Placental Lactogen Antibodies

Background

Placental Lactogen is a polypeptide hormone synthesized and secreted by the syncytiotrophoblast cells of the placenta. Structurally, it is highly homologous to growth hormone and prolactin. This hormone, by acting on the maternal metabolic process, promotes glucose antagonism, lipid mobilization and insulin resistance, thereby prioritizing the nutritional supply to the fetus. At the same time, it can also stimulate the development of breast acini, preparing for postpartum lactation. Since its discovery in 1962, placental prolactin has become a research focus due to its crucial role in the pathogenesis of gestational diabetes. Its concentration increases with the increase of gestational weeks. In clinical practice, it is often used as an important serological indicator for monitoring placental function and fetal development status, and is of great value for understanding the physiological changes and pathological mechanisms of pregnancy adaptation.

Structure Function Application Advantage Our Products

Structure of Placental Lactogen

Placental Lactogen is a protein with a molecular weight of approximately 22-25 kDa, and its precise molecular weight varies by species and splicing isomers.

Species	Human	Rhesus monkey	Rat	Mouse
Molecular Weight (kDa)	22.5	22.4	23.1	23.0
Primary Structural Differences	With 191 single amino acid peptide chain	Highly homologous to the human sequence	There are specific amino acid substitutions	Similar but not identical to the rat structure

This protein is composed of 191 amino acids, and its spatial structure is mainly made up of α -helices. The overall three-dimensional conformation is stabilized by two key disulfide bonds within the molecule, one of which is crucial for maintaining its binding ability to the growth hormone receptor. Its active center contains a hydrophilic annular region necessary for interaction with the receptor. The conformational specificity of this region determines its dual biological activities of lactation promotion and metabolic regulation.

Fig. 1:Comparison of amino acid sequences of the PRL/GH/PL family members from human and rat. Fig. 1 Comparison of amino acid sequences of the PRL/GH/PL family members from human and rat.¹

Key structural properties of Placental Lactogen:

Four-helix bundle protein structure
Intramolecular disulfide bonds maintain conformational stability
Receptor binding epitopes determine their dual biological activity

Functions of Placental Lactogen

The main physiological function of placental prolactin is to regulate maternal metabolism and promote fetal development. Its specific functions include:

Function	Description
Maternal metabolic regulation	By inducing insulin resistance, it prompts the mother to make greater use of lipids for energy supply, thereby ensuring the priority delivery of glucose to the fetus.
Fetal growth promotion	Binding with growth hormone receptors, directly stimulate the growth and development of fetal tissue and placenta.
Preparation for breast development	In the middle and late stages of pregnancy, it works in synergy with prolactin to promote the development of breast acini and prepare for postpartum lactation.
Nutrient mobilization	Enhance maternal lipolysis, increase the level of free fatty acids, and provide additional energy sources for both the mother and the fetus.

Placental prolactin mainly activates the JAK-STAT signaling pathway by binding to its receptor, thereby mediating the regulatory effects on growth and metabolism. Its concentration in the maternal serum is positively correlated with the weight of the placenta and the weight of the fetus, and it is an important clinical indicator for evaluating placental function.

Applications of Placental Lactogen and Placental Lactogen Antibody in Literature

1. Boime, I. R. V. I. N. G., et al. "Synthesis of human placental lactogen messenger RNA as a function of gestation." Journal of Biological Chemistry 251.3 (1976): 820-825. https://doi.org/10.1016/S0021-9258(17)33858-9

The article indicates that a comparative study of placentas in the early stage of pregnancy and full-term placentas has found that the amount of human placental prolactin (hPL) synthesized by full-term placentas increases by approximately four times. This is mainly due to the significant increase in hPL mRNA levels in full-term placental tissues, reflecting that as pregnancy progresses, the continuous differentiation of the placenta leads to an enhanced hPL synthesis capacity per unit tissue.

2. Barrera-Saldana, H. A., D. L. Robberson, and G. F. Saunders. "Transcriptional products of the human placental lactogen gene." Journal of Biological Chemistry 257.20 (1982): 12399-12404. https://doi.org/10.1016/S0021-9258(18)33727-X

The article indicates that in full-term placentas, the mRNA content of placental prolactin (hPL) is very abundant, accounting for approximately 5% of poly(A+)RNA. Its mature mRNA is approximately 860 nucleotides in length and there are multiple larger intranuclear RNA precursors. Through cDNA cloning analysis, it was confirmed that the hPL gene contains four small introns, which explains the size differences of its precursor molecules.

3. Duckworth, M. L., K. L. Kirk, and H. G. Friesen. "Isolation and identification of a cDNA clone of rat placental lactogen II." Journal of Biological Chemistry 261.23 (1986): 10871-10878. https://doi.org/10.1016/S0021-9258(18)67468-X

The cDNA of rat placental prolactin type II (rPLII) was successfully cloned. Its mRNA began to be expressed on the 12th day of pregnancy and reached its peak on the 18th day. Sequence analysis revealed that rPLII has a higher homology (52%) with rat prolactin at the amino acid level and a lower similarity (34%) with growth hormone, indicating that its evolutionary path is different from that of human placental prolactin.

4. Bolander Jr, F. F., and R. E. Fellows. "Purification and characterization of bovine placental lactogen." Journal of Biological Chemistry 251.9 (1976): 2703-2708. https://doi.org/10.1016/S0021-9258(17)33544-5

Researchers purified bovine placental prolactin (bPL) from bovine placentas. Its molecular weight is approximately 22,150 and its isoelectric point is 5.9. Structural analysis shows that bPL lies between bovine growth hormone and prolactin in terms of amino acid composition and immune characteristics, indicating that non-primate placental prolactin is in an intermediate position between the two in molecular evolution.

5. Garay, Samantha M., Lorna A. Sumption, and Rosalind M. John. "Prenatal health behaviours as predictors of human placental lactogen levels." Frontiers in Endocrinology 13 (2022): 946539. https://doi.org/10.3389/fendo.2022.946539

Research has found that a healthy diet pattern for pregnant women with a healthy weight can increase placental prolactin (hPL) levels. Higher hPL is significantly associated with an increased risk of neonatal birth weight percentile and large for gestational age infants, revealing the important impact of hPL on fetal growth.

Creative Biolabs: Placental Lactogen Antibodies for Research

Creative Biolabs specializes in the production of high-quality Placental Lactogen antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom Placental Lactogen Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our Placental Lactogen antibodies, custom preparations, or technical support, contact us at email.

Reference

Duckworth, M. L., K. L. Kirk, and H. G. Friesen. "Isolation and identification of a cDNA clone of rat placental lactogen II." Journal of Biological Chemistry 261.23 (1986): 10871-10878. https://doi.org/10.1016/S0021-9258(18)67468-X