Sf9, Baculovirus cells.
Pregnancy Specific Beta-1-Glycoprotein 1, PSBG1, B1G1, Fetal Liver Non-Specific Cross-Reactive Antigen 1/2, Pregnancy-Specific Beta-1 Glycoprotein C/D, CD66 Antigen-Like Family Member F, PS-Beta-C/D, PS-Beta-G-1, FL-NCA-1/2, PSBG-1, PSGGA, PSG95, SP1, Pregnancy-Specific Beta-1-Glycoprotein 1, Pregnancy-Specific B-1 Glycoprotein, Pregnancy-Specific Glycoprotein 1, CD66f Antigen, DHFRP2, PSGIIA, CD66f, PBG1, PSG1.
Greater than 90% as determined by SDS-PAGE.
PSG1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 394 amino acids (35-419a.a.) and having a molecular mass of 44.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PSG1 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Pregnancy Specific Beta-1-Glycoprotein 1, PSBG1, B1G1, Fetal Liver Non-Specific Cross-Reactive Antigen 1/2, Pregnancy-Specific Beta-1 Glycoprotein C/D, CD66 Antigen-Like Family Member F, PS-Beta-C/D, PS-Beta-G-1, FL-NCA-1/2, PSBG-1, PSGGA, PSG95, SP1, Pregnancy-Specific Beta-1-Glycoprotein 1, Pregnancy-Specific B-1 Glycoprotein, Pregnancy-Specific Glycoprotein 1, CD66f Antigen, DHFRP2, PSGIIA, CD66f, PBG1, PSG1.
Sf9, Baculovirus cells.
ADLQVTIEAE PTKVSEGKDV LLLVHNLPQN LTGYIWYKGQ MRDLYHYITS YVVDGEIIIY GPAYSGRETA YSNASLLIQN VTREDAGSYT LHIIKGDDGT RGVTGRFTFT LHLETPKPSI SSSNLNPRET MEAVSLTCDP ETPDASYLWW MNGQSLPMTH SLKLSETNRT LFLLGVTKYT AGPYECEIRN PVSASRSDPV TLNLLPKLPK PYITINNLNP RENKDVLNFT CEPKSENYTY IWWLNGQSLP VSPRVKRPIE NRILILPSVT RNETGPYQCE IRDRYGGIRS DPVTLNVLYG PDLPRIYPSF TYYRSGEVLY LSCSADSNPP AQYSWTINEK FQLPGQKLFI RHITTKHSGL YVCSVRNSAT GKESSKSMTV EVSGKWIPHH HHHH.
PSG1 is a highly glycosylated protein, consisting of a leader peptide followed by one N-terminal immunoglobulin variable region-like domain (N-domain) and two or three immunoglobulin constant region-like domains . The protein is primarily synthesized by the syncytiotrophoblast cells in the placenta and is the most abundant protein in the maternal bloodstream during the later stages of pregnancy .
The primary function of PSG1 is to act as an immunomodulator, protecting the growing fetus by modulating the maternal immune response . It has been observed to induce the production of transforming growth factor beta 1 (TGFB1) and vascular endothelial growth factor A (VEGFA), which play crucial roles in placental vascular morphogenesis and the establishment of the maternal-fetal interface .
The recombinant form of PSG1, produced in Sf9 insect cells, is used for various research and diagnostic purposes. The Sf9 cell line, derived from the fall armyworm (Spodoptera frugiperda), is commonly used for the expression of recombinant proteins due to its high efficiency and ability to perform post-translational modifications similar to those in mammalian cells .
PSG1 levels in maternal serum can serve as a biomarker for pregnancy-related conditions. Abnormal levels of PSG1 have been associated with complications such as preeclampsia and intrauterine growth restriction . Additionally, PSG1 has potential therapeutic applications due to its immunomodulatory properties, which could be harnessed to treat autoimmune diseases and other inflammatory conditions .
Ongoing research aims to further elucidate the molecular mechanisms underlying PSG1’s functions and its interactions with other proteins and cells in the maternal-fetal interface. Understanding these mechanisms could lead to the development of novel diagnostic and therapeutic strategies for pregnancy-related complications and other immune-related disorders .