Prolactin human

Research Area: IMMUNO AND CKS
Prolactin (PRL) is a multifunctional polypeptide hormone primarily produced by the lactotrophic cells of the anterior pituitary gland in vertebrates.

Prolactin is a lactogenic hormone that plays a role in breast cancer, regulation of reproductive function, and immunoregulation. The prolactin cDNA encodes a 227 amino acid residue protein with a putative 28 amino residue signal peptide. Removal of the signal peptide results in the mature hormone corresponding to amino acids 29-227 of natural prolactin. There are several natural occurring molecular forms of prolactin, including a monomer, a non-glycosylated form, and a glycosylated form.

Prolactin is manufactured using an all-human production system, with full chemically defined ingredients and with no serum. It is therefore completely animal- and xeno-component free.

Prolactin human has been used:

• in in vitro experiments to examine its effects in sleep-like concentrations on T-cell migration
• to study its effects on claudin 2 (CLDN2) expression in the Caco-2 intestinal epithelial cell model
• in microplate assays to demonstrate the specificity of the antibodies for vasoinhibin

Prolactin is glycosylated.

Prolactin is recognized in breast milk and can enhance Ca²⁺ absorption through both transcellular and paracellular pathways in the small and large intestine. It is crucial for lactation and reproduction and is demonstrated to have numerous effects on growth, development, metabolism, immunoregulation, and protection. The prolactin signaling pathway begins with the binding of prolactin to the prolactin receptor (PRLR).

Glycosylated human prolactin (G-hPRL) was first isolated and purified from human pituitaries by Lewis et al., with an estimated molecular mass of 25,000 Da and an immunological and biological activity of 25–50% that of non-glycosylated hPRL. The presence of a unique and partially occupied glycosylation site in Asn-31 in human, monkey, ovine, porcine, dromedary, equine and whale PRL makes it an ideal model of glycosylation for N-glycan studies since it exhibits the simplest type of glycosylation macroheterogeneity, with an occupancy range of 10-30% of G-hPRL relative to the total hPRL of either pituitary or recombinant origin. It has been postulated that hPRL glycosylation might possibly modulate the bioactivity of the circulating pool of the hormone, perhaps by selectively down regulating PRL action at individual target tissues.

This product is supplied as a solution in 0.2 μm filtered phosphate buffered saline with no additives or carrier proteins. It is aseptically filled.

Briefly centrifuge the vial before opening. After initial thawing it is recommended to store the protein in working aliquots at -20°C. The product can be diluted in PBS.