Anti-NUP153 monoclonal antibody (DCABH-5549)

Specifications


Host Species
Rabbit
Antibody Isotype
IgG
Clone
FQS8717(3)(C)
Species Reactivity
Human
Immunogen
Synthetic peptide (the amino acid sequence is considered to be commercially sensitive) within Human Nup153 aa 50-150 (Cysteine residue). The exact sequence is proprietary.Database link: P49790
Conjugate
Unconjugated

Applications


Application Notes
WB: 1/1000 - 1/10000; ICC/IF: 1/100 - 1/250; Flow Cyt: 1/10 - 1/100.
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.

Target


Alternative Names
NUP153; nucleoporin 153kDa; nucleoporin 153kD; nuclear pore complex protein Nup153; HNUP153; nucleoporin Nup153
Entrez Gene ID
UniProt ID

Product Background


Gene summary
NUP153 (Nucleoporin 153kDa) is a Protein Coding gene. Diseases associated with NUP153 include hiv-1. Among its related pathways are Gene Expression and Metabolism. GO annotations related to this gene include identical protein binding and nucleocytoplasmic transporter activity. 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.
Antigen Description
Possible DNA-binding subunit of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. 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. Nucleoporin 153 (Nup153) is a protein which in humans is encoded by the NUP153 gene. It is an essential component of the basket of nuclear pore complexes (NPCs) in vertebrates, and required for the achoring of NPCs. It also acts as the docking site of an importing karyopherin. On the cytoplasmic side of the NPC, Nup358 fulfills an analogous role. 0The function about NUP153 antigen include DNA binding; Ran GTPase binding; metal ion binding; protein binding; transporter activity; zinc ion binding.
Pathway
Antiviral mechanism by IFN-stimulated genes, organism-specific biosystem; Cytokine Signaling in Immune system, organism-specific biosystem; Disease, organism-specific biosystem; Export of Viral Ribonucleoproteins from Nucleus, organism-specific biosystem; Gene Expression, organism-specific biosystem; Glucose transport, organism-specific biosystem; HIV Infection, organism-specific biosystem.

Citations


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We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More

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References


Chatel, G; Desai, SH; et al. Domain topology of nucleoporin Nup98 within the nuclear pore complex. JOURNAL OF STRUCTURAL BIOLOGY 177:81-89(2012).
Buendia, B; Santa-Maria, A; et al. Caspase-dependent proteolysis of integral and peripheral proteins of nuclear membranes and nuclear pore complex proteins during apoptosis. JOURNAL OF CELL SCIENCE 112:1743-1753(1999).

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