Imp3 Antibody (AT32E9): sc-517409

Imp3 Antibody (AT32E9) is a mouse monoclonal IgG1 kappa light chain antibody that detects the Imp3 protein of human origin by western blotting (WB), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Imp3 (AT32E9) antibody is available as a non-conjugated anti-Imp3 monoclonal isotype antibody. Imp3, also known as BRMS2, C15orf12, or MRPS4, is a 184 amino acid protein characterized by the presence of one S4 RNA-binding domain, serving as the mammalian homolog of the yeast Imp3 protein. Imp3 is primarily localized in the nucleus, where Imp3 plays a crucial role in forming a heterotrimeric complex with MPP10 and Imp4, essential for early cleavage events during pre-18S ribosomal RNA processing. Proper functioning of Imp3 is vital for ribosome biogenesis, a process fundamental for protein synthesis in all living cells. Disruptions in ribosomal processing can lead to various cellular dysfunctions and are implicated in several diseases, including cancer and genetic disorders. The gene encoding Imp3 is located on human chromosome 15, a region harboring over 700 genes and accounting for nearly 3% of the human genome, with mutations in this chromosome being linked to conditions such as Angelman syndrome, Prader-Willi syndrome, Tay-Sachs disease, and Marfan syndrome.

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Imp3 Antibody (AT32E9) References:

1. Imp3p and Imp4p, two specific components of the U3 small nucleolar ribonucleoprotein that are essential for pre-18S rRNA processing.  |  Lee, SJ. and Baserga, SJ. 1999. Mol Cell Biol. 19: 5441-52. PMID: 10409734
2. The human Imp3 and Imp4 proteins form a ternary complex with hMpp10, which only interacts with the U3 snoRNA in 60-80S ribonucleoprotein complexes.  |  Granneman, S., et al. 2003. Nucleic Acids Res. 31: 1877-87. PMID: 12655004
3. Functional characterization of Pwp2, a WD family protein essential for the assembly of the 90 S pre-ribosomal particle.  |  Dosil, M. and Bustelo, XR. 2004. J Biol Chem. 279: 37385-97. PMID: 15231838
4. Effective gene therapy in an authentic model of Tay-Sachs-related diseases.  |  Cachón-González, MB., et al. 2006. Proc Natl Acad Sci U S A. 103: 10373-10378. PMID: 16801539
5. [The Prader-Willi syndrome].  |  Diene, G., et al. 2007. Ann Endocrinol (Paris). 68: 129-37. PMID: 17499572
6. Detailed analysis of 15q11-q14 sequence corrects errors and gaps in the public access sequence to fully reveal large segmental duplications at breakpoints for Prader-Willi, Angelman, and inv dup(15) syndromes.  |  Makoff, AJ. and Flomen, RH. 2007. Genome Biol. 8: R114. PMID: 17573966
7. Functional separation of pre-rRNA processing steps revealed by truncation of the U3 small nucleolar ribonucleoprotein component, Mpp10.  |  Lee, SJ. and Baserga, SJ. 1997. Proc Natl Acad Sci U S A. 94: 13536-41. PMID: 9391061
8. Mpp10p, a new protein component of the U3 snoRNP required for processing of 18S rRNA precursors.  |  Baserga, SJ., et al. 1997. Nucleic Acids Symp Ser. 64-7. PMID: 9478208