PRA1 Antibody (2A4): sc-293351

PRA1 Antibody (2A4) is a mouse monoclonal IgG2a kappa light chain antibody that detects PRA1 protein of human origin by western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). Anti-PRA1 antibody (2A4) is available as the non-conjugated format. PRA1, also known as prenylated Rab acceptor protein 1, RABAC1, or YIP3, is a crucial 185 amino acid multi-pass membrane protein that plays a significant role in vesicle formation from the Golgi complex. PRA1 functions in intracellular transport processes by regulating the activity of Rab GTPases, which are essential for the docking and fusion of vesicles with target membranes. This regulation is particularly important for maintaining cellular homeostasis and facilitating communication between organelles. PRA1 exists as a homodimer and is ubiquitously expressed, with high levels found in the pituitary gland, kidney, placenta, stomach, and lung. PRA1 interacts specifically with prenylated Rab proteins, including Rab 4B, Rab 5A, and Rab 5C, as well as other proteins such as VAMP-2, Rab GDI α, and piccolo, while showing weaker interactions with Rab 4A, Rab 6, Rab 7, Rab 17, and Rab 22. The gene encoding PRA1 is located on human chromosome 19q13.2, highlighting its significance in cellular function and potential implications in various diseases.

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PRA1 Antibody (2A4) References:

1. Interaction cloning and characterization of the cDNA encoding the human prenylated rab acceptor (PRA1).  |  Bucci, C., et al. 1999. Biochem Biophys Res Commun. 258: 657-62. PMID: 10329441
2. PRA1 inhibits the extraction of membrane-bound rab GTPase by GDI1.  |  Hutt, DM., et al. 2000. J Biol Chem. 275: 18511-9. PMID: 10751420
3. Prenylated Rab acceptor protein is a receptor for prenylated small GTPases.  |  Figueroa, C., et al. 2001. J Biol Chem. 276: 28219-25. PMID: 11335720
4. Expression analysis and chromosomal assignment of PRA1 and RILP genes.  |  Bucci, C., et al. 2001. Biochem Biophys Res Commun. 286: 815-9. PMID: 11520070
5. Envelope glycoprotein cytoplasmic domains from diverse lentiviruses interact with the prenylated Rab acceptor.  |  Evans, DT., et al. 2002. J Virol. 76: 327-37. PMID: 11739697
6. Pitfalls in the use of transfected overexpression systems to study membrane proteins function: the case of TSH receptor and PRA1.  |  Jacobs, C. and Pirson, I. 2003. Mol Cell Endocrinol. 209: 71-5. PMID: 14604818
7. PRA1 co-localizes with envelope but does not influence primate lentivirus production, infectivity or envelope incorporation.  |  Blancou, P., et al. 2005. J Gen Virol. 86: 1785-1790. PMID: 15914857
8. Genomic organization, expression profile, and characterization of the new protein PRA1 domain family, member 2 (PRAF2).  |  Fo, CS., et al. 2006. Gene. 371: 154-65. PMID: 16481131
9. PRA1 promotes the intracellular trafficking and NF-kappaB signaling of EBV latent membrane protein 1.  |  Liu, HP., et al. 2006. EMBO J. 25: 4120-30. PMID: 16917502
10. Prenylated Rab acceptor 1 (PRA1) inhibits TCF/beta-catenin signaling by binding to beta-catenin.  |  Kim, JT., et al. 2006. Biochem Biophys Res Commun. 349: 200-8. PMID: 16930546
11. Role of pH-regulated antigen 1 of Candida albicans in the fungal recognition and antifungal response of human neutrophils.  |  Losse, J., et al. 2011. Mol Immunol. 48: 2135-43. PMID: 21820180
12. NDRG2 and PRA1 interact and synergistically inhibit T-cell factor/β-catenin signaling.  |  Kim, JT., et al. 2012. FEBS Lett. 586: 3962-8. PMID: 23068607