Recombinant Human PTH1R/PTHR1 Protein, CF Summary
Product Specifications
Tyr23-Met189, 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.
5709-PR
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 250 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.
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Reconstitution Calculator
Background: PTH1R/PTHR1
PTH1R (parathyroid receptor-1, also called PTHR1) is an 85-95 kDa member of the G-protein coupled receptor family 2 that is a critical receptor regulating Ca++ homeostasis (1-5). The human PTH1R cDNA encodes 593 amino acids (aa) including a 26 aa signal sequence and a long extracellular domain (aa 27-189) that contains the PTH (parathyroid hormone) and PTHrP (PTH-related protein) docking site (aa 173-189), followed by seven transmembrane domains within the C-terminal 404 aa (2-4). Within the N-terminal ECD, human PTH1R shares 87%, 88%, 96%, 94% and 93% aa identity with mouse, rat, canine, bovine and porcine PTH1R, respectively. PTH of other mammals will bind and stimulate human PTH1R, although with differing affinities (2). PTH1R is mainly expressed in bone and kidney, but is also present on hepatocytes, smooth muscle cells, and in other tissues where PTH and PTHrP are found (1-3, 5, 6). Through PTH1R on osteoblasts, PTH promotes differentiation of osteoclasts, which in turn promote release of Ca++ from bone (1, 5). PTH1R on osteocytes, however, allows PTH to promote bone formation (7). In renal epithelium, it promotes conversion of Vitamin D to its active form, lowers Ca++ excretion and increases phosphate excretion (1, 5). Following PTH binding, PTH1R undergoes a conformation change which activates cAMP, IP3, PKC and Ca++ signaling pathways (1, 8). PTH1R is then phosphorylated and downregulated by internalization (9). Dwarfism in Jansen‑type metaphyseal chondrodysplasia is associated with PTH1R gain of function, while in Blomstrand chondrodysplasia, PTH1R function is lost (10, 11). Impaired PTH1R function may be a factor in developmental endochondromas in Ollier disease (12). Polymorphisms may also be associated with variation in bone mineral density (13).
- Potts, J.T. (2005) J. Endocrinol. 187:311.
- Schipani, E. et al. (1993) Endocrinology 132:2157.
- Zhou, A.T. et al. (1997) Proc. Natl. Acad. Sci. USA 94:3644.
- Pellegrini, M. et al. (1998) Biochemistry 37:12737.
- Lupp, A. et al. (2010) Eur. J. Endocrinol. 162:979.
- Watson, P.H. et al. (2000) J. Bone Miner. Res. 15:1033.
- O’Brien, C.A. et al. (2008) PLoS ONE 3:e2942.
- Thomas, B.E. et al. (2008) Mol. Endocrinol. 22:1154.
- Bounoutas, G.S. et al. (2006) Endocrinology 147:4674.
- Schipani, E. et al. (1995) Science 268:98.
- Wysolmerski, J.J. (2001) J. Clin. Endocrinol. Metab. 86:1788.
- Couvineau, A. et al. (2008) Hum. Mol. Genet. 17:2766.
- Vilarino-Guell, C. et al. (2007) Calcif Tissue Int. 81:270.
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