Parathyroid hormone (1 - 13) (human) peptide

Parathyroid hormone (1 - 13) (human) peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

H-SVSEIQLMHNLGK-OH

H-Ser-Val-Ser-Glu-Ile-Gln-Leu-Met-His-Asn-Leu-Gly-Lys-OH

13

95.63%

C₆₂H₁₀₆N₁₈O₂₀S

1455.67

Synthetic

Powder

Parathyroid hormone (1 - 13) (human) is amino acids 1-13 of the N-terminus of parathyroid hormone and is a tryptic fragment sharing only 6 and 7 amino acids with the N-terminal tryptic peptides of parathyroid hormone related protein and parathyroid hormone (7–84) respectively. Parathyroid hormone (1 - 13) (human) has no substantial homology with any other trypsin digestion fragments of human proteins, making it a highly specific marker for full length parathyroid hormone (1–84).

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Lopez et al (2010) Selected reaction monitoring-mass spectrometric immunoassay responsive to parathyroid hormone and related variants. Clin Chem. 56(2) 281 PMID: 20022981
• Kumar et al (2010) Quantification of Serum 1–84 Parathyroid Hormone in Patients with Hyperparathyroidism by Immunocapture In Situ Digestion Liquid Chromatography–Tandem Mass Spectrometry, Clinical Chemistry, 56(2) 306 PMID: 20007860

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.