Rabbit Anti-Human NUP88 Polyclonal antibody

Name: Rabbit Anti-Human NUP88 Polyclonal antibody
SKU: DPABH-21444
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Rabbit Anti-Human NUP88 Polyclonal antibody for WB, ELISA

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COA

SDS

Datasheet

Key features and details

Target: Human NUP88
Host: Rabbit
Application: WB, ELISA
Species Reactivity: Human, Mouse

Summary

Specifications

Antibody Isotype

IgG

Species Reactivity

Human; Mouse

Immunogen

Peptide

Conjugate

Unconjugated

Applications

Application Notes

WB: 1:1000-1:8000

General Notes

This product (Catalog No. DPABH-21444) is a rabbit-derived polyclonal antibody raised against human NUP88. This antibody exhibits cross-reactivity with Human NUP88 from mouse. It has been affinity purified by Protein A. Nucleoporin 88 (Nup88), also known as nuclear pore complex protein Nup88, is a protein encoded by the human NUP88 gene located on chromosome 17p13.2 that serves as a key structural component of the nuclear pore complex (NPC), a large multiprotein assembly embedded in the nuclear envelope that regulates the bidirectional transport of macromolecules between the nucleus and cytoplasm. As a non-fibrous glycoprotein (non-FG nucleoporin) localized exclusively to the cytoplasmic face of the NPC, Nup88 forms stable subcomplexes with other nucleoporins such as Nup214 (also called CAN) and Nup358, contributing to the assembly and anchoring of cytoplasmic filaments while lacking phenylalanine-glycine (FG) repeat domains typical of many nucleoporins. Its primary function involves facilitating nuclear export pathways, particularly those mediated by the exportin CRM1 (exportin-1), including the transport of 60S ribosomal subunits and select nuclear export signal (NES)-bearing proteins like NFAT, though its role can vary by cell type and context, such as attenuating NF-κB export in certain models. Structurally, Nup88 features an N-terminal β-propeller domain for protein interactions and a C-terminal coiled-coil domain that mediates binding to partners like Nup214, enabling its recruitment to the NPC; the protein exists in multiple isoforms, with the canonical 741-amino-acid form having a molecular mass of approximately 88 kDa.
DPABH-21444 is suitable for use in Western blot (WB) (1:1,000–1:8,000) application.
DPABH-21444 is supplied as a liquid formulation in PBS with 0.02% sodium azide and 50% glycerol, pH 7.3. For long-term storage, keep at −20 °C. For short-term use, store at 2–8 °C. Avoid repeated freeze–thaw cycles to maintain antibody integrity and performance.

Target

Alternative Names

88 kDa nucleoporin; nucleoporin 88kDa; Nucleoporin Nup88; NUP88

Entrez Gene ID

4927

UniProt ID

Q99567

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Nesprin-1 impact on tumorigenic cell phenotypes

MOLECULAR BIOLOGY REPORTS

Authors: Sur-Erdem, Ilknur; Hussain, Muhammed Sajid; Asif, Maria; Pinarbasi, Nareg; Aksu, Ali Cenk; Noegel, Angelika A.

Abstract

The largest protein of the nuclear envelope (NE) is Nesprin-1 which forms a network along the NE interacting with actin, Emerin, Lamin, and SUN proteins. Mutations in the SYNE1 gene and reduction in Nesprin-1 protein levels have been reported to correlate with several age related diseases and cancer. In the present study, we tested whether Nesprin-1 overexpression can reverse the malignant phenotype of Huh7 cells, a human liver cancer cell line, which carries a mutation in the SYNE1 gene resulting in reduced Nesprin-1 protein levels, has altered nuclear shape, altered amounts and localization of NE components, centrosome localization and genome stability. Ectopic expression of a mini-Nesprin-1 led to an improvement of the nuclear shape, corrected the mislocalization of NE proteins, the centrosome positioning, and the alterations in the DNA damage response network. Additionally, Nesprin-1 had a profound effect on cellular senescence. These findings suggest that Nesprin-1 may be effective in tumorigenic cell phenotype correction of human liver cancer.

The development of a single molecule fluorescence standard and its application in estimating the stoichiometry of the nuclear pore complex

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Authors: Tie, Hieng Chiong; Madugula, Viswanadh; Lu, Lei

Abstract

We report here an image-based method to quantify the stoichiometry of diffraction-limited sub-cellular protein complexes in vivo under spinning disk confocal microscopy. A GFP single molecule fluorescence standard was first established by immobilizing His-tagged GFP molecules onto the glass surface via nickel nitrilotriacetic acid functionalized polyethylene glycol. When endogenous nucleoporins were knocked down and replaced by the exogenously expressed and knockdown-resistant GFP-nucleoporins, the stoichiometry of the nucleoporin was estimated by the ratio of its fluorescence intensity to that of the GFP single molecules. Our measured stoichiometry of Nup35, Nup93, Nup133 and Nup88 is 23, 18, 14 and 9 and there are possibly16 copies of Nup107-160 complex per nuclear pore complex. (C) 2016 The Authors. Published by Elsevier Inc.