Recombinant Human Prolactin Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Prolactin Protein, CF Summary

• Details of Functionality: 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 #: Q5THQ0
• N-terminal Sequence: Met
• Protein/Peptide Type: Recombinant Proteins
• Gene: PRL
• Purity: >97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 24 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.

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 Phosphate and NaCl.
• Purity: >97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile 4 mM HCl containing 1 mg/mL bovine serum albumin.

Notes

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

Alternate Names for Recombinant Human Prolactin Protein, CF

• 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 (1-6). 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).

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.

Publications for Prolactin (682-PL)(6)

Publications using 682-PL

• 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 Compressive stress-mediated p38 activation required for ERalpha?+?phenotype in breast cancer Nature Communications, 2021-11-29;12(1):6967. 2021-11-29 [PMID: 34845227] (Bioassay, Human)
• P Anders, X Song, B György, N Szentmary, B Seitz, Z Gatzioufas Effect of prolactin on normal and keratoconus human corneal stromal fibroblasts in vitro PLoS ONE, 2021-04-01;16(4):e0249344. 2021-04-01 [PMID: 33793669] (Bioassay, Human)
• L Han, M Zhang, Z Xing, DN Coleman, Y Liang, JJ Loor, G Yang Knockout of butyrophilin subfamily 1 member A1 (BTN1A1) alters lipid droplet formation and phospholipid composition in bovine mammary epithelial cells J Anim Sci Biotechnol, 2020-07-03;11(0):72. 2020-07-03 [PMID: 32637097] (Cell Culture, Bovine)
• Oliveira-Ferrer L, Wellbrock J, Bartsch U, Penas E, Hauschild J, Klokow M, Bokemeyer C, Fiedler W, Schuch G Combination therapy targeting integrins reduces glioblastoma tumor growth through antiangiogenic and direct antitumor activity and leads to activation of the pro-proliferative prolactin pathway. Mol Cancer, 2013-11-20;12(1):144. 2013-11-20 [PMID: 24257371] (Bioassay, Human)
• Xu D, Lin L, Lin X Immunoregulation of autocrine prolactin: suppressing the expression of costimulatory molecules and cytokines in T lymphocytes by prolactin receptor knockdown. Cell. Immunol., 2010-03-02;263(1):71-8. 2010-03-02 [PMID: 20307875] (Bioassay, Human)
• Chakravarti P, Henry MK, Quelle FW Prolactin and heregulin override DNA damage-induced growth arrest and promote phosphatidylinositol-3 kinase-dependent proliferation in breast cancer cells. Int. J. Oncol., 2005-02-01;26(2):509-14. 2005-02-01 [PMID: 15645137] (Bioassay, Human)

Bioinformatics

• Gene Symbol: PRL
• Uniprot:
  • Q5THQ0()