GH Human, Plant

Growth Hormone Human Recombinant, Plant
Cat. No.
BT13413
Source
Nicotiana benthamiana plant
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 97.0% as determined by 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

GH human Recombinant produced in Nicotiana benthamiana plant is a single chain containing 205 amino acids (molecular formula C1025H1570N280O306S7) and 6-His-tag at the N-terminal having the total molecular mass of 22.9kDa.

Product Specs

Introduction
Growth Hormone (GH) belongs to the somatotropin/prolactin hormone family, which are essential for regulating growth. The GH gene resides within the growth hormone locus on chromosome 17, clustered with four other related genes. This arrangement, where the genes share the same transcriptional orientation, is believed to have arisen from gene duplication events. The five genes exhibit significant sequence similarity. Alternative splicing further contributes to the diversity of growth hormones by generating additional isoforms, potentially enabling functional specialization. Unlike the other four genes at this locus, which are expressed in placental tissue, this specific family member is expressed in the pituitary gland. Mutations or deletions affecting this gene can lead to growth hormone deficiency, resulting in short stature.
Description
Recombinant human Growth Hormone (GH), produced in Nicotiana benthamiana plants, is a single-chain protein comprised of 205 amino acids. Its molecular formula is C1025H1570N280O306S7, and it includes a 6-His-tag at the N-terminal. The protein has a molecular mass of 22.9 kDa.
Physical Appearance
White, lyophilized (freeze-dried) powder, sterile filtered.
Formulation
Lyophilized from a solution containing 1 mg/ml GH in 0.05 M PBS buffer at pH 7.5.
Solubility
To reconstitute the lyophilized GH, it is recommended to dissolve it in sterile 18 M-cm H2O at a concentration of at least 100 µg/ml. This solution can be further diluted into other aqueous solutions as needed.
Stability
Lyophilized GH remains stable at room temperature for up to 3 weeks. However, for extended storage, it should be stored desiccated at a temperature below -18°C. Once reconstituted, GH can be stored at 4°C for 2-7 days. For long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is recommended. It is crucial to avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 97.0% as determined by SDS-PAGE analysis.
Biological Activity
The biological activity of human Growth Hormone is evaluated by measuring cell proliferation using Nb2-11 cells. The ED50 is less than 0.04-0.1 ng/mL.
Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Source
Nicotiana benthamiana plant
Amino Acid Sequence
HHHHHHFPTI PLSRPFDNAM LRAHRLHQLA FDTYQEFEEA YIPKEQKYSF LQNPQTSLCF SESIPTPSNR EETQQKSNLE LLRISLLLIQ SWLEPVQFLR SVFANSLVYG ASDSNVYDLL KDLEEGIQTL MGRLEDGSPR TGQIFKQTYS KFDTNSHNDD ALLKNYGLLY CFRKDMDKVE TFLRIVQCRS VEGSCGFAG

Product Science Overview

Introduction

Growth hormone (GH), also known as somatotropin, is a peptide hormone that plays a crucial role in stimulating growth, cell reproduction, and cell regeneration in humans and other animals . Human growth hormone (hGH) is particularly important for human development and has various biological functions, including protein synthesis, cell proliferation, and metabolism .

Recombinant Growth Hormone

Recombinant DNA technology has revolutionized the production of growth hormones. Initially, growth hormone was extracted from human pituitary glands, but this method had limitations, including the risk of contamination and limited supply . The advent of recombinant DNA technology allowed for the production of hGH in various host systems, including bacteria, yeast, and mammalian cells .

Plant-Based Expression Systems

In recent years, plant-based expression systems have emerged as a promising alternative for producing recombinant proteins, including hGH. Plant systems offer several advantages over traditional animal and yeast systems:

  • Safety: Plant-based systems are free from human or animal pathogens, reducing the risk of contamination.
  • Cost-Effectiveness: Plants can be grown at a lower cost compared to animal cell cultures.
  • Scalability: Plants can be cultivated on a large scale, providing a potentially limitless source of recombinant proteins .
Molecular Pharming

Molecular pharming refers to the use of genetically modified plants to produce pharmaceutical proteins. This approach has gained attention due to its potential to produce therapeutic proteins, antibodies, and enzymes at a lower cost and with fewer safety concerns . Plant-based expression systems can utilize various plant tissues, such as seeds, leaves, and roots, to produce recombinant proteins. These systems can employ stable transformation of the nuclear genome or transient expression methods to achieve high yields of the desired protein .

Production of Recombinant hGH in Plants

The production of recombinant hGH in plants involves several steps:

  1. Gene Cloning: The gene encoding hGH is cloned into a suitable plant expression vector.
  2. Transformation: The expression vector is introduced into plant cells using techniques such as Agrobacterium-mediated transformation or biolistic particle delivery.
  3. Expression: The transformed plant cells express the hGH gene, producing the recombinant protein.
  4. Purification: The recombinant hGH is extracted and purified from the plant tissues using various biochemical techniques .
Advantages and Challenges

Advantages:

  • Low Risk of Contamination: Plant-based systems are free from human pathogens.
  • Cost-Effective Production: Lower production costs compared to animal cell cultures.
  • Scalability: Potential for large-scale production.

Challenges:

  • Regulatory Approval: Ensuring that plant-derived recombinant proteins meet regulatory standards for therapeutic use.
  • Yield Optimization: Improving the yield and stability of recombinant proteins in plant systems.
  • Post-Translational Modifications: Ensuring that plant-derived proteins undergo appropriate post-translational modifications, such as glycosylation, to maintain their functionality .

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.