GHBP Human
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.
Description
GHBP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids and having a molecular mass of 28107.01 Dalton.
GHR is purified by proprietary chromatographic techniques.
Product Specs
Growth hormone binding protein (GHBP) is a transmembrane receptor that binds to growth hormone (GH). Upon binding, the receptor forms a dimer, initiating intracellular and intercellular signaling pathways that promote growth. A notable variant of this gene, GHRd3, lacks exon three and has been extensively studied. Mutations in the GHBP gene have been linked to Laron syndrome, also referred to as growth hormone insensitivity syndrome (GHIS), a disorder characterized by restricted growth. Although additional splice variants exist, such as one encoding a soluble form of the protein (GHRtr), they have not been fully characterized.
Recombinant human GHBP, produced in E.Coli, is a single, non-glycosylated polypeptide chain composed of 248 amino acids, with a molecular weight of 28107.01 Dalton. GHR is purified using proprietary chromatographic methods.
To reconstitute the lyophilized GHBP, it is advised to dissolve it in sterile 18MΩ-cm H2O to a concentration not lower than 100µg/ml. The solution can be further diluted in other aqueous solutions if needed.
Lyophilized GHBP, while stable at room temperature for up to 3 weeks, should ideally be stored in dry conditions below -18°C. After reconstitution, GHBP should be stored at 4°C for 2-7 days. For long-term storage, it is recommended to store it below -18°C. To enhance stability during long-term storage, consider adding a carrier protein such as HSA or BSA (0.1%). Avoid repeated freeze-thaw cycles.
(a) Size-exclusion high-performance liquid chromatography (SEC-HPLC) analysis.
(b) Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
GHBP demonstrates full biological activity, as evidenced by its capacity to form a 2:1 complex with growth hormone.
1. UV spectroscopy at 280 nm, employing an absorbance value of 2.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value was determined using the PC GENE computer analysis program for protein sequences (IntelliGenetics).
2. Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis, utilizing a calibrated GHBP solution as a reference standard.
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Product Science Overview
Growth Hormone Binding Protein (GHBP) is a crucial component in the regulation of growth hormone (GH) activity in the human body. GHBP is derived from the extracellular domain of the Growth Hormone Receptor (GH-R) and plays a significant role in modulating the availability and activity of GH in the bloodstream.
The high-affinity human GHBP was first described in 1986 . It is a 60-kilodalton (kDa), 246-amino acid, single-chain glycoprotein. This protein 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 for this process remain unknown, although it is suggested that the sulfhydryl group of a free cysteine in the region of cleavage may play a crucial role in proteolysis .
GHBP is highly specific for human GH, with a rapid association rate and a slower dissociation rate. It circulates in the blood at nanomolar concentrations, allowing it to efficiently bind and release GH in the circulation . Approximately 45% of circulating GH is complexed with GHBP, creating a dynamic equilibrium that regulates GH availability .
The physiological significance of GHBP lies in its ability to modulate the bioavailability of GH. By binding to GH, GHBP can prolong the half-life of GH in the bloodstream, thereby enhancing its biological activity. However, studies have shown that recombinant GHBP does not enhance the in vivo bioactivity of GH in normal rats, indicating that the role of GHBP in GH bioactivity may be more complex than initially thought .
Recombinant GHBP has been characterized in great structural detail. It is produced using recombinant DNA technology, which involves inserting the gene encoding GHBP into a host organism, such as bacteria or yeast, to produce the protein in large quantities. This recombinant form of GHBP is used in various research and clinical applications to study its structure, function, and potential therapeutic uses .
GHBP has attracted considerable attention among basic scientists and clinicians due to its role in GH regulation. It is used in research to study the mechanisms of GH action and its interactions with GHBP. Clinically, GHBP levels are measured to assess GH activity and diagnose GH-related disorders. For example, low levels of GHBP may indicate GH deficiency, while high levels may be associated with conditions such as acromegaly .
