Recombinant Human NUP214 protein (GST tag N-Terminus)
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Recombinant Human NUP214 protein (GST tag N-Terminus) is a Human Fragment protein, in the 1 to 97 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
대체 명칭 보기
CAIN, CAN, KIAA0023, NUP214, Nuclear pore complex protein Nup214, 214 kDa nucleoporin, Nucleoporin Nup214, Protein CAN
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human NUP214 protein (GST tag N-Terminus) (AB152837)
12.5% SDS-PAGE analysis of ab152837 stained with Coomassie Blue.
Reactivity 정보
서열 정보
특성 및 보관 정보
제형
Purification 테크닉
배송 시 보관 조건
적절한 단기 보관 조건
적절한 장기 보관 조건
분주 정보
보관 정보
추가 정보
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
NUP214 participates in the assembly and function of the NPC by regulating cargo movement. This protein acts as a docking site for transport receptors aiding in the import and export of macromolecules. NUP214 exhibits a part in the nuclear pore complex interacting dynamically with other nucleoporins like NUP88 and NUP62. Its biological role maintains nuclear and cytoplasmic homeostasis which is important for normal cell function and division influencing gene expression and cellular responses to stimuli.
Pathways
NUP214 plays a significant role in nucleocytoplasmic transport mechanisms and is integrated into the Ran GTPase pathway. This pathway ensures that proteins and RNA efficiently move across the nuclear envelope fulfilling specific cellular functions. NUP214's functional relationships include interactions with importin and exportin proteins which recognize nuclear localization and export signals on cargo molecules. These interactions are vital for the cell cycle and signal transduction pathways highlighting NUP214's involvement in important cellular activities.
일반 정보
기능
Part of the nuclear pore complex (PubMed : 9049309). Has a critical role in nucleocytoplasmic transport (PubMed : 31178128). May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex (PubMed : 31178128, PubMed : 8108440).. (Microbial infection) Required for capsid disassembly of the human adenovirus 5 (HadV-5) leading to release of the viral genome to the nucleus (in vitro).
Post-translational modifications
Probably glycosylated as it reacts with wheat germ agglutinin (WGA).
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Product promise
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