species
Showing Publications 1 - 5 of 5.
Publications using 1288-F3/CF Applications Species
RG Walker, M Czepnik, EJ Goebel, JC McCoy, A Vujic, M Cho, J Oh, S Aykul, KL Walton, G Schang, DJ Bernard, AP Hinck, CA Harrison, E Martinez-H, AJ Wagers, RT Lee, TB Thompson Structural basis for potency differences between GDF8 and GDF11 BMC Biol, 2017-03-03;15(1):19. 2017-03-03 [PMID: 28257634] (Bioassay, Human) Bioassay Human
Nanda S, Savvidou M, Syngelaki A, Akolekar R, Nicolaides KH Prediction of gestational diabetes mellitus by maternal factors and biomarkers at 11 to 13 weeks. Prenat. Diagn., 2010-12-28;31(2):135-41. 2010-12-28 [PMID: 21268030] (ELISA (Standard)) ELISA (Standard)
Miron P, Lambert J, Marcil A, Cowans NJ, Stamatopoulou A, Spencer K Maternal plasma levels of follistatin-related gene protein in the first trimester of pregnancies with Down syndrome. Prenat. Diagn., 2010-03-01;30(3):224-8. 2010-03-01 [PMID: 20063262] (ELISA (Standard)) ELISA (Standard)
Jeanpierre S, Nicolini FE, Kaniewski B, Dumontet C, Rimokh R, Puisieux A, Maguer-Satta V BMP4 regulation of human megakaryocytic differentiation is involved in thrombopoietin signaling. Blood, 2008-07-29;112(8):3154-63. 2008-07-29 [PMID: 18664625] (Bioassay, Human) Bioassay Human
Butler GS, Dean RA, Tam EM, Overall CM Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein shedding. Mol. Cell. Biol., 2008-05-27;28(15):4896-914. 2008-05-27 [PMID: 18505826] (Bioassay, Human) Bioassay Human

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Bioinformatics

Gene Symbol FSTL3
Uniprot