PTH Human

Parathyroid Hormone (1-34) Human Recombinant
Cat. No.
BT19959
Source
Escherichia Coli.
Synonyms
Parathyrin, PTH, Parathormone.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Parathyroid Hormone Human Recombinant (C181H290N55O51S2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 34 amino acids and having a molecular mass of 4117.8 Dalton.
The PTH is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Parathyroid hormone (PTH), also known as parathormone, is an 84-amino acid polypeptide hormone secreted by the parathyroid glands. It plays a crucial role in calcium homeostasis by increasing calcium levels in the bloodstream. Conversely, calcitonin, a hormone produced by the thyroid gland's parafollicular cells, lowers calcium concentration. PTH exerts its calcium-elevating effects by targeting three primary sites: Bones: PTH promotes the release of calcium from bone reserves. This process, known as bone resorption, involves the breakdown of bone tissue by osteoclasts. While osteoclasts don't possess PTH receptors, PTH indirectly stimulates them by binding to osteoblasts, the bone-forming cells. This binding triggers osteoblasts to increase RANKL expression, a molecule that interacts with RANK receptors on osteoclast precursors, promoting their fusion into mature, bone-resorbing osteoclasts. Kidneys: PTH enhances active calcium reabsorption in the distal tubules and the thick ascending limb of the nephrons, reducing calcium loss through urine. Intestines: PTH indirectly boosts intestinal calcium absorption by stimulating the production of vitamin D and upregulating the enzyme responsible for converting vitamin D to its active form, 1,25-dihydroxy vitamin D. Active vitamin D enhances calcium absorption in the intestines via calbindin, a calcium-binding protein. Recombinant human full-length PTH 1-84 shows promise as an anti-osteoporotic agent due to its bone formation-stimulating properties. It increases bone turnover, stimulates osteoblasts, and reduces both vertebral and non-vertebral fractures.
Description
Recombinant Human Parathyroid Hormone (C181H290N55O51S2), produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 84 amino acids with a molecular weight of 4117.8 Daltons. The purification process involves proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The protein (1 mg/ml) underwent lyophilization after extensive dialysis against a buffer containing 1.15 mg sodium citrate, 7.31 mg sodium chloride, 0.21 mg citric acid, 0.1117 mg EDTA-Na2, 0.2 mg Tween 80, and 50 mg Mannitol.
Solubility
For reconstitution, it is recommended to dissolve the lyophilized Parathyroid Hormone in sterile 18 MΩ-cm H2O at a concentration not less than 100 µg/ml. Further dilutions can be prepared in other aqueous solutions.
Stability
Lyophilized Parathyroid Hormone remains stable at room temperature for up to 3 weeks but should be stored desiccated at -18°C or below for extended periods. After reconstitution, the PTH solution should be stored at 4°C for 2-7 days or frozen at -18°C for future use. For long-term storage, adding a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 98.0% as determined by: (a) RP-HPLC analysis (b) SDS-PAGE analysis
Biological Activity
The biological activity, determined using the UMR106 cell/cAMP assay, corresponds to a specific activity of 10,000 Units/mg.
Synonyms
Parathyrin, PTH, Parathormone.
Source
Escherichia Coli.
Amino Acid 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.

Product Science Overview

Introduction

Parathyroid Hormone (1-34) (Human Recombinant), also known as Teriparatide, is a synthetic form of the natural parathyroid hormone (PTH). It consists of the first 34 amino acids of the full-length human parathyroid hormone, which is crucial for its biological activity. This recombinant form is used primarily in the treatment of osteoporosis, a condition characterized by weak and brittle bones.

Biological Function

Parathyroid hormone plays a vital role in regulating calcium levels in the blood. It achieves this by stimulating the release of calcium from bones, increasing calcium absorption in the intestines, and promoting calcium reabsorption in the kidneys. The recombinant form, Teriparatide, mimics these actions and is used to stimulate bone formation.

Mechanism of Action

Teriparatide acts on the parathyroid hormone 1 receptor (PTH1R), which is found in bone and kidney tissues. When administered, it stimulates bone remodeling by promoting the activity of osteoblasts (cells responsible for bone formation) over osteoclasts (cells responsible for bone resorption). This leads to an increase in bone mineral density (BMD) and overall bone strength .

Clinical Applications

Teriparatide is primarily used in the treatment of osteoporosis in postmenopausal women and men at high risk of fractures. It has been shown to significantly reduce the risk of vertebral and non-vertebral fractures by increasing bone mass and improving bone architecture . It is administered as a daily subcutaneous injection.

Safety and Efficacy

Clinical trials have demonstrated that Teriparatide is effective in increasing bone mineral density and reducing fracture risk. However, there are concerns about its long-term safety, particularly its potential to cause osteosarcoma (a type of bone cancer) based on studies in rats . Despite these concerns, the benefits of Teriparatide in treating osteoporosis often outweigh the risks, especially in patients with severe osteoporosis .

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