GHBP Human, Sf9
GHR, GHBP, GHIP.
Greater than 95.0% as determined by SDS-PAGE.
Description
GHBP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 254 amino acids (19-264aa) and having a molecular mass of 29.4kDa.
GHBP is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
Growth Hormone Binding Protein (GHBP) is a protein belonging to the cytokine receptor superfamily. It binds to two Growth Hormone (GH) receptors, facilitating signal transduction through receptor dimerization. At high concentrations, GHBP acts as an antagonist due to variations in binding site affinities. This antagonistic effect is amplified when the binding site affinity is reduced.
Human GHBP, produced in Sf9 insect cells using a baculovirus expression system, is a single, glycosylated polypeptide chain. It consists of 254 amino acids (19-264aa) with a molecular weight of 29.4kDa. An 8 amino acid Histidine tag is fused to the C-terminus of the GHBP protein. Purification is achieved through proprietary chromatographic methods.
The GHBP solution is provided at a concentration of 1mg/ml and contains 10% glycerol in a phosphate-buffered saline solution (pH 7.4).
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
The purity of GHBP is determined by SDS-PAGE analysis and is greater than 95.0%.
The biological activity of GHBP is assessed by its ability to inhibit GH-induced proliferation of Nb2-11 rat lymphoma cells in the presence of 1.25ng/ml human growth hormone. The ED50 for this inhibitory effect is less than or equal to 10ng/ml.
GHR, GHBP, GHIP.
FSGSEATAAI LSRAPWSLQS VNPGLKTNSS KEPKFTKCRS PERETFSCHW TDEVHHGTKN LGPIQLFYTR RNTQEWTQEW KECPDYVSAG ENSCYFNSSF TSIWIPYCIK LTSNGGTVDE KCFSVDEIVQ PDPPIALNWT LLNVSLTGIH ADIQVRWEAP RNADIQKGWM VLEYELQYKE VNETKWKMMD PILTTSVPVY SLKVDKEYEV RVRSKQRNSG NYGEFSEVLY VTLPQMSQFT
CEEDFYLEHH HHHH
Product Science Overview
GHBP was first identified in 1986 and has since been recognized in various species . The high-affinity human GHBP is a 60-kilodalton (kDa), 246-amino acid, single-chain glycoprotein. It corresponds to the extracellular domain of the GH-R and is believed to arise from the receptor through proteolytic cleavage . The precise site of cleavage and the enzyme responsible remain unknown, although it is suggested that a free cysteine’s sulfhydryl group in the cleavage region may play a significant role .
GHBP binds to GH with high specificity, rapid association, and slower dissociation rates, allowing it to efficiently bind and release GH in the circulation . This dynamic equilibrium ensures that approximately 45% of circulating GH is complexed with GHBP . The binding of GH to GHBP modulates the hormone’s bioavailability and activity, playing a critical role in growth regulation and metabolic processes.
The production of recombinant GHBP involves expressing the protein in suitable host systems, such as Sf9 insect cells. The Sf9 cell line, derived from the fall armyworm (Spodoptera frugiperda), is commonly used for recombinant protein production due to its high expression levels and ability to perform post-translational modifications .
Recombinant GHBP is used in various research and clinical applications, including studying GH action mechanisms, developing GH analogs, and investigating GH-related disorders . The recombinant form of GHBP has been characterized in great structural detail, providing valuable insights into its binding kinetics and physiological roles .
In conclusion, GHBP is a vital component in the regulation of GH activity, and its recombinant production in systems like Sf9 cells has significantly advanced our understanding of GH physiology and its therapeutic potential.
