Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. When Recombinant Human PTH1R/PTHR1 is used at 2 μg/mL, the concentration of biotinylated human PTHrP that produces 50% of the optimal binding response is found to be approximately 0.03 ‑ 0.12 μg/mL. |
Source | Chinese Hamster Ovary cell line, CHO-derived human PTH1R/PTHR1 protein Tyr23-Met189, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Tyr23 |
Protein/Peptide Type | Recombinant Proteins |
Gene | PTH1R |
Purity | >95%, 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. |
Dilutions |
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Theoretical MW | 20.0 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. |
SDS-PAGE | 25-40 kDa, reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 250 μg/mL in PBS. |
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).
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