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Recombinant Ovine Growth Hormone

Certificate of Analysis and Data Sheet

Source:
E.Coli

Catalog No.
CYT-237

Background:

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.

Description :

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 22015 Dalton. Recombinant Ovine GH is purified by proprietary chromatographic techniques.

Physical Appearance:

Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation:

Ovine-GH was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Solubility:

It is recommended to reconstitute the lyophilized Ovine-GH in sterile 18MΩ-cm H2O not less than 100ug/ml, which can then be further diluted to other aqueous solutions.

Stability:

Lyophilized Ovine-GH although stable at room temperature for 3 weeks, should be stored desiccated below -18 C. Upon reconstitution Ovine-GH should be stored at 4 C between 2-7 days and for future use below -18 C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

Purity:

Greater than 98.0% as determined by: (a) Analysis by RP-HPLC. (b) Anion-exchange FPLC. (c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained.

Amino-Acid Sequence :

The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Phe-Pro-Ala.

Dimers and aggregates:

Less than 1% as determined by silver-stained SDS-PAGE gel analysis.

Biological Activity:

ProSpec's Ovine Growth Hormone is fully biologically active when compared to standard. The activity as determined by the dose-dependant stimulation of the proliferation FDCP13B9 cells.

Endotoxin:

Less than 0.1 ng/ug (IEU/ug) of roGH.

Protein content:

Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.7 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of Ovine-GH as a Reference Standard.

Usage:

Prospec'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.


Gene:

Name:GH1

Protein synonyms/aliases:

Somatotropin precursor (Growth hormone).

Protein Family:

Belongs to the somatotropin/prolactin family.

Protein Domains:


Domains:
IPR001400   Somatotropin hormone

Related proteins:

Recombinant Human Prolactin
Recombinant Ovine Prolactin
Recombinant Human Placental-Corr Growth Hormone-22K
Recombinant Human Pituitary Growth Hormone-20K
Recombinant Rat Growth Hormone
Recombinant bream Growth Hormone

Protein links:

Recombinant Ovine Growth Hormone protein domain

Recombinant Ovine Growth Hormone protein family


Precursor- Protein structure and amino acid sequence:


Latest Publications:

1. Optimization of immobilized metal ion affinity chromatography for single-step purification of recombinant ovine growth hormone expressed in Escherichia coli.
J Chromatogr A 2003 May 23;998(1-2):93-101
2. The impact of a transgene for ovine growth hormone on the performance of two breeds of sheep.
J Anim Sci 2002 Sep;80(9):2325-33
3. Kinetics of inclusion body production in batch and high cell density fed-batch culture of Escherichia coli expressing ovine growth hormone.
J Biotechnol 1999 Oct 8;75(2-3):161-72
4. Effect of the codon following the ATG start site on the expression of ovine growth hormone in Escherichia coli.
Protein Expr Purif 1999 Nov;17(2):215-23
5. Production and characterisation of deletion mutants of ovine growth hormone.
J Mol Endocrinol 1999 Aug;23(1):97-106
6. Identification of novel sites in the ovine growth hormone receptor involved in binding hormone and conferring species specificity.
Eur J Biochem 1999 Apr;261(2):555-62

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中華民國95年06月06日更新