Recombinant Rat Prolactin Protein, ＞98%(SDS-PAGE), high purity

Item Number

rp155196

• Product Name: Recombinant Rat Prolactin Protein, ＞98%(SDS-PAGE), high purity
• Synonyms: Decidual prolactin; GHA1; Growth hormone A1; Lactogenic hormone; Luteotropic hormone; Mammotropin; PRL; Prolactin; Prolactin precursor
• Grade: ActiBioPure™, Animal Free, Bioactive, Carrier Free, 高性能
• Specifications & Purity: Animal Free, Carrier Free, Bioactive, ActiBioPure™, High performance, ≥98%(SDS-PAGE)
• Purity: ＞98%(SDS-PAGE)
• Bioactivity: Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using rat Nb2-11 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 10⁶ IU/mg.
• Endotoxin Concentration: < 1 EU/μg
• Expression System: E.coli
• Species: Rat
• Amino Acids: 30-226 aa
• Sequence: LPVCSGGDCQ TPLPELFDRV VMLSHYIHTL YTDMFIEFDK QYVQDREFIA KAINDCPTSS LATPEDKEQA QKVPPEVLLN LILSLVHSWN DPLFQLITGL GGIHEAPDAI ISRAKEIEEQ NKRLLEGIEK IISQAYPEAK GNEIYLVWSQ LPSLQGVDEE SKDLAFYNNI RCLRRDSHKV DNYLKFLRCQ IVHKNNC
• Protein Tag: No tag
• Accession #: P01237
• Predicted molecular weight: 22.6 kDa
• SDS-PAGE: 22.6 kDa

Product Description

Various hormones are secreted from the anterior pituitary during development and growth. Prolactin is a growth factor secreted by the anterior pituitary that is necessary for the proliferation and differentiation of the mammary glands.
Background
The neuroendocrine pituitary hormone Prolactin (PRL), also known as lactotrophin, mamotrophin, luteotropic hormone (LTH), or luteotropin, is a secreted hormone that affects reproduction and homeostasis in vertebrates. The functions of PRL can be placed in six broad categories: 1) reproduction and lactation; 2) growth and development; 3) endocrinology and metabolism; 4) brain and behavior; 5) immunomodulation; and 6) electrolyte balance. PRL is secreted by the anterior pituitary gland, mammary gland, placenta, brain, uterus, decidua, dermal fibroblasts, B cells, T cells, NK cells, and some breast cancer cell lines. Although the major form of PRL is a 23 kDa monomeric protein, splice variants of 14, 16, and 22 kDa have been identified. PRL has also been found to be glycosylated, phosphorylated, dimerized, and polymerized. Glycosylation, phosphorylation, dimerization, or polymerization of PRL result in lower activity.
Cell activation by PRL is mediated by a single chain membrane-bound protein belonging to the class 1 cytokine superfamily. The PRL receptor (PRL R) contains an extracellular, transmembrane, and intracellular domain. Transcriptional regulation of the PRL R gene results in several different species-dependent isoforms of PRL R being produced. Although the cytoplasmic domains of the different isoforms vary in length and composition, their extracellular domains are identical. In rats, three major PRL receptor isoforms have been described, a short (291 amino acid), an intermediate (393 amino acid), and a long (591 amino acid). PRL receptors are found in mammary tissue, pituitary gland, brain, heart, lung thymus, spleen, liver, pancreas, kidney, adrenal gland, uterus, skeletal muscle, and skin. A soluble form of PRL-R containing the 206NH2-terminal amino acids of the extracellular domain is secreted by mammary epithelial cells and is found in milk. Binding of the transmembrane PRL R results in ligand dimerization followed by binding and phosphorylation of Jak2. Jak2 then phosphorylates STAT and the long form of PRL R. C-src, fyn, and the Ras/Raf/MAP kinase pathway have also been found to be activated upon PRL R ligand binding.