Recombinant Mouse FLRG Protein
Recombinant Mouse FLRG Protein Summary
Product Specifications
Val24-Val256, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
1255-F3
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
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. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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1255-F3/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
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.
|
Reconstitution Calculator
Background: Follistatin-related Gene Protein/FLRG
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).
- 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.
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