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Growth Hormone Binding Protein

ovine (sheep), recombinant, E. coli

Cat. No. Amount Price (EUR) Buy / Note
PR-433 100 μg 471,50 Add to Basket/Quote Add to Notepad

For in vitro use only!

Shipping: shipped at ambient temperature

Storage Conditions: store at -20 °C
avoid freeze/thaw cycles

Shelf Life: 12 months

Molecular Weight: 22 kDa

Accession number: P67930

Accession number: P67930

Purity: > 95 % (SDS-PAGE, RP-HPLC)

Form: lyophilised (GH was lyophilised from a 1 mg/ml solution with 0.0045 mM NaHCO3)

Solubility: It is recommended to reconstitute the lyophilised GH in sterile bidest H2O not less than 100 μg/ml, which can then be further diluted to other aqueous solutions. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).

The Growth Hormone (GH) is a polypeptide that is secreted by the adenohypophysis. Growth hormone, also known as somatotropin, stimulates mitosis, cell differentiation and cell growth. Species-specific growth hormones have been synthesized. GH augments the cytolytic activity of T-cells, antibody synthesis, and granulocyte differentiation induced by GM-CSF. GH also enhances production of TNF-alpha, generation of superoxide anions from peritoneal macrophages, and natural killer activity. Recombinant Ovine Growth Hormone produced in E. coli is a single, non-glycosylated polypeptide chain containing 200 amino acids and having a molecular mass of 22.015 kDa. Recombinant Ovine GH is purified by proprietary chromatographic techniques.

Endotoxin: Less than 0.1 ng/μg (IEU/μg) of GH.

Selected References:
Gupta et al. (2003) Optimization of immobilized metal ion affinity chromatography for single-step purification of recombinant ovine growth hormone expressed in Escherichia coli. J. Chromatogr. A. 998:93.
Adams et al. (2002) The impact of a transgene for ovine growth hormone on the performance of two breeds of sheep. J. Anim. Sci. 80:2325.
Panda et al. (1999) Kinetics of inclusion body production in batch and high cell density fed-batch culture of Escherichia coli expressing
ovine growth hormone. J. Biotechnol. 75:161.
Puri et al. (1999) Effect of the codon following the ATG start site on the expression of ovine growth hormone in Escherichia coli. Protein Expr. Purif. 17:215.
Sami et al. (1999) Production and character isation of deletion mutants of ovine growth hormone. J. Mol. Endocrinol. 23:97.
Allan et al. (1999) Identification of novel sites in the ovine growth hormone receptor involved in binding hormone and conferring species specificity. Eur. J. Biochem. 261:555.