Recombinant Human TSH R Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human TSH R Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit rhTSH-induced cAMP accumulation in HEK293 human embryonic kidney cells transfected with human TSH R. The ED50 for this effect is 2-12 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human TSH R protein
Human TSH R
(Met22-Gly413)
Accession # P16473
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Met22
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
TSHR
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
71 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.

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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human TSH R Fc Chimera Protein, CF

  • 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

Background

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.

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Bioinformatics

Gene Symbol TSHR
Entrez
Uniprot