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AB285794

Recombinant Human Nucleophosmin protein

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Recombinant Human Nucleophosmin protein is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.

View Alternative Names

NPM, NPM1, Nucleophosmin, Nucleolar phosphoprotein B23, Nucleolar protein NO38, Numatrin

1 Images
SDS-PAGE - Recombinant Human Nucleophosmin protein (AB285794)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Nucleophosmin protein (AB285794)

15% SDS-PAGE of GST-tagged ab285794

Lane 1 : Marker
Lane 2 : 0.1 μg NPM
Lane 3 : 0.2 μg NPM
Lane 4 : 0.5 μg NPM

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

GST tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P06748

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.303% Tris

storage-buffer

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Reactivity data

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

This product is manufactured by BioVision, an Abcam company and was previously called 7258 Nucleophosmin (hNPM), human recombinant. 7258-1000 is the same size as the 1 mg size of ab285794.
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Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"32 kDa","actualMolecularWeight":"59.8 kDa","aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P06748","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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

Nucleophosmin also known as NPM1 or B23 is a multifunctional nucleolar phosphoprotein with a molecular weight of approximately 37 kDa. It is highly expressed in the nucleolus of many human cells and is involved in various cellular processes. NPM1 aids ribosome biogenesis intracellular transport of ribosomal components and regulation of the centrosome. Its nucleocytoplasmic shuttling ability is due to its N-terminal domain which plays an important role in binding to nucleic acids and other proteins. Apart from these functions NPM1 acts as a histone chaperone and is important for maintaining genomic integrity.
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.

NPM1 mutations are commonly observed in acute myeloid leukemia (AML) where they affect the normal function of the protein leading to leukemogenesis. NPM1 is also linked to tumorigenesis through its impact on the p53 tumor suppressor pathway. Specifically alterations in NPM1 can disrupt the balance of other related proteins like ALK and p53 influencing the onset and progression of leukemia. Understanding the roles of NPM1 in these contexts is essential for developing targeted therapies to treat AML and other related disorders effectively.
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Specifications

Form

Liquid

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General info

Function

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).

Sequence similarities

Belongs to the nucleoplasmin family.

Post-translational modifications

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).

Subcellular localisation

Nucleus

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Product protocols

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Target data

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).
See full target information NPM1
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