SEMG1
SEMG1 (semenogelin 1, previously semenogelin I; aliases CT103 and SEMG) is a secreted protein and the predominant protein in semen. It helps form the gel matrix that encases ejaculated spermatozoa and is cleaved into peptides with distinct functions. Browse Assay Genie's current range of SEMG1 research reagents below, or read on for the biology behind the target.
SEMG1 is the predominant protein in semen. The secreted protein takes part in forming a gel matrix that encases ejaculated spermatozoa. It is made as a preproprotein and is processed by the prostate-specific antigen (PSA) protease into several peptide products, each with distinct functions. This proteolysis also breaks down the gel matrix, which allows the spermatozoa to move more freely.
Among the peptides released from SEMG1, SgI-29 is an antimicrobial peptide with antibacterial activity. Alpha-inhibin-92 and alpha-inhibin-31 are also derived from proteolytic degradation of semenogelin, and they inhibit the secretion of pituitary follicle-stimulating hormone. Studies of the SEMG1 protein therefore cover both its structural role in semen and the activities of its cleavage products.
The SEMG1 gene belongs to the semenogelin family. It lies in a gene cluster on chromosome 20 together with another similar semenogelin gene, SEMG2. The protein was formerly called semenogelin I, and the gene has also been listed under the aliases CT103 and SEMG. Researchers working on SEMG1 may use an SEMG1 antibody or an SEMG1 ELISA kit to study the intact protein and its processing, and should consider SEMG2 in parallel because of the close similarity between the two genes.
SEMG1 forms the gel matrix around ejaculated spermatozoa, and its PSA-mediated cleavage breaks the matrix down so that sperm move more freely.
The SEMG1-derived peptide SgI-29 has antibacterial activity, making the protein relevant to studies of host defence peptides in semen.
Alpha-inhibin-92 and alpha-inhibin-31, derived from semenogelin degradation, inhibit pituitary follicle-stimulating hormone secretion.
SEMG1 is a preproprotein processed by PSA protease into multiple peptides with distinct functions, offering a model for protease-substrate analysis.
SEMG1 is the predominant protein in semen and helps form the gel matrix that encases ejaculated spermatozoa. PSA protease cleaves it into peptides, which breaks down the matrix and frees the sperm. Some of these peptides have antibacterial or hormone-inhibiting activity.
The HGNC name is semenogelin 1, and the previous name was semenogelin I. Aliases and previous symbols include CT103 and SEMG. UniProt lists the protein as Semenogelin-1, and its processed products include SgI-29 and the alpha-inhibin peptides.
Yes. SEMG1 belongs to the semenogelin family and sits in a gene cluster on chromosome 20 with another similar semenogelin gene, SEMG2. Check the datasheet of any product for its validated reactivity.
The closely related semenogelin 2 gene product, which lies in the same chromosome 20 cluster, has its own page at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P04279; product specifications from Assay Genie datasheets.