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Manufactured by BioVendor

Growth Hormone Mouse E. coli Recombinant

  • Regulatory status:RUO
  • Source:E. coli
  • Other names:GH
  • Species:Mouse
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Cat. No. Size Price


New RP1765400100 100 μg
New RP1765401000 1 mg
New RP1765400200 200 μg
PubMed Product Details
Technical Data

Description

Mouse Growth Hormone Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids and having a molecular mass of 22 kDa. Mouse GH is purified by proprietary chromatographic techniques.

Amino Acid Sequence

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

Source

E. coli

Purity

Greater than 95.0% as determined by (a) Analysis by RP-HPLC, (b) Analysis by SDS-PAGE.

Biological Activity

BioVendor’s GH is contains 3 units/mg.

Formulation

Mouse Growth Hormone Recombinant contains 50mM Tris-HCl, pH8.0, 150mM NaCl buffer.

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Lyophilized mouse Growth Hormone although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution mouse 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 prevent freeze-thaw cycles.

Physical Appearance

Sterile filtered white lyophilized (freeze-dried) powder.

Summary

Research topic

Growth hormone and factor-related products

Summary

The endocrine system of human Growth Hormone (hGH), also named Somatropin, is characterized by an extreme complexity. hGH is the product of the GH-1 gene located on chromosome 17 and expressed in pituitary cells. 80% of the gene expression results in a non-glycolsylated 22 kDa protein consisting of 191 amino acids. The other 20% of gene expression results in a variant form of 20 kDa by alternative splicing. Additionally, several more smaller variants can be found in circulation as well as translational modificated proteins and different degrees of protein aggregation. Further on, bioactivity of Growth Hormone is regulated by a specific binding protein (GHBP) formed by the extra cellular part of the cellular transmembran GH-receptor. These modifications allow a tight control of the half-life period hGH and of its bioactivity. GH is species specific. Not only synthesis and posttranslational modification but also secretion of hGH is tightly regulated. Spontaneous pulsatile secretion takes place with a single pulse every three hours and a maximal secretion during night’s sleep. Several different attractions as physiologic stress or hypoglycaemia and amino acids result in additional hGH secretion, induced by the hypothalamic hormones Somatostatin and GH-Releasing Hormone (GHRH). Age, sexual steroids, nutritional status, illness and emotions influence the amount of secreted hGH. Because of the multitude of influencing factors the normal quantitative secretion is not known. Physiological functions are partially exerted by Insulin-like Growth Factors (IGFs). In children and adolescent the hGH system is the main regulator of growth. If the hGH system fails totally, human growth will end at 120 cm. Beside regulation of growth hGH exerts an anabolic effect on muscle and connective tissue as wells as on bone and different other organs (heart, intestine). Further hGH was proved to have a lipolytic effect. Growth Hormone pathology is characterized by extreme high or extreme low hGH secretion. During childhood it is the Growth Hormone deficiency congenital or acquired, which leads to microsomia. For diagnosis of Growth Hormone deficiency an hGH stimulation test has to be done or the spontaneous excretion must be investigated. The therapy consists of substitution of endogenous Growth Hormone by recombinant hGH resulting in normalization of growth. In adulthood hGH deficiency is mostly caused by pituitary adenoma (and their surgical excision). hGH deficiency shows typical disease pattern, equivalent to advanced aging (adipositas, muscle dystrophy, arteriosclerosis, osteoporosis, adynamia). Substitutional therapy is a well-known, approved and efficient therapy of severe Growth Hormone deficiency in adulthood. Therapeutical success is directly as well as indirectly proved by measurement of IGF in serum. Excessive hGH secretion, mostly causes by pituitary adenoma, results in childhood in gigantism, in adulthood in acromegalie, leading to enlarged extremities, diabetes, heart insufficiency and tumor growth. Surgical excision of the adenoma is the therapy of choice. If tumor excision is not possible or incomplete, a medicinal therapy with somatostatin preparation will be conducted, resulting in inhibition of hGH production. Alternatively hGH analoga (e.g. Pegvisomat) are used to block the hGH receptor and thereby inhibit action of endogenous hGH. Determination of human Growth Hormone (hGH, Somatropin) is done for diagnostic of Growth Hormone deficiency or Growth Hormone excess (arcomegaly). During medicinal and/or after surgical therapy of arcomegaly Growth Hormone (and IGF-I) measurement is used for therapy control.

References to Summary

References to Growth Hormone

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  • Camanni F, Massara F, Belforte L, Rosatello A, Molinatti GM. Effect of dopamine on plasma growth hormone and prolactin levels in normal and acromegalic subjects. J Clin Endocrinol Metab. 1977 Mar;44 (3):465-73
  • Celniker AC, Chen AB, Wert RM Jr, Sherman BM. Variability in the quantitation of circulating growth hormone using commercial immunoassays. J Clin Endocrinol Metab. 1989 Feb;68 (2):469-76
  • Crowley S, Hindmarsh PC, Matthews DR, Brook CG. Growth and the growth hormone axis in prepubertal children with asthma. J Pediatr. 1995 Feb;126 (2):297-303
  • Daughaday WH. The adenohypophysis In: "Textbook of Endocrinology", R.H. Williams ed., W.B. Saunders. 1981;Philadelphia, p;73
  • Daughaday WH, Cryer PE. Growth hormone hypersecretion and acromegaly. Hosp Pract. 1978 Aug;13 (8):75-80
  • Drobny EC, Amburn K, Baumann G. Circadian variation of basal plasma growth hormone in man. J Clin Endocrinol Metab. 1983 Sep;57 (3):524-8
  • Eddy RL, Gilliland PF, Ibarra JD Jr, McMurry JF Jr, Thompson JQ. Human growth hormone release. Comparison of provocative test procedures. Am J Med. 1974 Feb;56 (2):179-85
  • Frasier SD. A preview of growth hormone stimulation tests in children. Pediatrics. 1974 Jun;53 (6):929-37
  • Goldfine ID. Medical treatment of acromegaly. Annu Rev Med. 1978;29:407-15
  • Hashida S, Nakagawa K, Ishikawa E, Ohtaki S. Basal level of human growth hormone (hGH) in normal serum. Clin Chim Acta. 1985 Sep 30;151 (2):185-6
  • Kelly JJ, Rajkovic IA, O'Sullivan AJ, Sernia C, Ho KK. Effects of different oral oestrogen formulations on insulin-like growth factor-I, growth hormone and growth hormone binding protein in post-menopausal women. Clin Endocrinol (Oxf). 1993 Nov;39 (5):561-7
  • Lewis UJ, Singh RN, Tutwiler GF, Sigel MB, VanderLaan EF, VanderLaan WP. Human growth hormone: a complex of proteins. Recent Prog Horm Res. 1980;36:477-508
  • LI CH. Human growth hormone: perspective on its chemistry and physiology. In: "Advances in human growth hormone research", S. Raiti ed. U.S. Department of Health, Education and Welfare Publ. DMEW publ. no. (NJH). 74-612, p. 321;
  • Reutens AT, Hoffman DM, Leung KC, Ho KK. Evaluation and application of a highly sensitive assay for serum growth hormone (GH) in the study of adult GH deficiency. J Clin Endocrinol Metab. 1995 Feb;80 (2):480-5
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