Recombinant Human Nucleophosmin protein (His tag)
Recombinant Human Nucleophosmin protein (His tag)
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Recombinant Human Nucleophosmin protein (His tag) is a Human Full Length protein, in the 1 to 294 aa range, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE.
別名を表示する
NPM, NPM1, Nucleophosmin, Nucleolar phosphoprotein B23, Nucleolar protein NO38, Numatrin
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Nucleophosmin protein (His tag) (AB268818)
SDS-PAGE analysis of ab268818.
Reactivity data
配列情報
出荷温度及び保存条件
出荷温度
短期保存温度
長期保存温度
分注に関する情報
保管に関する情報
補足情報
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
One of the central roles of NPM1 is its involvement in the regulation of cell growth and proliferation. NPM1 forms a complex with other nucleolar proteins affecting ribosome subunit assembly and transport. This protein also participates in the control of the ARF/p53 pathway by sequestering p53-regulating proteins which are essential for cell cycle control and apoptosis. Its interactions with proteins such as nucleolin and nucleophosmin-like proteins allow NPM1 to perform its functions in organizing the nucleolus and regulating responses to stress signals.
Pathways
The NPM1 protein is integrally involved in key cellular pathways like the regulation of the cell cycle and apoptosis. It directly interacts with pathways such as the ribosome biogenesis pathway and the p53 pathway. NPM1 has connections with proteins like ARF and MDM2 which play roles in retinoblastoma protein (pRb) regulation and in the control of tumor-suppressor activities. These pathways under NPM1’s influence are critical for maintaining cellular homeostasis and ensuring proper cell cycle checkpoints.
製品の性状
製品の状態
Liquid
一般的な情報
機能
Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication : phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade (PubMed : 22528486). In complex with MYC enhances the transcription of MYC target genes (PubMed : 25956029). May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1 (By similarity).
配列の類似性
Belongs to the nucleoplasmin family.
翻訳後修飾
Acetylated at C-terminal lysine residues, thereby increasing affinity to histones.. ADP-ribosylated.. Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at Ser-4 by PLK2 in S phase is required for centriole duplication and is sufficient to trigger centriole replication. Phosphorylation at Ser-4 by PLK1 takes place during mitosis. Phosphorylated by CDK2 at Ser-125 and Thr-199. Phosphorylation at Thr-199 may trigger initiation of centrosome duplication. Phosphorylated by CDK1 at Thr-199, Thr-219, Thr-234 and Thr-237 during cell mitosis. When these four sites are phosphorated, RNA-binding activity seem to be abolished. May be phosphorylated at Ser-70 by NEK2. The Thr-199 phosphorylated form has higher affinity for ROCK2. CDK6 triggers Thr-199 phosphorylation when complexed to Kaposi's sarcoma herpesvirus (KSHV) V-cyclin, leading to viral reactivation by reducing viral LANA levels.. Sumoylated by ARF.. Ubiquitinated. Ubiquitination leads to proteasomal degradation. Deubiquitinated by USP36 (PubMed:19208757).
細胞内局在性
Nucleus
ターゲットの情報
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