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Rat Anti-NUP153 Recombinant Antibody (R4C8) (CBMAB-N3994-WJ)


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Summary

Host Animal
Rat
Specificity
Human, Mouse, Rat, Monkey
Clone
R4C8
Application
WB, ICC, ELISA

Basic Information

Specificity
Human, Mouse, Rat, Monkey
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
nucleoporin 153
Introduction
Nuclear pore complexes regulate the transport of macromolecules between the nucleus and cytoplasm. They are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. Nucleoporins are glycoproteins found in nuclear pores and contain characteristic pentapeptide XFXFG repeats as well as O-linked N-acetylglucosamine residues oriented towards the cytoplasm. The protein encoded by this gene has three distinct domains: a N-terminal region containing a pore targeting and an RNA-binding domain domain, a central region containing multiple zinc finger motifs, and a C-terminal region containing multiple XFXFG repeats. Alternative splicing results in multiple transcript variants of this gene. [provided by RefSeq, May 2013]
Entrez Gene ID
Human9972
Mouse218210
Rat25281
Monkey703888
UniProt ID
HumanP49790
MouseE9Q3G8
RatP49791
MonkeyF6V9A5
Alternative Names
Nucleoporin 153; 153 KDa Nucleoporin; Nucleoporin 153kDa; Nucleoporin Nup153; Nuclear Pore Complex Protein Hnup153; Nuclear Pore Complex Protein Nup153; Nucleoporin 153kD; HNUP153; N153;
Function
Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC).
(Microbial infection) Interacts with HIV-1 caspid protein P24 and thereby promotes the integration of the virus in the nucleus of non-dividing cells (in vitro).
(Microbial infection) Binds HIV-2 protein vpx and thereby promotes the nuclear translocation of the lentiviral genome (in vitro).
Biological Process
mRNA transportIEA:UniProtKB-KW
Negative regulation of RNA export from nucleusManual Assertion Based On ExperimentIDA:UniProtKB
Nuclear pore complex assemblyManual Assertion Based On ExperimentIMP:UniProtKB
Nucleocytoplasmic transport1 PublicationIC:ComplexPortal
Protein import into nucleusManual Assertion Based On ExperimentIBA:GO_Central
RNA export from nucleusManual Assertion Based On ExperimentIBA:GO_Central
Viral entry into host cellIEA:UniProtKB-KW
Viral penetration into host nucleusIEA:UniProtKB-KW
Cellular Location
Nucleus
Nucleus membrane
Nucleus, nuclear pore complex
Tightly associated with the nuclear membrane and lamina (By similarity).
Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Dissociates from the NPC structure early during prophase of mitosis. Integrated in the newly assembled nuclear envelope of postmitotic cells early in G1. Colocalized with NUP98 and TPR to the nuclear basket at the nucleoplasmic side of the NPC. Detected in diffuse and discrete intranuclear foci. Remained localized to the nuclear membrane after poliovirus (PV) infection.
PTM
Phosphorylated in interphase, hyperphosphorylated during mitosis. May play a role in the reversible disassembly of the nuclear pore complex during mitosis (By similarity).
Proteolytically degraded after poliovirus (PV) infection; degradation is partial and NCP- and TPR-binding domains withstand degradation.
O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.
More Infomation

Schertzer, M., Jullien, L., Pinto, A. L., Calado, R. T., Revy, P., & Londoño-Vallejo, A. (2023). Human RTEL1 Interacts with KPNB1 (Importin β) and NUP153 and Connects Nuclear Import to Nuclear Envelope Stability in S-Phase. Cells, 12(24), 2798.

Shen, Q., Kumari, S., Xu, C., Jang, S., Shi, J., Burdick, R. C., ... & Xiong, Y. (2023). The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores. Proceedings of the National Academy of Sciences, 120(13), e2202815120.

Wang, X., Gao, H. B., Gao, Y. M., Du, S. J., & Wu, C. S. (2023). The expression and clinical significance of miR-133b and NUP153 in colorectalcancer.

Demeneva, V. V., Tolmacheva, E. N., Nikitina, T. V., Sazhenova, E. A., Yuriev, S. Y., Makhmutkhodzhaev, A. S., ... & Vasilyev, S. A. (2023). Expression of the NUP153 and YWHAB genes from their canonical promoters and alternative promoters of the LINE-1 retrotransposon in the placenta of the first trimester of pregnancy. Vavilov Journal of Genetics and Breeding, 27(1), 63.

LaJoie, D., Turkmen, A. M., Mackay, D. R., Jensen, C. C., Aksenova, V., Niwa, M., ... & Ullman, K. S. (2022). A role for Nup153 in nuclear assembly reveals differential requirements for targeting of nuclear envelope constituents. Molecular Biology of the Cell, 33(13), ar117.

Singh, S. P., Raja, S., & Mahalingam, S. (2020). Viral protein X unlocks the nuclear pore complex through a human Nup153-dependent pathway to promote nuclear translocation of the lentiviral genome. Molecular Biology of the Cell, 31(4), 304-317.

Leone, L., Colussi, C., Gironi, K., Longo, V., Fusco, S., Li Puma, D. D., ... & Grassi, C. (2019). Altered Nup153 expression impairs the function of cultured hippocampal neural stem cells isolated from a mouse model of Alzheimer’s disease. Molecular Neurobiology, 56, 5934-5949.

Wu, Y., Fang, G., Wang, X., Wang, H., Chen, W., Li, L., ... & Cai, Y. (2019). NUP153 overexpression suppresses the proliferation of colorectal cancer by negatively regulating Wnt/β-catenin signaling pathway and predicts good prognosis. Cancer Biomarkers, 24(1), 61-70.

Bilir, Ş., Kojidani, T., Mori, C., Osakada, H., Kobayashi, S., Koujin, T., ... & Haraguchi, T. (2019). Roles of Nup133, Nup153 and membrane fenestrations in assembly of the nuclear pore complex at the end of mitosis. Genes to cells, 24(5), 338-353.

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For research use only. Not intended for any clinical use.

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