Pma1p Antibody (40B7): sc-57978
- Pma1p Antibody (40B7) is a mouse monoclonal IgM Pma1p antibody, cited in 4 publications, provided at 250 µl supernatant
- raised against a nuclear preparation of S. cerevisiae origin
- recommended for detection of Pma1p of y origin by WB and IF
- At present, we have not yet completed the identification of the preferred secondary detection reagent(s) for Pma1p Antibody (40B7). This work is in progress.
Pma1p Antibody (40B7) is a mouse monoclonal IgM antibody that detects Pma1p of Saccharomyces cerevisiae origin by western blotting (WB) and immunofluorescence (IF). Anti-Pma1p antibody (40B7) is available as the non-conjugated format. Pma1p serves as the major plasma membrane proton ATPase in yeast, playing a pivotal role in maintaining cellular pH and membrane potential, which is essential for various physiological processes, including nutrient uptake and waste removal. Pma1p is predominantly located in the plasma membrane, where Pma1p is involved in the transport of protons across the membrane, thereby contributing to the establishment of an electrochemical gradient crucial for ATP synthesis and cellular metabolism. Proper localization of Pma1p is vital, as any disruption can lead to impaired cellular function and stress responses. Additionally, Pma1p undergoes post-translational modifications, such as phosphorylation, which can influence activity and stability, further underscoring importance in cellular homeostasis. Oligomerization of Pma1p facilitates partition into lipid rafts—membrane microdomains rich in saturated fatty acids and sterols—enhancing transport to the cell surface. The Sec24p homolog Lst1p plays a critical role in the export of Pma1p by directly conveying Pma1p into a COPII vesicle, ensuring proper localization and function within the cell.
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Pma1p Antibody (40B7) References:
- Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast. | Bagnat, M., et al. 2000. Proc Natl Acad Sci U S A. 97: 3254-9. PMID: 10716729
- Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. | Shimoni, Y., et al. 2000. J Cell Biol. 151: 973-84. PMID: 11086000
- Plasma membrane proton ATPase Pma1p requires raft association for surface delivery in yeast. | Bagnat, M., et al. 2001. Mol Biol Cell. 12: 4129-38. PMID: 11739806
- Ceramide biosynthesis is required for the formation of the oligomeric H+-ATPase Pma1p in the yeast endoplasmic reticulum. | Lee, MC., et al. 2002. J Biol Chem. 277: 22395-401. PMID: 11950838
- Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of living S. cerevisiae cells. | Malinska, K., et al. 2004. J Cell Sci. 117: 6031-41. PMID: 15536122
- Synthesis of sphingolipids with very long chain fatty acids but not ergosterol is required for routing of newly synthesized plasma membrane ATPase to the cell surface of yeast. | Gaigg, B., et al. 2005. J Biol Chem. 280: 22515-22. PMID: 15817474
- Mechanism of polyamine tolerance in yeast: novel regulators and insights. | Porat, Z., et al. 2005. Cell Mol Life Sci. 62: 3106-16. PMID: 16374585
- Proteomic analysis of detergent-resistant membranes from Candida albicans. | Insenser, M., et al. 2006. Proteomics. 6 Suppl 1: S74-81. PMID: 16534748
- Very long-chain fatty acid-containing lipids rather than sphingolipids per se are required for raft association and stable surface transport of newly synthesized plasma membrane ATPase in yeast. | Gaigg, B., et al. 2006. J Biol Chem. 281: 34135-45. PMID: 16980694
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
Pma1p Antibody (40B7) | sc-57978 | 250 µl supernatant | $322.00 |