Recombinant Mouse TGF-beta RIII Protein, CF

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Recombinant Mouse TGF-beta RIII Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its ability to inhibit TGF-beta 2 activity on HT‑2 mouse T cells. Tsang, M. et al. (1995) Cytokine 7:389. The ED50 for this effect is 8-40 ng/mL in the presence of 1 ng/mL of rhTGF-beta 2.
Mouse myeloma cell line, NS0-derived mouse TGF-beta RIII protein
Gly23-Thr785, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Predicted Molecular Mass
85.6 kDa
105-115 kDa, reducing conditions

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Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.


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.
  • 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.
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Background: TGF-beta RIII

Transforming growth factor beta receptor III (TGF-beta RIII; also betaglycan) is a ubiquitously expressed, 280 kDa type I transmembrane proteoglycan member of the TGF-beta superfamily of proteins (1). Mouse TGF-beta RIII is synthesized as an 850 amino acid (aa) precursor that consists of a 22 aa signal sequence, a 763 extracellular domain (ECD), a 23 aa transmembrane region, and a 42 aa cytoplasmic tail (SwissProt # O88393). The large ECD contains heparan sulfate and chondroitin sulfate glycosaminoglycans, five potential N-linked glycosylation sites, and a zona pellucida-like domain from residues 454 - 731 (1 - 2). The short cytoplasmic domain is rich in serine and threonine, but has no discernible signaling structure typical of receptor kinases (2). Proteolysis at one of two potential juxtamembrane cleavage sites (Lys743Lys and Leu750AlaValVal) allows cells to release TGF-beta RIII in a soluble form (1 - 2). Mouse TGF beta RIII shares 94%, 82%, 80%, and 67% aa sequence identity with rat, human, porcine, and chicken TGF-beta RIII, respectively (2). In all of these species, TGF beta RIII contains 17 cysteines that are 100% conserved (2). TGF-beta RIII binds with high affinity to TGF-beta 1, TGF-beta 2, and TGF-beta 3 isoforms (1). TGF-beta RIII functions by binding, and then "presenting" ligand to TGF-beta type II receptors (1, 3). It also functions to limit ligand availability to the receptor via proteolysis which releases the soluble form of TGF beta RIII along with any bound factors, making them inaccessible to cell-surface receptors (1, 3). TGF-beta RIII can therefore enhance or inhibit cell signaling. TGF-beta RIII has been shown to play an essential role in the formation of the atrioventricular cushion and coronary vessels during development of the heart (4 - 6). TGF beta RIII also plays a role in many cancers. Increased expression of TGF beta RIII is found in higher grade lymphomas, and reduced expression of TGF beta RIII is found with advanced stage neuroblastomas and ovarian carcinomas (4, 7 - 9). Low TGF-beta RIII expression also correlates with higher grade among a cohort of breast cancers (4, 10). Additionally, overexpression of TGF-beta RIII in MDA-231 human breast cancer cells and DU145 prostate cancer cells results in decreased tumor invasion in vitro and in vivo (4, 11 - 12).

  1. Kolodziejczyk, S.M. and B.K. Hall (1996) Biochem. Cell Biol. 74:299.
  2. Ponce-Castaneda, M.V. et al. (1998) Biochim. Biophys. Acta 1384:189.
  3. Lopez-Casillas, F. et al. (1993) Cell 73:1435.
  4. Criswell, T.L. and C.L. Arteaga (2007) J. Biol. Chem. 282:32491.
  5. Brown, C.B. et al. (1999) Science 283:2080.
  6. Compton, L.A. et al. (2007) Circ. Res. 101:784.
  7. Woszczyk, D. et al. (2004) Med. Sci. Monit. 10:CRIII3.
  8. Bristow, R.E. et al. (1999) Cancer 85:658.
  9. Iolascon, A. et al. (2000) Br. J. Cancer 82:1171.
  10. Dong, M. et al. (2007) J. Clin. Invest. 117:206.
  11. Turley, R.S. et al. (2007) Cancer Res. 67:1090.
  12. Sun, L. and  C. Chen (1997) J. Biol. Chem. 272:25367.
Long Name
Transforming Growth Factor beta Receptor III
Entrez Gene IDs
7049 (Human); 21814 (Mouse); 29610 (Rat)
Alternate Names
betaglycan proteoglycan; Betaglycan; BGCAN; TBRIII; TGF-beta receptor type 3; TGF-beta receptor type III; TGF-beta RIII; TGFbetaRIII; TGFBR3; TGF-bRIII; TGFR-3; Transforming growth factor beta receptor III; transforming growth factor beta receptor type 3; transforming growth factor, beta receptor III (betaglycan, 300kDa); transforming growth factor, beta receptor III

Citation for Recombinant Mouse TGF-beta RIII Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. The neovascularization effect of dedifferentiated fat cells
    Authors: H Watanabe, S Goto, R Kato, S Komiyama, Y Nagaoka, T Kazama, C Yamamoto, Y Li, N Konuma, K Hagikura, T Matsumoto
    Sci Rep, 2020;10(1):9211.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay


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