GH Porcine
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY.They may not be used as drugs,agricultural or pesticidal products, food additives or household chemicals.
Description
Growth Hormone is purified by proprietary chromatographic techniques.
Product Specs
(a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) analysis.
(b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Product Science Overview
The development of recombinant porcine growth hormone began with the construction of a porcine cDNA library. This library was created using the reverse transcripts of the total mRNA isolated from porcine pituitary glands. Researchers screened out clones containing the pGH cDNA gene and sequenced them . The gene was then modified and expressed in Escherichia coli (E. coli) cells. Initially, the pGH produced in E. coli cells was present in the form of inclusion bodies and lacked biological activity. However, a procedure was developed to isolate pGH from E. coli cells, resulting in a highly purified and bioactive product .
The production of recombinant pGH involves the use of a temperature-inducible expression system for small-scale fermentation. In a 10-liter fermenter, the culture density can reach approximately 130 grams of wet cells per liter, with an expression level of around 60% . The recombinant pGH is then isolated and purified through a series of steps, ensuring a high level of purity and biological activity.
Recombinant pGH has been extensively studied for its potential applications in agriculture. When administered to pigs, it has been shown to significantly increase growth rates, feed efficiency, and muscle content . For example, Beijing Black hogs treated with pGH exhibited a 24.39% increase in growth rate and a 29.37% increase in feed efficiency . These improvements make recombinant pGH a valuable tool for enhancing livestock production and efficiency.
Beyond its agricultural applications, recombinant pGH also holds promise for research and therapeutic purposes. Studies have explored the use of transgenic pigs expressing human growth hormone (hGH) in their milk as a model for mass production of therapeutic proteins . This approach aims to purify hGH from transgenic pig milk and assess its potential for therapeutic use. The results indicate that the purified recombinant hGH from transgenic pig milk is biosimilar to commercially available somatropin, with no observed toxicological differences .
