GH Gilthead Seabream

Growth Hormone Gilthead Seabream Recombinant
Cat. No.
BT12928
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.
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Description

Somatotropin Gilthead Seabream Recombinant Sparus Aurata produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21.4 kDa.
The Gilthead Seabream Growth-Hormone Recombinant is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Growth hormone (GH) belongs to the somatotropin/prolactin hormone family, which are crucial for growth regulation. This gene, along with four others, forms the growth hormone locus on chromosome 17. These genes share the same transcriptional orientation, suggesting evolution through gene duplication. Notably, they exhibit high sequence similarity. Alternative splicing further amplifies this diversity by generating various isoforms of the five growth hormones, potentially enabling specialized functions. Unlike the other four genes in the growth hormone locus, this specific gene is expressed in the pituitary gland but not in placental tissue. Mutations or deletions in this gene result in growth hormone deficiency, leading to short stature.
Description
Recombinant Somatotropin Gilthead Seabream (Sparus aurata), produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 188 amino acids. It features an additional Alanine residue at the N-terminus and has a molecular weight of 21.4 kDa. The purification of Recombinant Gilthead Seabream Growth Hormone is achieved through proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The protein was lyophilized from a concentrated solution (1 mg/ml) containing 0.02% sodium bicarbonate (NaHCO3).
Solubility
To reconstitute the lyophilized Gilthead Seabream Growth Hormone, it is recommended to dissolve it in 0.4% sodium bicarbonate (NaHCO3) or water adjusted to a pH of 8-9. The initial concentration should be at least 100 µg/ml. This solution can be further diluted into other aqueous solutions. For optimal results, consider using a carrier protein like bovine serum albumin (BSA) or a similar agent during dilution.
Stability
Lyophilized Gilthead Seabream Growth Hormone remains stable at room temperature for a minimum of two weeks. However, for long-term storage, it is recommended to store it in a desiccated state below -18°C. After reconstitution and filter sterilization, GH can be stored at 4°C at a pH of 9 for up to 4 weeks. For extended storage periods or when working with more diluted solutions, adding a carrier protein (0.1% human serum albumin (HSA) or BSA) is advisable. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 98.0% through the following methods: (a) Size-Exclusion High-Performance Liquid Chromatography (SEC-HPLC) analysis. (b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Biological Activity
Binding assays, using radiolabeled (125I) gilthead seabream GH and dolphin fish liver microsomal fraction, demonstrated high specific binding. This binding was characterized by a dissociation constant (Ka) of 1.93 nM and a maximum binding capacity (Bmax) of 540 fmol/mg of microsomal fraction protein. Similar to ovine placental lactogen, recombinant gilthead seabream Growth Hormone displayed growth-promoting effects when administered orally to Sparus aurata larvae or intraperitoneally to juvenile fish.
Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Source
Escherichia Coli.
Amino Acid Sequence

AQPITDGQRLFSIAVSRVQHLHLLAQRLFSDFESSLQTEEQPQLNKIFLQ

DFCNCDYIISPIDKHETQRSSVLKLLSISYRLVESWEFPSRSLSGGSAPR

NQISPKLSELKTGIHLLIRANEDGAEIFPDRSALQLAPYGNYYQSLGTDE

SLRRTYELLACFKKDMHKVETYLTVAKCRLSPEANCTL

Product Science Overview

Introduction

The gilthead seabream (Sparus aurata) is a valuable species in aquaculture due to its high market demand and nutritional value. Growth hormone (GH) plays a crucial role in regulating growth and metabolism in fish, making it a key focus for enhancing aquaculture productivity. Recombinant growth hormone (rGH) technology has been developed to produce GH in large quantities, facilitating its use in aquaculture.

Cloning and Expression

The cDNA coding for the mature gilthead seabream growth hormone (gsGH) was initially cloned into a pGEM-T vector. This cDNA was then transferred into a prokaryotic expression vector, pET-8, and expressed in Escherichia coli BL21 (DE3) cells upon induction with isopropyl β-D-1-thiogalactopyranoside (IPTG) . The expressed protein was found within the inclusion-body pellet, which was solubilized in 4.5 M urea, refolded at pH 11.3 in the presence of catalytic amounts of cysteine, and purified to over 98% purity .

Purification and Characterization

The recombinant gsGH was purified using gel-filtration on a Superdex column under non-denaturing conditions. The purified protein was identified as a monomeric alanyl-gsGH through partial amino acid N-terminal sequencing . Binding assays demonstrated high specific binding of the [125I]gsGH to gilthead seabream liver microsomal fractions, characterized by a dissociation constant (Kd) of 1.93 nM .

Biological Activity

Recombinant gsGH exhibited significant growth-stimulating activity when administered orally to gilthead seabream larvae or intraperitoneally to juvenile fish . This activity is comparable to that of ovine placental lactogen, indicating the potential of gsGH in promoting growth in aquaculture .

Metabolic Effects

Studies have shown that recombinant bovine growth hormone (rbGH) can induce metabolic remodeling in gilthead seabream. Intraperitoneal injection of extended-release rbGH in gilthead seabream fingerlings and juveniles resulted in enhanced somatic growth. This was achieved through increased lipolysis and glycogenolysis in the liver, higher lipid use, and lower protein oxidation in muscle tissues . The metabolic response favored protein sparing, promoting muscle growth by utilizing lipids as the primary energy source .

Applications in Aquaculture

The use of recombinant growth hormones in aquaculture offers several advantages:

  • Enhanced Growth: rGH can significantly improve growth rates in fish, leading to higher yields.
  • Improved Feed Efficiency: By promoting the use of lipids as an energy source, rGH can enhance feed efficiency.
  • Sustainable Production: The use of rGH can contribute to more sustainable aquaculture practices by reducing the reliance on wild fish stocks for feed.

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