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0032 (0)16 41 44 07
+32 1650 9045
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Česká republika Praha
US New York
0032 (0)16 41 44 07
Recombinant Human Parathyroid Hormone (PTH1-84)
(Cat. No.: C010)
Parathyroid hormone is the most important endocrine regulator of calcium and phosphorus concentration in extracellular fluid. This hormone is secreted from cells of the parathyroid glands and finds its major target cells in bone and kidney. Another hormone, parathyroid hormone-related protein, binds to the same receptor as parathyroid hormone and has major effects on development.
Like most other protein hormones, parathyroid hormone 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 is secreted as a linear protein of 84 amino acids.
Recombinant Human PTH produced in E. coli is a single, non-glycosylated, polypeptide chain containing 84 amino acids and having a molecular mass of 9 kDa.
Biological Activity: rHuPTH is fully biologically active when compared to standards. The activity calculated by UMR106 cell/cAMP method corresponding to a specific activity of 1.0 x 104 IU/mg.
Purity: Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Anion-exchange FPLC.
(c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.
Endotoxin: Less than 0.1 ng/µg (IEU/µg) of rHuPTH.
Formulation: The protein (1mg/ml) was lyophilized after extensive dialyses against 1.15mg sodium citrate, 7.31mg sodium chloride, 0.21mg citric acid, 0.1117 EDTA-Na2, 0.2mg Tween 80 and 50mg Mannitol.
Storage: Lyophilized rHuPTH although stable at room temperature for 3 weeks, should be stored desiccated below -18oC. Upon reconstitution rHuPTH should be stored at 4oC between 2-7 days and for future use below -18oC. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.
Reconstitution: It is recommended to reconstitute the lyophilized rHuPTH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
1: Arch Surg 2009 Jan;Vol 144(1)
Elevation of parathyroid hormone levels in children who underwent parathyroidectomy for hyperparathyroidism.
2: Vet Surg 2009 Jan;Vol 38(1)
Validation of a rapid parathyroid hormone assay and intraoperative measurement of parathyroid hormone in dogs with benign naturally occurring primary hyperparathyroidism.
[Abstract] OBJECTIVES: To (1) validate a rapid chemiluminescent parathyroid hormone (PTH) assay, (2) determine it's usefulness locating a parathyroid nodule(s), and (3) determine if >50% decrease in PTH corresponds with excision of autonomously functioning parathyroid tissue. STUDY DESIGN: Prospective cohort study. ANIMALS: Dogs (n=12) with naturally occurring primary hyperparathyroidism and 25 healthy dogs. METHODS: The assay was validated with linearity, precision, and intermethod comparison. Preoperative and postoperative systemic plasma PTH concentrations, measured from saphenous venous blood, were compared. Intraoperative local PTH concentrations were measured in right and left jugular venous blood before and after surgical excision of the grossly abnormal
parathyroid gland(s). RESULTS: Within run and day-to-day precisions were acceptable (coefficient of variation <15%). Dilutional parallelism was used to demonstrate high correlation between measured and calculated PTH concentrations (R(2)=0.99). The assay methods had good correlation but numerical results of the rapid assay were usually lower than the immunoradiometric assay. Seven of 12 dogs had uniglandular disease and five had multiglandular disease. Systemic and local PTH concentrations decreased >50% in all the dogs after excision of the parathyroid gland(s). Mean preoperative systemic plasma PTH concentrations were significantly higher than mean postoperative systemic concentrations. Local PTH concentrations could not be used reliably to differentiate the side of the autonomously
functioning gland(s). Hypercalcemia resolved postoperatively in all the dogs. CONCLUSION: This assay measures PTH in dogs. Rapid PTH measurement provided documentation of decreased PTH concentration after removal of autonomously functioning parathyroid tissue. CLINICAL RELEVANCE: Use of this assay allows documentation of a significant decrease in PTH concentration after excision of autonomously functioning parathyroid tissue.
3: Bone 2008 Dec;
Marked reduction of bone turnover by alendronate attenuates the acute response of bone resorption marker to endogenous parathyroid hormone.
[Abstract] The aim of this study was to assess the effects of the antiresorptive treatments of alendronate (ALN), risedronate (RIS) and raloxifene (RLX) on the response of bone to endogenous parathyroid hormone (PTH) induced by acute hypocalcemia. Forty women (age, 55-80 years) with postmenopausal osteoporosis (treated with ALN, RIS and RLX or untreated-control group) were given infusions of sodium ethylenediaminetetraacetic acid (EDTA; 10 mg/kg of body weight). Serum ionized calcium (iCa), plasma intact PTH and marker of bone resorption, serum beta C-terminal telopeptide of type I collagen (beta-CTX; beta CrossLaps) were followed for 180 min. In all women, decrease in serum iCa following the EDTA load resulted in an acute increase in serum PTH. Between 60 and 180 min,
plasma PTH in the ALN and RIS treated women remained significantly higher than in the control group. The integrated beta-CTX responses (area under curves, AUCs) to peaks of PTH were significantly lower in the ALN treated women than in those treated with RIS, RLX or control group. There was no significant difference in beta-CTX AUC response to PTH between RIS, RLX and control women. Taken together, these findings suggest that in women with postmenopausal osteoporosis treated with ALN, a substantial reduction of bone turnover blunts the acute bone resorbing effect of endogenous PTH.
4: Endocrinology 2009 Jan;
The chemokine Cxcl1 is a novel target gene of PTH/PTHrP in committed osteoblasts.
[Abstract] The PTH receptor (PTHR1) is expressed on osteoblasts and responds to PTH or PTHrP in an endocrine or autocrine/paracrine manner, respectively. A microarray study carried out on PTHR1-positive osteoblasts (Kusa 4b10 cells) identified the CXC family chemokine ligand 1 (Cxcl1) as a novel immediate PTH/PTHrP responsive gene. Cxcl1 is a potent neutrophil chemoattractant with recognized roles in angiogenesis and inflammation, but a role in bone biology has not been described. Cxcl1 mRNA levels were up-regulated one hour after either PTH or PTHrP treatment of differentiated Kusa 4b10 osteoblasts (15-fold) and mouse calvarial osteoblasts (160-fold), and in rat metaphyseal bone (5-fold) one hour after a single subcutaneous injection of PTH. Furthermore, PTH treatment
stimulated a 10-fold increase in secreted Cxcl1 protein by both Kusa 4b10 cells and calvarial osteoblasts. Immunohistochemistry and PCR demonstrated that CXCR2, the receptor for Cxcl1, is highly expressed in osteoclast precursors (haemopoietic cells) but is predominantly undetectable in the osteoblast lineage, suggesting that osteoblast-derived Cxcl1 may act as a chemoattractant for osteoclast precursors. Confirming this hypothesis, recombinant Cxcl1 dose-dependently stimulated migration of osteoclast precursors in cell culture studies, as did conditioned media from Kusa 4b10 cells treated with PTH. This data indicate that local action through the PTHR1 could stimulate cells of the osteoblast lineage to release a chemokine capable of attracting osteoclast precursors to the bone environment.
Protein Accession No.:
SVSEI QLMHN LGKHL NSMER VEWLR KKLQD VHNFV ALGAP LAPRD AGSQR PRKKE DNVLV ESHEK SLGEA DKADV NVLTK AKSQ
*NOTE: ALL PRODUCTS ARE FOR RESEARCH USE ONLY