Measured in a cell proliferation assay using Nb2-11 rat lymphoma cells. Gout, P.W. et al. (1980) Cancer Res. 40:2433. The ED 50 for this effect is 0.25-1 ng/mL.
Source
E. coli-derived mouse Prolactin protein Leu32-Cys228, with an N-terminal Met
>95%, 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
Dilutions
Bioactivity
Theoretical MW
22.6 kDa. 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.
Publications
Read Publications using 1445-PL in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Prolactin Protein
PRL
Prolactin
Background
Prolactin (gene name PRL) is a secreted neuroendocrine pituitary hormone that acts primarily on the mammary gland to promote lactation, but has pleiotropic effects in both males and females (1-3). Mouse Prolactin is predominantly found as 23 kDa non-glycosylated monomers. Mouse prolactin shares 60% and 85% amino acid sequence identity with human and rat prolactin, respectively; however, activation of the human prolactin receptor by rat prolactin has been demonstrated (3). Prolactin is synthesized mainly by the anterior pituitary in all mammals, where secretion is under tonic inhibition by hypothalamic dopamine (2, 3). Secretion can be stimulated by suckling and diurnally by estradiol in rodents during pro-estrus and mating (2). In humans prolactin is also produced peripherally, while in rodents, the only known non-pituitary source is the placenta (1-3). Mouse serum Prolactin declines until mid-pregnancy, but increases in late pregnancy (1). Post-translational modifications such as polymerization, phosphorylation, and proteolytic cleavage can alter the activities of prolactin (3). Cleavage by matrix metalloproteinases or Cathepsin D can produce N-terminal 16 kDa antiangiogenic fragments also called vasoinhibins (4, 5). Thrombin can produce C-terminal 16 kDa fragments that are not antiangiogenic (3). The prolactin receptor (gene name PRLR) is a transmembrane type I glycoprotein that belongs to the cytokine hematopoietic receptor family. Expression of the prolactin receptor is widespread (2, 3). Each prolactin molecule is thought to bind two receptor molecules (6).
Linzer, D.I.H. et al. (1985) J. Biol. Chem. 260:9574.
Grattan, D.R. and I.C. Kokay (2008) J. Neuroendocrinol. 20:752.
Ben-Jonathan, N. et al. (2008) Endocr. Rev. 29:1.
Piwnica, D. et al. (2006) Mol. Endocrinol. 20:3263.
Macotela, Y. et al. (2006) J. Cell Sci. 119:1790.
Broutin, I. et al. (2010) J. Biol. Chem. 285:8422.
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