Polyclonal antibody to Semenogelin II

Semenogelin I (SgI) and Semenogelin II (SgII) are the major seminal vesicle secreted proteins in human semen. SgI and SgII, in semen both originate from the glandular epithelium of the seminal vesicles which secrete them at high concentrations. Human Sg1 is a non-glycosylated protein of 439 amino acids with a molecular weight of ~50 kDa. A few percent of the worlds population also carry an allele that gives rise to a truncated SgI molecule with a molecular mass of 43 kDa. Human SgII is a 559 amino acid protein with a molecular weight of approx 63 kDa. SgII has a potential site for N-linked glycosylation and approximately half of the molecules in human semen are glycosylated yielding two SgII species with a different of 5 kDa. SgI has a single Cys residue and SgII has two Cys residues, and the molecules can exist as covalent homo- and heteromultimers. Whereas SgI/SgII was originally identified as the major components present in seminal vesicle secretion, they are now known to be expressed in a number of tissues. The list includes seminal vesicles, epididymis, vas deferens, prostate, skeletal muscle, kidney, colon, trachea, lung, breast and retina as well as in several malignant tissues and cell lines. The non-genital expression of SgI/SgII suggests that these proteins also have functions that are unrelated to sperm.