HCG, full name Human Chorionic Gonadotropin, is a heterodimeric glycoprotein hormone naturally secreted by placental trophoblast cells during early gestation. It belongs to the gonadotropin hormone family, sharing an identical alpha subunit with luteinizing hormone (LH), follicle-stimulating hormone (FSH) and thyroid-stimulating hormone (TSH). The unique β-subunit endows HCG with specific receptor binding characteristics, distinguishing it from other glycoprotein hormones. For laboratory applications, our HCG is produced via eukaryotic recombinant expression system, which supports proper glycosylation modification on both subunits. Glycosylation is critical to maintain molecular stability, receptor binding affinity and full biological activity, which cannot be achieved by simple synthetic peptides.

The primary biological function of HCG is binding to LH/CG receptors expressed on Leydig cells in testis and granulosa-lutein cells in ovary. In reproductive research models, HCG simulates the physiological function of luteinizing hormone, triggering multiple downstream signaling events. In male-related laboratory studies, it stimulates Leydig cells to synthesize and secrete testosterone, supporting research on testicular endocrine function and steroidogenesis. In female preclinical experiments, HCG can induce ovulation, promote corpus luteum formation and boost progesterone secretion, making it an essential reagent for reproductive physiology, follicle development and ovarian cell culture research.

Apart from core reproductive endocrinology research, HCG is widely used in multiple extended laboratory research areas. It participates in studies targeting steroid hormone synthesis pathways, G-protein coupled receptor (GPCR) signaling cascades, placental cell differentiation and pregnancy immune regulation. Researchers also utilize HCG to build animal models for investigating gonadal function, hormone receptor desensitization, and the crosstalk between reproductive hormones and metabolic homeostasis. Due to high similarity with LH in receptor activation, HCG serves as a cost-effective research substitute for LH in many in vitro cell assays.

Our recombinant HCG is produced in eukaryotic expression platform. After expression, the protein is purified through multi-step chromatography procedures, including affinity chromatography, ion exchange chromatography and size exclusion chromatography. These purification steps efficiently remove host cell proteins, residual genomic DNA, misfolded protein aggregates and unassembled free subunits. Each batch undergoes comprehensive quality control testing, including SDS-PAGE purity analysis, HPLC detection, endotoxin assay, biological activity calibration and appearance inspection. COA, SDS-PAGE images and activity test reports can be provided with each batch to meet laboratory quality archive and audit standards. The finished product adopts lyophilization technology to stabilize the heterodimer structure, preventing subunit dissociation during transportation and long-term cold storage. This product is supplied to university laboratories, biotech research institutes and pharmaceutical preclinical R&D teams for gonadal cell culture, steroidogenesis experiments, ovulation mechanism research, GPCR signaling exploration and reproductive toxicology studies.