JAR Cell Lysate: sc-2276

The JAR Cell Lysate is derived from the JAR cell line, which is a well-established line of human choriocarcinoma cells used extensively in scientific research. Originating in the mid-20th century, this cell line has become a crucial tool in the study of placental biology and cellular behavior. The lysate itself is produced by lysing, or breaking down, the JAR cells, thereby releasing their internal contents, which include proteins, DNA, RNA, and various cellular enzymes. This complex mixture is incredibly valuable for biochemical studies and molecular biology experiments. Researchers utilize the JAR Cell Lysate to analyze protein expression, investigate cellular response mechanisms, and understand gene function. Additionally, its application extends to the study of cell signaling pathways and the examination of cellular responses to various external stimuli. By providing a snapshot of the cellular components and their interactions, JAR Cell Lysate serves as a key resource in elucidating the complex processes of cell communication and regulation, offering insights that are vital for advancing basic scientific knowledge and understanding fundamental biological mechanisms.

JAR Cell Lysate References:

1. Identification of phosphorylation sites in the PKD1-encoded protein C-terminal domain.  |  Li, HP., et al. 1999. Biochem Biophys Res Commun. 259: 356-63. PMID: 10362514
2. Soluble HLA-G: purification from eukaryotic transfected cells and detection by a specific ELISA.  |  Fournel, S., et al. 1999. Am J Reprod Immunol. 42: 22-9. PMID: 10429763
3. Site-directed mutagenesis, proteolytic cleavage, and activation of human proheparanase.  |  Abboud-Jarrous, G., et al. 2005. J Biol Chem. 280: 13568-75. PMID: 15659389
4. Taurine transporter in fetal T lymphocytes and platelets: differential expression and functional activity.  |  Iruloh, CG., et al. 2007. Am J Physiol Cell Physiol. 292: C332-41. PMID: 16956961
5. The role of homeobox protein distal-less 3 and its interaction with ETS2 in regulating bovine interferon-tau gene expression-synergistic transcriptional activation with ETS2.  |  Ezashi, T., et al. 2008. Biol Reprod. 79: 115-24. PMID: 18322277
6. Increased expression of Dsg2 in malignant skin carcinomas: A tissue-microarray based study.  |  Brennan, D. and Mahoney, MG. 2009. Cell Adh Migr. 3: 148-54. PMID: 19458482
7. Cytotoxicity and activation of CB1954 in a human tumour cell line.  |  Sunters, A., et al. 1991. Biochem Pharmacol. 41: 1293-8. PMID: 2018561
8. Effect of a combination oral contraceptive (desogestrel+ethinyl estradiol) on the expression of low-density lipoprotein receptor and its transcription factor (SREBP2) in placental trophoblast cells.  |  Arjuman, A., et al. 2011. Contraception. 84: 160-8. PMID: 21757058
9. Regulation of Mcl-1 by SRSF1 and SRSF5 in cancer cells.  |  Gautrey, HL. and Tyson-Capper, AJ. 2012. PLoS One. 7: e51497. PMID: 23284704
10. Biosynthesis and secretion of laminin and laminin-associated glycoproteins by nonmalignant and malignant human keratinocytes: comparison of cell lines from primary and secondary tumors in the same patient.  |  Frenette, GP., et al. 1988. Cancer Res. 48: 5193-202. PMID: 2457436
11. Conformational intermediates in the production of the combinable form of the beta-subunit of chorionic gonadotropin.  |  Ruddon, RW., et al. 1989. Endocrinology. 124: 862-9. PMID: 2463905
12. Palmitoleate Protects against Zika Virus-Induced Placental Trophoblast Apoptosis.  |  Muthuraj, PG., et al. 2021. Biomedicines. 9: PMID: 34200091
13. The biosynthesis, processing, and secretion of laminin by human choriocarcinoma cells.  |  Peters, BP., et al. 1985. J Biol Chem. 260: 14732-42. PMID: 3840485
14. 17 beta-Hydroxysteroid dehydrogenase: enzymatic activity and mRNA species in choriocarcinoma cells.  |  Barbieri, RL. and Gao, X. 1994. Gynecol Obstet Invest. 37: 210-4. PMID: 8005555
15. A 60 kd MDM2 isoform is produced by caspase cleavage in non-apoptotic tumor cells.  |  Pochampally, R., et al. 1998. Oncogene. 17: 2629-36. PMID: 9840926