Name；GROWTH HORMONE, HUMAN
CAS；9002-72-6
Synonyms；
HGH
STH
GHN
phyol
phyone
SJ-011
POSILAC
somacton
HGH HUMAN
GH, HUMAN
BOVINE GH
EINECS(EC#)；232-666-5
MDL Number；MFCD00081960
Definition；
Hormone secreted by the anterior lobe of the pituitary. It causes an increase in general body growth and also affects carbohydrate and lipid metabolism.
storage temp. 2-8°C
form ；lyophilized powder
Basic Information；
Growth hormone (GH), also called human growth hormone (HGH or hGH) or somatotropic hormone, somatotropin is a single polypeptide chain of 191 amino acids[1](qv) having two disulfide bonds, one between Cys-53 and Cys-165, forming a large loop in the molecule, and the other between Cys-182 and Cys-189, forming a small loop near the C-terminus. The structure of GH is shown in Figure 1; molecular mass is 22,125; the empirical formula is C990H1529N262O300S7.
Purified GH is a white amorphous powder in its lyophilized form. It is readily soluble (concentrations>10 mg/mL) in dilute aqueous buffers at pH values above 7.2. The isoelectric point is 5.2 and the generally accepted value for the extinction coefficient at 280 nm is 17, 700 (M•cm)−1, although other values have been reported. The equilibrium denaturation of GH has been studied. A two-state mechanism is indicated with a Gibbs free energy of unfolding of 60.7 ± 4 kJ/mol (14.5 ± 1 kcal/mol).
In solution, GH exists predominantly as a monomer, with a small fraction as a dimer and higher molecular weight oligomers. Under certain conditions, GH can be induced to form larger amounts of dimers, trimers, and higher oligomers although the conditions leading to self-association are not well understood. GH is a globular protein having approximately 55% α-helical character, a value determined independently in studies using circular dichroism and Raman spectroscopy. A protein of a high degree of homology and structural similarity is porcine growth hormone, the crystal structure of which has been solved. This structure shows four antiparallel helices connected by strands of polypeptide having little structure. A crystal structure of GH complexed with the extracellular domain of its receptor has been reported. In this complex, the structure of GH is readily obvious and shows the four-helical bundle connected in an up–up–down–down fashion rather than the more common up–down–up–down. This work has convincingly shown that GH possesses two binding sites for its receptor and that the hormone functions by dimerizing its receptor on the cell membrane[2].
The product should be stored at –20 °C. The lyophilized product remains active for one year at –20 °C. Upon reconstitution, the cytokine can be stored at 2–8 °C for short term only or at –20 °C to –80 °C in aliquots for long term. Avoid repeated freeze-thaw cycles[3].
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