SEMG1 Human

Semenogelin I is a non-glycosylated protein consisting of 439 amino acid residues with a molecular mass of approximately 50 kDa . The primary structure of SgI includes motifs rich in glutamine, serine, glycine, and lysine residues, which are characteristic of both SgI and SgII . These motifs are highly conserved and play a significant role in the protein’s function.

The primary function of Semenogelin I is to form a gel matrix that encases ejaculated spermatozoa. This matrix is crucial for the initial immobilization of sperm, which is later broken down by the prostate-specific antigen (PSA) protease. The proteolysis of Semenogelin I by PSA results in smaller peptides that facilitate the release and motility of spermatozoa .

Semenogelin I is predominantly expressed in the seminal vesicles, but its transcripts and protein have also been detected in other tissues such as the vas deferens, prostate, epididymis, and trachea . Immunohistochemical studies have shown that the basal cell layer of the secretory epithelium in the prostate, trachea, and bronchi is stained by antibodies recognizing both SgI and SgII . This indicates that the expression of Semenogelin is not restricted to epithelial cells.

Human recombinant Semenogelin I is produced using recombinant DNA technology. This involves the insertion of the gene encoding Semenogelin I into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. The recombinant protein is then purified for various research and clinical applications.

Recombinant Semenogelin I is used in various research studies to understand its role in sperm motility and fertility. It is also utilized in the development of diagnostic assays for male fertility and in the study of prostate-specific antigen (PSA) activity. Additionally, the protein’s involvement in the formation and breakdown of the seminal coagulum makes it a potential target for contraceptive research.