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AB4641

Anti-NSP1 antibody [32D6]

5

(1 Review)

|

(11 Publications)

Mouse Monoclonal NSP1 antibody. Suitable for WB, ICC/IF and reacts with Saccharomyces cerevisiae samples. Cited in 11 publications.

View Alternative Names

Nsp1p, Nuclear pore protein NSP1, Nucleoporin NSP1, p110

1 Images
Immunocytochemistry/ Immunofluorescence - Anti-NSP1 antibody [32D6] (AB4641)
  • ICC/IF

AbReview20740****

Immunocytochemistry/ Immunofluorescence - Anti-NSP1 antibody [32D6] (AB4641)

ab4641 (1/5000) detecting NSP1 in Saccharomyces cerevisae DDY1810 (green). Cells were fixed in paraformaldehyde, permeabilized in methanol/acetone and counterstained with DAPI in order to highlight the nucleus (blue). For further experimental details please refer to Abreview.

Image courtesy of an anonymous Abreview.

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

32D6

Isotype

IgG

Carrier free

No

Reacts with

Saccharomyces cerevisiae

Applications

WB, ICC/IF

applications

Specificity

This antibody was initially identified as directed against a nuclear pore complex antigen by immunofluorescence localization. A screen of a lgt11 expression library yielded a single positive clone carrying an insert bearing ~66% of the C-terminal portion of NSP1. To confirm that 32D6 possessed high affinity for NSP1, strain RS453, which expresses a shortened isoform of NSP1, was compared to the wildtype strain BJ5465. NSP1 in RS453 contains an internal deletion that removes the coding sequence for 6 FXFG repeats, which are not essential for function and encodes a protein that has been observed to migrate at approxmately 85 kDa on SDS gels. The predicted size of wildtype NSP1 is 86.5 kDa, but NSP1 has been observed to migrate on SDS gels at ~100 kDa. In our gels, the apparent molecular mass of wildtype NSP1 was 108 kDa, whereas the short isoform of NSP1 in RS453 migrated at 91 kDa. The detection of two protein bands of apparent sizes 108 kDa and 91 kDa in BJ5465 and RS453, respectively, demonstrated that 32D6 recognized the pore complex protein NSP1.

Reactivity data

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Product details

This antibody is a useful marker of yeast nuclear pores.

Properties and storage information

Form
Liquid
Purity
Tissue culture supernatant
Purification notes
Sterile filtered.
Storage buffer
Preservative: 0.065% Sodium azide Constituents: Tissue culture supernatant
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The non-structural protein 1 (NSP1) is a protein encoded by the genome of coronaviruses including SARS-CoV-2 the virus responsible for COVID-19. It plays important mechanical roles in viral infection and replication. NSP1 weighing around 20 kDa acts by binding to the host's ribosomes where it inhibits host protein translation. This action shuts down the host's antiviral defense mechanisms aiding viral replication. NSP1 is expressed during coronavirus infections and has a role in disrupting host immune responses making it an important target in studying viral pathogenesis and immune evasion.
Biological function summary

NSP1 contributes to the suppression of host gene expression. It is part of a strategy employed by viruses to combat host immune defenses allowing them to replicate efficiently in host cells. By interfacing with the host's mRNA translation machinery NSP1 can selectively inhibit the production of proteins important for the immune response. This process involves interactions that lead to the degradation of host mRNAs preventing the synthesis of proteins needed to mount an effective defense against the virus.

Pathways

NSP1 is involved in intervening in host cellular pathways that control translation and immune signaling. It interacts with the ribosomal 40S subunit making it an essential element in the antiviral pathways specific to the interferon response. Proteins such as ribosomal proteins and other translation initiation factors are impacted by NSP1's presence which modulates their normal activities to favor viral protein synthesis. Its function in these pathways highlights NSP1's strategic importance in viral evasion tactics.

