Recombinant Human TSHR Fc Chimera Protein, CF

Recombinant Human TSHR Fc Chimera Protein, CF Summary

Product Specifications

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.

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).

Related Research Areas

• Reproductive Peptide Hormones and Regulators