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AB159019

Recombinant Human NUP98 protein (GST tag N-Terminus)

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Recombinant Human NUP98 protein (GST tag N-Terminus) is a Human Fragment protein, in the 1 to 110 aa range, expressed in Wheat germ, suitable for ELISA, WB.

View Alternative Names

ADAR2, NUP98, Nuclear pore complex protein Nup98-Nup96

1 Images
SDS-PAGE - Recombinant Human NUP98 protein (GST tag N-Terminus) (AB159019)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human NUP98 protein (GST tag N-Terminus) (AB159019)

ab159019 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB

applications

Biologically active

No

Accession

P52948

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MKLYQTPLELKLKHSTVHVDELCPLIVPNLGVAVIHDYADWVKEASGDLPEAQIVKHWSLTWTLCEALWGHLKELDSQLNEPREYIQILERRRAFSRWLSCTATPQIEEE","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":110,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"P52948","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

The NUP98 protein also known as nucleoporin 98 plays an important role in cellular mechanics. It forms a part of the nuclear pore complex important for regulating nucleocytoplasmic transport. With an approximate mass of 98 kDa NUP98 expresses mainly in the nucleus across various cell types. Alternative splicing of the NUP98 gene can lead to different isoforms. In some research contexts NUP98 is also referred to by related terms such as NUP96. Its expression appears widespread in many tissues replacing or complementing other nucleoporins.
Biological function summary

The NUP98 protein contributes to nuclear-cytoplasmic transport processes as part of the nuclear pore complex. In association with other nucleoporins NUP98 acts in cargo transport between the nucleus and cytoplasm facilitating the movement of RNA and proteins. It also participates in the assembly and disassembly cycles of the nuclear pore complex (NPC). Known interactions include those with components like the 13C2 complex and other mRNA export factors. NUP98's function impacts NPC architecture and its transport efficiency.

Pathways

NUP98 has essential roles beyond mechanical transport. It integrates into the mRNA export pathway collaborating with proteins like CRM1 (exportin-1) to regulate mRNA export. Additionally it plays a role in gene expression regulation by binding to gene promoters involving pathways linked to protein synthesis and cell cycle regulation. Connections with histone modifications suggest its involvement in chromatin remodeling linking it further to the regulation of gene expression pathways.

NUP98 associations are significant. It is implicated in certain hematological malignancies like acute myeloid leukemia (AML) where it forms fusion proteins with partners such as HOXA9 and NSD1. Genetic rearrangements involving NUP98 contribute to oncogenesis altering normal cell function. Other conditions including dysregulation in autoimmune diseases suggest potential links to aberrant signaling pathways. Understanding these disease links involves studying interactions with proteins like MLL another significant player in leukemia pathogenesis.

Specifications

Form

Liquid

General info

Function

Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC (PubMed : 33097660). May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes (PubMed : 28221134). Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body) (PubMed : 28221134).. (Microbial infection) Interacts with HIV-1 capsid protein P24 and nucleocapsid protein P7 and may thereby promote the integration of the virus in the host nucleus (in vitro) (PubMed : 23523133). Binding affinity to HIV-1 CA-NC complexes bearing the capsid change Asn-74-Asp is reduced (in vitro) (PubMed : 23523133).

Sequence similarities

Belongs to the nucleoporin GLFG family.

Post-translational modifications

Isoform 1 to isoform 4 are autoproteolytically cleaved to yield Nup98 and Nup96 or Nup98 only, respectively (PubMed:10087256, PubMed:12191480, PubMed:18287282, PubMed:20407419). Cleaved Nup98 is necessary for the targeting of Nup98 to the nuclear pore and the interaction with Nup96 (PubMed:12191480, PubMed:20407419).. Proteolytically degraded after poliovirus (PV) infection; degradation is partial and NCP- and TPR-binding domains withstand degradation.

Product protocols

Target data

Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC (PubMed : 33097660). May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes (PubMed : 28221134). Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body) (PubMed : 28221134).. (Microbial infection) Interacts with HIV-1 capsid protein P24 and nucleocapsid protein P7 and may thereby promote the integration of the virus in the host nucleus (in vitro) (PubMed : 23523133). Binding affinity to HIV-1 CA-NC complexes bearing the capsid change Asn-74-Asp is reduced (in vitro) (PubMed : 23523133).
See full target information NUP98

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