Nuclear Envelope and Nuclear Pore Marker Antibody (39C7): sc-57946

Nuclear Envelope and Nuclear Pore Marker Antibody (39C7) is a mouse monoclonal IgG1 antibody that detects Nuclear Envelope and Nuclear Pore Marker of mouse, rat, human, and yeast origin by immunofluorescence (IF). Nuclear Envelope and Nuclear Pore Marker (39C7) antibody is available as the non-conjugated form. The nuclear envelope serves as a critical barrier that protects genetic material within the nucleus, while also playing a vital role in chromatin organization and regulation. This double membrane structure maintains nucleus integrity and facilitates proper gene expression. Nuclear pores embedded within the envelope regulate molecule transport between nucleus and cytoplasm, ensuring essential proteins and RNA move freely while preventing harmful substance passage. POM152, NSP1, p110, and p95 proteins are integral to nuclear pore complex functionality, serving as important markers in cellular process studies. These proteins assist in nuclear envelope structural integrity and play significant roles in cellular growth and signaling pathways, highlighting their importance in understanding yeast biology and eukaryotic cell function.

Alexa Fluor^® is a trademark of Molecular Probes Inc., OR., USA

LI-COR^® and Odyssey^® are registered trademarks of LI-COR Biosciences

Nuclear Envelope and Nuclear Pore Marker Antibody (39C7) References:

1. The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint.  |  Iouk, T., et al. 2002. J Cell Biol. 159: 807-19. PMID: 12473689
2. The Ran GTPase cycle is required for yeast nuclear pore complex assembly.  |  Ryan, KJ., et al. 2003. J Cell Biol. 160: 1041-53. PMID: 12654904
3. Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments.  |  Kiseleva, E., et al. 2004. J Struct Biol. 145: 272-88. PMID: 14960378
4. Multiple conformations in the ligand-binding site of the yeast nuclear pore-targeting domain of Nup116p.  |  Robinson, MA., et al. 2005. J Biol Chem. 280: 35723-32. PMID: 16105837
5. Yeast nuclear envelope subdomains with distinct abilities to resist membrane expansion.  |  Campbell, JL., et al. 2006. Mol Biol Cell. 17: 1768-78. PMID: 16467382
6. NSP1: a yeast nuclear envelope protein localized at the nuclear pores exerts its essential function by its carboxy-terminal domain.  |  Nehrbass, U., et al. 1990. Cell. 61: 979-89. PMID: 2112428
7. Yeast nuclear envelope proteins cross react with an antibody against mammalian pore complex proteins.  |  Aris, JP. and Blobel, G. 1989. J Cell Biol. 108: 2059-67. PMID: 2661560
8. In vitro translocation through the yeast nuclear envelope. Signal-dependent transport requires ATP and calcium.  |  Kalinich, JF. and Douglas, MG. 1989. J Biol Chem. 264: 17979-89. PMID: 2681187
9. Identification of pathogenic gene mutations in LMNA and MYBPC3 that alter RNA splicing.  |  Ito, K., et al. 2017. Proc Natl Acad Sci U S A. 114: 7689-7694. PMID: 28679633
10. Epigenetics in LMNA-Related Cardiomyopathy.  |  Wang, Y. and Dobreva, G. 2023. Cells. 12: PMID: 36899919
11. LMNA Cardiomyopathy: Important Considerations for the Heart Failure Clinician.  |  Rosario, KF., et al. 2023. J Card Fail. 29: 1657-1666. PMID: 37659618
12. POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope.  |  Wozniak, RW., et al. 1994. J Cell Biol. 125: 31-42. PMID: 8138573