Recombinant Human Prolactin Protein, CF Summary
Product Specifications
Leu29-Cys227, with an N-terminal Met
Analysis
Product Datasheets
682-PL
Carrier Free
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.
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.
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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).
- Cooke, N.E. et al. (1981) J. Biol. Chem. 256:4007.
- Grattan, D.R. and I.C. Kokay (2008) J. Neuroendocrinol. 20:752.
- Ben-Jonathan, N. et al. (2008) Endocr. Rev. 29:1.
- Bernichtein, S. et al. (2010) J. Endocrinol. 206:1.
- Goffin, V. et al. (2011) Nat. Rev. Urology 8:597.
- Price, A.E. et al. (1995) Endoc. 136:4827.
- Hoffmann, T. et al. (1993) J. Endoc. Invest. 16:807.
- Cole, E. et al. (1991) Endoc. 129:2639.
- 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.
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.
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Citations: Showing 1 - 7
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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 -
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 -
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 -
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 -
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 -
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 -
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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