Teriparatide acetate is a 34-residue peptide corresponding to the N-terminal 1-34 region of human parathyroid hormone (PTH). This sequence contains the principal receptor-binding and activation determinants required for signaling through parathyroid hormone receptor type 1 (PTH1R).
As a defined human PTH(1-34) research peptide, Teriparatide is widely used in studies of class B1 GPCR activation, cAMP signaling, receptor trafficking, bone-cell biology and parathyroid hormone structure–activity relationships.
Product Information
| Property | Specification |
|---|---|
| Product Name | Teriparatide Acetate |
| Catalog No. | AS2517 |
| CAS No. | 99294-94-7 |
| Peptide Identity | Human PTH (1-34) |
| Sequence | Ser-Val-Ser-Glu-Ile-Gln-Leu-Met-His-Asn-Leu-Gly-Lys-His-Leu-Asn-Ser-Met-Glu-Arg-Val-Glu-Trp-Leu-Arg-Lys-Lys-Leu-Gln-Asp-Val-His-Asn-Phe |
| One-Letter Sequence | SVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNF |
| Peptide Length | 34 amino-acid residues |
| Peptide Molecular Formula | C181H291N55O51S2 |
| Peptide Moiety Molecular Weight | Approximately 4117.72 Da |
| Salt Form | Acetate |
| Primary Receptor | PTH1R / Parathyroid Hormone Receptor Type 1 |
| Research Areas | PTH1R pharmacology, cAMP signaling, receptor trafficking, bone-cell biology, peptide SAR |
PTH (1-34) Contains the Receptor-Active Region of Human PTH
Native human parathyroid hormone contains 84 amino-acid residues. The N-terminal 1-34 region retains the sequence required for strong PTH1R binding and receptor activation, allowing Teriparatide to serve as a compact reference ligand for mechanistic studies.
PTH1R follows the characteristic two-domain recognition mechanism of class B1 GPCRs. Residues in the C-terminal portion of PTH(1-34) contribute strongly to interaction with the receptor extracellular domain, while the peptide N-terminus engages the transmembrane receptor core and promotes activation.
The first several N-terminal residues are especially important for Gs coupling and cAMP generation. Sequence substitutions in this region can therefore produce substantial changes in signaling efficacy even when receptor binding remains measurable.
PTH1R Signaling and Endosomal cAMP
PTH1R is a well-established model for studying spatially organized GPCR signaling. After ligand binding, the receptor can activate Gs-dependent adenylyl cyclase and increase intracellular cAMP.
PTH(1-34)-activated PTH1R can also recruit β-arrestin and continue generating cAMP after receptor internalization into endosomal compartments. This signaling behavior has made the PTH1R system important for studies of receptor trafficking, signal duration and location-dependent GPCR pharmacology.
Recent structural work has further characterized β-arrestin engagement with activated PTH1R and linked specific arrestin-coupling conformations to receptor internalization and intracellular trafficking.
Full-Length PTH and PTH (1-34)
| Feature | Human PTH (1-84) | Teriparatide / PTH (1-34) |
|---|---|---|
| Length | 84 residues | 34 residues |
| PTH1R-Activating N-Terminus | Present | Present |
| Residues 35-84 | Present | Absent |
| Common Research Use | Full-hormone biology and processing | Receptor pharmacology, signaling and peptide SAR |
These two molecular forms should be identified separately in experimental records. PTH(1-34) captures the principal receptor-active region but does not contain the complete C-terminal sequence of the native hormone.
Acetate Salt and Molecular Weight
The commonly reported molecular formula C181H291N55O51S2 and molecular weight of approximately 4117.72 Da describe the Teriparatide peptide moiety.
Because this product is supplied as an acetate form, total bulk material can also contain acetate and residual water. For precise molar preparation, peptide content and counterion information should therefore be considered together with nominal vial mass.
We recommend using lot-specific analytical information for quantitative receptor or cellular assays instead of assuming that the complete dry mass represents 100% peptide moiety.
Methionine Oxidation and Analytical Control
Teriparatide contains methionine at positions 8 and 18. Methionine oxidation is therefore a relevant analytical consideration during synthesis, purification, storage and repeated handling of the peptide.
For studies comparing receptor potency or signaling kinetics, the intended sequence, molecular mass and chromatographic purity should be evaluated together. LC-MS can also help identify oxidation-related molecular species that may not be apparent from nominal purity alone.
Our Peptide Quality Control capabilities support analytical HPLC and mass spectrometry according to the selected specification.
Research Applications
Teriparatide acetate can support PTH1R ligand-binding studies, cAMP measurements, β-arrestin and receptor-trafficking experiments, osteoblast and bone-cell research, peptide structure–activity analysis and comparison of PTH-derived receptor agonists.
Researchers working with endocrine regulatory peptides can explore our Parathyroid Hormone (PTH) Peptides collection.
Sequence variants, truncated PTH fragments, labeled derivatives and non-natural amino-acid analogs can be evaluated through our Chemical Peptide Synthesis capabilities.
Frequently Asked Questions
Is Teriparatide the same sequence as full-length human PTH?
Teriparatide corresponds to residues 1-34 of human PTH. Full-length human PTH contains 84 amino-acid residues.
What receptor is activated by PTH (1-34)?
The principal research target is PTH1R, a class B1 G protein-coupled receptor that can signal through Gs/cAMP and additional intracellular pathways.
Does 4117.72 Da include the acetate counterion?
No. The value of approximately 4117.72 Da refers to the Teriparatide peptide moiety. Acetate and residual water should be considered separately when exact bulk-material composition is required.
Can modified PTH (1-34) analogs be synthesized?
Yes. Residue substitutions, truncations, labels and other defined PTH analogs can be evaluated through Chemical Peptide Synthesis.