PTH
Spezies: Human
Recombinant
> 98.0 % as determined by:1. Analysis by RP-HPLC2. Anion-exchange FPLC3. Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel
Active
PTH is fully biologically active when compared to standards. The activity calculated by UMR106 cell/cAMP method corresponding to a specific activity of 1.0×104 U/mg.
Reinheit
> 98.0 % as determined by:1. Analysis by RP-HPLC2. Anion-exchange FPLC3. Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel
Endotoxin-Niveau
Level Less than 0.1 ng/myg (IEU/myg) of Parathyroid Hormone (PTH
PTH
Spezies: Human
Wirt: Escherichia coli (E. coli)
> 97 % by SDS-PAGE and HPLC analyses.
Active
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Rekonstitution
It is recommended to reconstitute the lyophilized Parathyroid Hormone (PTH) in sterile 18 M-omega-cm H2O not less than 100 myg/ml, which can then be further diluted to other aqueous solutions.
Parathyroid Hormone (PTH) is the most important endocrine regulator of calcium and phosphorus concentration in extracellular fluid. Parathyroid Hormone (PTH) is secreted from cells of the parathyroid glands and finds Parathyroid Hormone's major target cells in bone and kidney. Like most other protein hormones, Parathyroid Hormone (PTH) is synthesized as a preprohormone. After intracellular processing, the mature hormone is packaged within the Golgi into secretory vesicles, the secreted into blood by exocytosis. Parathyroid Hormone (PTH) is secreted as a linear protein of 84 amino acids. Recombinant Human Parathyroid Hormone (PTH) produced in E. coli is a single, non-glycosylated, polypeptide chain containing 84 amino acids and having a molecular mass of 9,000 Da. Synonym: PTH. Formulation: The protein (1 mg/ml) was lyophilized after extensive dialyses against 1.15 mg sodium citrate, sodium chloride 7.31 mg, 0.21 mg citric acid, 0.1117 mg EDTA-Na2, 0.2 mg Tween 80 and 50 mg Mannitol.