(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
Activity
Measured by its binding ability in a functional ELISA. Immobilized GH1 (CSB-MP009407HU) at 1 μg/ml can bind human GHR, the EC50 of human GHR protein is 24.96-33.39 ng/ml.
Human GH1 protein his/myc tag (CSB-MP009407HU) captured on COOH chip can bind Human GHR protein Fc tag (CSB-MP009411HU) with an affinity constant of 6.1 nM as detected by LSPR Assay.
The extracellular ligand-binding domain of human growth hormone receptor (residues 27–264) demonstrates high-affinity interaction with GH1, yielding a KD of 6.1 nM by LSPR and an EC50 of 24.96–33.39 ng/ml in functional ELISA—data that supports use in receptor-ligand interaction assays, affinity characterization by SPR or BLI, and competitive inhibition studies for blocking antibody screening. Mammalian cell expression preserves native glycosylation and disulfide bonding critical for conformational integrity of this domain, making the protein appropriate for therapeutic antibody epitope mapping and small-molecule inhibitor screening in oncology-focused drug discovery. The C-terminal hFc1 tag facilitates oriented capture on Protein A surfaces, providing a suitable basis for ligand-binding assays and positive controls, while purity exceeding 90% by SDS-PAGE and endotoxin levels below 1.0 EU/μg satisfy criteria typical for cell-based functional studies.
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