Recombinant Human Prolactin Protein, CF

Catalog # Availability Size / Price Qty
682-PL-050
R&D Systems Recombinant Proteins and Enzymes
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Citations (7)
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Recombinant Human Prolactin Protein, CF Summary

Product Specifications

Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
Measured in a cell proliferation assay using Nb2‑11 rat lymphoma cells. Gout, P.W. et al. (1980) Cancer Res. 40:2433. The ED50 for this effect is 0.03‑0.1 ng/mL.
Source
E. coli-derived human Prolactin protein
Leu29-Cys227, with an N-terminal Met
Accession #
N-terminal Sequence
Analysis
Met
Predicted Molecular Mass
24 kDa

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682-PL

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

682-PL

Formulation Lyophilized from a 0.2 μm filtered solution in Phosphate and NaCl.
Reconstitution Reconstitute at 100 μg/mL in sterile 4 mM HCl containing 1 mg/mL bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Background: Prolactin

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 (1-6). Prolactin is predominantly found as 199 amino acid, 25 kDa glycosylated and 23 kDa non-glycosylated monomers (6). Human prolactin shares only 60% and 63% amino acid sequence identity with mouse and rat prolactin, respectively, although rat prolactin can activate the human prolactin receptor (3). Post-translational modifications such as polymerization, complex formation with IgG (in humans), glycosylation, and proteolytic cleavage can alter the activities of prolactin (6-8). Non-glycosylated prolactin is produced by the pituitary and packaged in storage granules before secretion, while glycosylated prolactin is reported to be constitutively secreted, have lower biological potency, and be removed from the circulation more quickly (3, 6, 7). Cleavage by matrix metalloproteinases or Cathepsin D can produce N-terminal 16 kDa antiangiogenic fragments also called vasoinhibins (9, 10). Thrombin can produce C-terminal 16 kDa fragments that are not antiangiogenic (3). Prolactin is synthesized mainly by the anterior pituitary in all mammals, where secretion is under tonic inhibition by hypothalamic dopamine (2, 3). In humans, prolactin is also produced peripherally (2-5). Prolactin expression is low during early human pregnancy, but increases in late pregnancy (2, 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 (2-5). Each prolactin molecule is thought to bind two receptor molecules (11). In addition to its lactogenic activity, peripherally produced prolactin plays roles in breast and prostate cancer development, regulation of reproductive function, and immunoregulation (5, 6).

References
  1. Cooke, N.E. et al. (1981) J. Biol. Chem. 256:4007.
  2. Grattan, D.R. and I.C. Kokay (2008) J. Neuroendocrinol. 20:752.
  3. Ben-Jonathan, N. et al. (2008) Endocr. Rev. 29:1.
  4. Bernichtein, S. et al. (2010) J. Endocrinol. 206:1.
  5. Goffin, V. et al. (2011) Nat. Rev. Urology 8:597.
  6. Price, A.E. et al. (1995) Endoc. 136:4827.
  7. Hoffmann, T. et al. (1993) J. Endoc. Invest. 16:807.
  8. Cole, E. et al. (1991) Endoc. 129:2639.
  9. Piwnica, D. et al. (2006) Mol. Endocrinol. 20:3263.
  10. Macotela, Y. et al. (2006) J. Cell Sci. 119:1790.
  11. Broutin, I. et al. (2010) J. Biol. Chem. 285:8422.
Entrez Gene IDs
5617 (Human); 19109 (Mouse)
Alternate Names
PRL; Prolactin

Citations for Recombinant Human Prolactin Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

7 Citations: Showing 1 - 7
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  1. Idiosyncratic nature of lactation reveals link to breast cancer risk
    Authors: Germain, D;Chattopadhyay, M;Jenkins, E;Janssen, W;Mashaka, T;
    Research square
    Species: Mouse
    Sample Types: Organoid
    Applications: Bioassay
  2. Compressive stress-mediated p38 activation required for ERalpha?+?phenotype in breast cancer
    Authors: PM Munne, L Martikaine, I Räty, K Bertula, Nonappa, J Ruuska, H Ala-Hongis, A Peura, B Hollmann, L Euro, K Yavuz, L Patrikaine, M Salmela, J Pokki, M Kivento, J Väänänen, T Suomi, L Nevalaita, M Mutka, P Kovanen, M Leidenius, T Meretoja, K Hukkinen, O Monni, J Pouwels, B Sahu, J Mattson, H Joensuu, P Heikkilä, LL Elo, C Metcalfe, MR Junttila, O Ikkala, J Klefström
    Nature Communications, 2021-11-29;12(1):6967.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Effect of prolactin on normal and keratoconus human corneal stromal fibroblasts in vitro
    Authors: P Anders, X Song, B György, N Szentmary, B Seitz, Z Gatzioufas
    PLoS ONE, 2021-04-01;16(4):e0249344.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Knockout of butyrophilin subfamily 1 member A1 (BTN1A1) alters lipid droplet formation and phospholipid composition in bovine mammary epithelial cells
    Authors: L Han, M Zhang, Z Xing, DN Coleman, Y Liang, JJ Loor, G Yang
    J Anim Sci Biotechnol, 2020-07-03;11(0):72.
    Species: Bovine
    Sample Types: Whole Cells
    Applications: Cell Culture
  5. Combination therapy targeting integrins reduces glioblastoma tumor growth through antiangiogenic and direct antitumor activity and leads to activation of the pro-proliferative prolactin pathway.
    Authors: Oliveira-Ferrer L, Wellbrock J, Bartsch U, Penas E, Hauschild J, Klokow M, Bokemeyer C, Fiedler W, Schuch G
    Mol Cancer, 2013-11-20;12(1):144.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Immunoregulation of autocrine prolactin: suppressing the expression of costimulatory molecules and cytokines in T lymphocytes by prolactin receptor knockdown.
    Authors: Xu D, Lin L, Lin X
    Cell. Immunol., 2010-03-02;263(1):71-8.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. Prolactin and heregulin override DNA damage-induced growth arrest and promote phosphatidylinositol-3 kinase-dependent proliferation in breast cancer cells.
    Authors: Chakravarti P, Henry MK, Quelle FW
    Int. J. Oncol., 2005-02-01;26(2):509-14.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay

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