Recombinant Human TSHR Fc Chimera Protein, CF

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Recombinant Human TSHR Fc Chimera Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. In a Goat Anti-Human IgG Fc Antibody (Catalog # G-102-C) coated plate, Recombinant Human TSHR Fc Chimera present at 2.5 μg/mL (100 μL/well) can bind Biotinylated Recombinant Human TSH alpha/beta Heterodimer with an ED50 of 0.12-0.6 μg/mL.
Chinese Hamster Ovary cell line, CHO-derived human TSHR protein
Human TSH R
Accession # P16473
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
71 kDa

Product Datasheets

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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 500 μg/mL in 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: TSHR

Thyroid stimulating hormone receptor (TSH R) is an approximately 120 kDa glycosylated receptor for the endocrine hormone thyrotropin (TSH). TSH consists of a common alpha subunit which is also a subunit of luteinizing hormone (LH), follicle stimulating hormone (FSH), and chorionic gonadotropin (CH), plus a beta subunit which is unique to TSH. It is produced by the anterior pituitary and triggers the thyroid gland to release thyroxine (T4). T4 is then converted to triiodothyronine (T3) which exerts wide-ranging effects on growth and metabolism (1). TSH R additionally binds to the related hormone thyrostimulin which is composed of different alpha and beta subunits (2). TSH R is the dominant target of autoreactive antibodies in Graves’ disease but is a more rare target in Hashimoto’s thyroiditis (3). Human TSH R consists of a 393 amino acid (aa) N-terminal extracellular domain (ECD) with 7 tandem leucine-rich repeats, a 7-transmembrane segment region, and an 82 aa C-terminal cytoplasmic tail (4-6). Within the N-terminal ECD, human TSH R shares 87% aa sequence identity with mouse and rat TSH R. Alternative splicing generates soluble isoforms that are substituted and truncated following the fifth LRR (7, 8). TSH R is primarily expressed by epithelial cells of the thyroid (thyrocytes), although it has also been detected in multiple non-endocrine tissues. TSH R is expressed as a disulfide linked heterodimer; it is proteolytically cleaved, and the C-terminal fragment is subsequently trimmed at its N-terminus (9-11). The 53 kDa alpha domain can be released by disulfide reduction at the cell surface and retains the ability to bind TSH (12, 13). The agonistic anti-TSH R antibodies produced in Graves’ disease preferentially recognize the free alpha subunit over the heterodimeric receptor (14). The activation of TSH R in brown adipose tissue can trigger the up-regulation of UCP-1 as well as thermogenesis (15).

  1. de Lloyd, A. et al. (2010) J. Endocrinol. 204:13.
  2. Nakabayashi, K. et al. (2002) J. Clin. Invest. 109:1445.
  3. Dong, Y.H. and D.-G. Fu (2014) Eur. Rev. Med. Pharmacol. Sci. 18:3611.
  4. Parmentier, M. et al. (1989) Science 246:1620.
  5. Nagayama, Y. et al. (1989) Biochem. Biophys. Res. Commun. 165:1184.
  6. Misrahi, M. et al. (1990) Biochem. Biophys. Res. Commun. 166:394.
  7. Takeshita, A. et al. (1992) Biochem. Biophys. Res. Commun. 188:1214.
  8. Graves, P.N. et al. (1992) Biochem. Biophys. Res. Commun. 187:1135.
  9. Graves, P.N. et al. (1996) Endocrinology 137:3915.
  10. Latif, R. et al. (2001) J. Biol. Chem. 276:45217.
  11. de Bernard, S. et al. (1999) J. Biol. Chem. 274:101.
  12. Couet, J. et al. (1996) Biochemistry 35:14800.
  13. Couet, J. et al. (1996) J. Biol. Chem. 271:4545.
  14. Chazenbalk, G.D. et al. (2002) J. Clin. Invest. 110:209.
  15. Endo, T. and T. Kobayashi (2008) Am. J. Physiol. Endocrinol. Metab. 295:E514.
Long Name
Thyroid Stimulating Hormone Receptor
Entrez Gene IDs
7253 (Human); 22095 (Mouse)
Alternate Names
CHNG1; LGR3; LGR3hTSHR-I; MGC75129; seven transmembrane helix receptor; thyroid stimulating hormone receptor; Thyroid-stimulating hormone receptor; thyrotropin receptor; thyrotropin receptor-I, hTSHR-I; TSH R; TSHR; TSH-R


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