Recombinant Human Prolactin R Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Prolactin R Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit Prolactin-induced proliferation of Nb2‑11 rat lymphoma cells. Gout, P.W. et al. (1980) Cancer Res. 40:2433. The ED50 of this effect is 0.04-0.24 µg/mL in the presence of 0.5 ng/mL of recombinant human Prolactin.
Source
Mouse myeloma cell line, NS0-derived human Prolactin R protein
Human Prolactin R
(Gln25-Asp234)
Accession # P16471
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
No results obtained: Gln25 predicted
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
PRLR
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
51 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
66 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Prolactin R Fc Chimera Protein, CF

  • delta 4-delta 7/11 truncated prolactin receptor
  • delta 4-SF1b truncated prolactin receptor
  • hPRL receptor
  • hPRLrI
  • PRLR
  • PRL-R
  • Prolactin R
  • prolactin receptor delta 7/11
  • prolactin receptor
  • ProlactinR
  • secreted prolactin binding protein

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 (1, 2). 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 (2).

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) (2). PRL receptors are found in mammary tissue, pituitary gland, brain, heart, lung thymus, spleen, liver, pancreas, kidney, adrenal gland, uterus, skeletal muscle, and skin (3). A soluble form of PRL-R containing the 206 NH2-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 (2).

  1. Kelly, P.A. et al. (2001) Biochem. Society Transaction 29:48.
  2. Freeman, M.E. et al. (2000) Physiol. Rev. 80:1532.
  3. Nagano, M. and P.A. Kelly (1994) J. Biol. Chem. 269:13337.

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Bioinformatics

Gene Symbol PRLR
Entrez
Uniprot