GH Ovine

Growth Hormone Ovine Recombinant
Cat. No.
BT13678
Source
Escherichia Coli.
Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek'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

Growth Hormone Ovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids and having a molecular mass of 22015 Dalton.
The GH Ovine Recombinant is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Growth Hormone (GH) belongs to the somatotropin/prolactin family of hormones, known for their crucial role in regulating growth. The GH gene resides within the growth hormone locus on chromosome 17, alongside four related genes, arranged in the same transcriptional orientation. This arrangement is believed to be a result of gene duplication events. These five genes exhibit remarkable sequence similarity. Alternative splicing further diversifies these growth hormones, producing additional isoforms with specialized functions. While expressed in the pituitary gland, this specific family member, unlike the other four genes in the growth hormone locus, is not found in placental tissue. Mutations or deletions in the GH gene are linked to growth hormone deficiency and short stature.
Description
Recombinant Ovine Growth Hormone, produced in E.Coli, is a single, non-glycosylated polypeptide chain comprised of 200 amino acids, with a molecular weight of 22015 Daltons. The purification of Recombinant Ovine GH is achieved using proprietary chromatographic methods.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein was lyophilized from a concentrated solution (1mg/ml) containing 0.0045mM NaHCO3.
Solubility
To reconstitute the lyophilized Growth Hormone, it is recommended to dissolve it in sterile 18MΩ-cm H2O to a concentration not less than 100µg/ml. This solution can be further diluted using other aqueous solutions.
Stability
Lyophilized Growth Hormone, while stable at room temperature for up to 3 weeks, should be stored in a dry environment below -18°C. Once reconstituted, Ovine GH should be stored at 4°C for a period of 2-7 days. For long-term storage, freezing below -18°C is recommended. To enhance stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is advisable. Avoid repeated freeze-thaw cycles.
Purity
Exceeds 98.0% as determined by:
(a) Size Exclusion Chromatography-High Performance Liquid Chromatography (SEC-HPLC) analysis.
(b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Biological Activity
The biological activity is evaluated by measuring the dose-dependent stimulation of proliferation in FDCP13B9 cells.
Protein Content
Protein quantification was performed using two independent methods:
1. UV spectroscopy at 280 nm, utilizing an absorbance value of 0.7 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is determined using the PC GENE computer analysis program for protein sequences (IntelliGenetics).

2. Reverse-Phase High Performance Liquid Chromatography (RP-HPLC) analysis, employing a calibrated Growth Hormone solution as a reference standard.
Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Source
Escherichia Coli.
Amino Acid Sequence
1     afpamslsgl fanavlraqh lhqlaadtfk efertyipeg qrysiqntqv 
51    afcfsetipa  ptgkneaqqk sdlellrisl lliqswlgpl qflsrvftns 
101  lvfgtsdrvy eklkdleegi lalmreledv tpragqilkq tydkfdtnmr 
151  sddallknyg llscfrkdlh ktetylrvmk  crrfgeasca f

Product Science Overview

Historical Context

The development of recombinant DNA technology in the late 20th century paved the way for the production of recombinant proteins, including growth hormones. The heterologous expression and production of recombinant growth hormones from various species, such as bovine, porcine, and ovine, have been extensively studied . The ability to produce these hormones in large quantities has significant implications for both agricultural and medical applications.

Production and Expression

Recombinant ovine growth hormone is typically produced using Escherichia coli (E. coli) as a host organism. The process involves inserting the gene encoding the ovine growth hormone into the E. coli genome, allowing the bacteria to produce the hormone. Various factors, such as temperature, induction conditions, and media composition, are optimized to achieve high yields of biologically active roGH .

One notable study demonstrated the expression of roGH targeted to the inner membrane of E. coli using a signal sequence, DsbA. This approach resulted in a relatively high soluble protein yield of 65.3 mg/L, with the protein being easily solubilized and purified .

Biological Function

Ovine growth hormone consists of 190 or 191 amino acids with two disulfide bridges. It significantly enhances whole-body growth rate by stimulating protein synthesis with minimal effect on protein degradation . Additionally, it has been shown to increase milk and meat production in animals, making it a valuable tool in the agricultural industry .

Applications

The primary applications of recombinant ovine growth hormone include:

  1. Agriculture: Enhancing growth rates and productivity in livestock, leading to increased meat and milk production.
  2. Research: Studying the effects of growth hormones on various biological processes and developing new therapeutic approaches for growth-related disorders.
Challenges and Future Directions

Despite the promising applications, the production and use of recombinant growth hormones face several challenges. These include regulatory hurdles, ethical concerns, and potential side effects. Future research aims to address these challenges by improving production methods, ensuring safety, and exploring new applications.

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.