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Recombination of a plasmid that contains the human Prolactin receptor (PRLR) protein (25-234aa) encoding gene and the C-terminal FC-tag gene is the first step during the production of the recombinant human PRLR protein. The constructed plasmid is introduced into mammalian cells. Mammalian cells that can survive in the presence of a specific antibiotic are selected to be cultured for the induction of protein expression. After expression, CUSABIO uses affinity purification to isolate and purify the recombinant human PRLR protein from the cell lysate. Denaturing SDS-PAGE is then applied to resolve the resulting recombinant human PRLR protein. Its purity exceeds 85%.
PRLR is a vital receptor involved in various important bodily processes. It's particularly significant in the development of mammary glands during pregnancy and lactation [1]. PRLR comes in different structures and functions, and its transcripts and proteins differ across various tissues [2]. The expression of PRLR is controlled by several promoters, leading to varied regulation in different tissues [3]. PRLR plays roles in diverse biological functions like lactation, reproduction, metabolism, behavior, immune regulation, growth, and maintaining water-salt balance, all through specific prolactin receptors [3]. Moreover, PRLR's specific function and how much it's expressed depend on the tissue [4].
In breast cancer, both PRL and PRLR are crucial for normal breast development and cancer formation [5]. PRLR has two similar repeated units in its extracellular domain, with the unit nearer to the membrane binding specifically with prolactin [6]. PRLR also helps mammary epithelial cell (MEC) differentiation, including the induction of milk proteins, which depend on STAT5 [7]. Additionally, PRLR has been found to regulate pain responses, specifically in females, through a mechanism that targets nociceptors [8]. It's also a promising target for antibody therapy because it's expressed in many types of breast cancers [9].
Regulating PRLR is complex and involves various modulators such as steroid hormones and protein kinase C [10]. Furthermore, the protein-tyrosine phosphatase SHP-2 influences signaling events through PRLR [11]. Moreover, the protein kinase GSK3β plays a key role in the degradation of PRLR by phosphorylating the serine residue at position 349 [12]. Finally, a fusion protein with dual functions has been shown to increase cell death in PRLR-positive breast cancer cells when co-cultured with natural killer cells [13].
References:
[1] L. Ma, J. Gao, Y. Guan, X. Shi, H. Zhang, M. Ayrapetovet al., Acetylation modulates prolactin receptor dimerization, Proceedings of the National Academy of Sciences, vol. 107, no. 45, p. 19314-19319, 2010. https://doi.org/10.1073/pnas.1010253107
[2] W. Ding and W. Wu, Multiple human prolactin receptors and signaling, African Journal of Biotechnology, vol. 9, no. 7, p. 940-949, 2010. https://doi.org/10.5897/ajb09.069
[3] Z. Hu, Z. Li, & M. Dufau, Multiple and tissue-specific promoter control of gonadal and non-gonadal prolactin receptor gene expression, Journal of Biological Chemistry, vol. 271, no. 17, p. 10242-10246, 1996. https://doi.org/10.1074/jbc.271.17.10242
[4] H. Xue, J. Xu, M. Wu, L. Chen, & L. Xu, Identification and sequence analysis of prolactin receptor and its differential expression profile at various developmental stages in striped hamsters, Brazilian Journal of Medical and Biological Research, vol. 54, no. 5, 2021. https://doi.org/10.1590/1414-431x202010274
[5] D. Sa-nguanraksa, K. Mitpakdi, N. Samarnthai, T. Thumrongtaradol, & P. O-charoenrat, Expression of long-form prolactin receptor is associated with lower disease-free and overall survival in node-negative breast cancer patients, Gland Surgery, vol. 10, no. 1, p. 130-142, 2021. https://doi.org/10.21037/gs-20-569
[6] T. Ohkubo, S. Atomura, H. Adachi, & D. Murase, Prolactin specifically interacts with membrane distal extracellular domain of chicken prolactin receptor, The Journal of Poultry Science, 2011. https://doi.org/10.2141/jpsa.010111
[7] C. Brisken, M. Socolovsky, H. Lodish, & R. Weinberg, The signaling domain of the erythropoietin receptor rescues prolactin receptor-mutant mammary epithelium, Proceedings of the National Academy of Sciences, vol. 99, no. 22, p. 14241-14245, 2002. https://doi.org/10.1073/pnas.222549599
[8] M. Patil, S. Belugin, J. Mecklenburg, A. Wangzhou, C. Paige, P. Barba-Escobedoet al., Prolactin regulates pain responses via a female-selective nociceptor-specific mechanism, Iscience, vol. 20, p. 449-465, 2019. https://doi.org/10.1016/j.isci.2019.09.039
[9] M. Anderson, Q. Zhang, L. Rodriguez, C. Hecquet, C. Donawho, P. Ansellet al., Abbv-176, a prlr antibody drug conjugate with a potent dna-damaging pbd cytotoxin and enhanced activity with parp inhibition, BMC Cancer, vol. 21, no. 1, 2021. https://doi.org/10.1186/s12885-021-08403-5
[10] C. Ormandy, C. Lee, P. Kelly, & R. Sutherland, Regulation of prolactin receptor expression by the tumour promoting phorbol ester 12‐o‐tetradecanoylphorbol‐13‐acetate in human breast cancer cells, Journal of Cellular Biochemistry, vol. 52, no. 1, p. 47-56, 1993. https://doi.org/10.1002/jcb.240520108
[11] S. Ali and S. Ali, Recruitment of the protein-tyrosine phosphatase shp-2 to the c-terminal tyrosine of the prolactin receptor and to the adaptor protein gab2, Journal of Biological Chemistry, vol. 275, no. 50, p. 39073-39080, 2000. https://doi.org/10.1074/jbc.m007478200
[12] F. Haglund, M. Lu, V. Vukojević, I. Nilsson, A. Andreasson, M. Dzabicet al., Prolactin receptor in primary hyperparathyroidism – expression, functionality and clinical correlations, Plos One, vol. 7, no. 5, p. e36448, 2012. https://doi.org/10.1371/journal.pone.0036448
[13] H. Ding, G. Buzzard, S. Huang, M. Sehorn, R. Marcus, & Y. Wei, Mica-g129r: a bifunctional fusion protein increases prlr-positive breast cancer cell death in co-culture with natural killer cells, Plos One, vol. 16, no. 6, p. e0252662, 2021. https://doi.org/10.1371/journal.pone.0252662
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