NSP1 plays a significant role in the pathogenesis of COVID-19 directly impacting how coronavirus diseases manifest and progress. The protein's interference with host cellular processes contributes to the severity of the illness given its role in dampening the immune response. NSP1 is also connected to proteins involved in the innate immune response such as interferon-stimulating genes that are part of the body's primary defense mechanisms. Understanding NSP1's function and interactions offers insights into therapeutic strategies that can mitigate the immune suppression caused by COVID-19 aiming to lessen disease burden and pathogenic outcomes.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Publications (11)

Recent publications for all applications. Explore the full list and refine your search

Biomaterials research 29:0201 PubMed40330275

2025

Impact of Culture Duration on the Properties and Functionality of Yeast-Derived Extracellular Vesicles.

Applications

Unspecified application

Species

Unspecified reactive species

Gyeongchan Jeon,Yang-Hoon Kim,Jiho Min

Molecular biology of the cell 33:ar35 PubMed35293775

2022

A perinuclear α-helix with amphipathic features in Brl1 promotes NPC assembly.

Applications

Unspecified application

Species

Unspecified reactive species

Jlenia Vitale,Azqa Khan,Annett Neuner,Elmar Schiebel

Nucleus (Austin, Tex.) 13:79-93 PubMed35171083

2022

Uip4p modulates nuclear pore complex function in .

Applications

Unspecified application

Species

Unspecified reactive species

Pallavi Deolal,Imlitoshi Jamir,Krishnaveni Mishra

Journal of cell science 133: PubMed32973112

2020

Nucleolar size regulates nuclear envelope shape in .

Applications

Unspecified application

Species

Unspecified reactive species

Gurranna Male,Pallavi Deolal,Naresh Kumar Manda,Shantam Yagnik,Aprotim Mazumder,Krishnaveni Mishra

eLife 9: PubMed32352375

2020

An advanced cell cycle tag toolbox reveals principles underlying temporal control of structure-selective nucleases.

Applications

Unspecified application

Species

Unspecified reactive species

Julia Bittmann,Rokas Grigaitis,Lorenzo Galanti,Silas Amarell,Florian Wilfling,Joao Matos,Boris Pfander

The Journal of cell biology 217:877-894 PubMed29439116

2018

Brr6 and Brl1 locate to nuclear pore complex assembly sites to promote their biogenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Wanlu Zhang,Annett Neuner,Diana Rüthnick,Timo Sachsenheimer,Christian Lüchtenborg,Britta Brügger,Elmar Schiebel

The Journal of cell biology 216:2425-2442 PubMed28659328

2017

Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes.

Applications

Unspecified application

Species

Unspecified reactive species

Diana Rüthnick,Annett Neuner,Franziska Dietrich,Daniel Kirrmaier,Ulrike Engel,Michael Knop,Elmar Schiebel

The Journal of cell biology 203:215-32 PubMed24165936

2013

The transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1.

Applications

ICC/IF, WB

Species

Unspecified reactive species, Unspecified reactive species

Paolo Colombi,Brant M Webster,Florian Fröhlich,C Patrick Lusk

PLoS genetics 9:e1003871 PubMed24146631

2013

Yeast Tdh3 (glyceraldehyde 3-phosphate dehydrogenase) is a Sir2-interacting factor that regulates transcriptional silencing and rDNA recombination.

Applications

ICC/IF

Species

Saccharomyces cerevisiae S288C

Alison E Ringel,Rebecca Ryznar,Hannah Picariello,Kuan-lin Huang,Asmitha G Lazarus,Scott G Holmes

Aging 5:551-74 PubMed23924582

2013

Mitochondrial membrane lipidome defines yeast longevity.

Applications

Unspecified application

Species

Unspecified reactive species

Adam Beach,Vincent R Richard,Anna Leonov,Michelle T Burstein,Simon D Bourque,Olivia Koupaki,Mylène Juneau,Rachel Feldman,Tatiana Iouk,Vladimir I Titorenko
View all publications

Product promise

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