Recombinant human GST-Nucleophosmin-ALK fusion protein (Active)
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Recombinant human GST-Nucleophosmin-ALK fusion protein (Active) is a Human protein, expressed in Baculovirus infected Sf9 cells, with >70%, suitable for SDS-PAGE, FuncS.
View Alternative Names
NPM, NPM1, Nucleophosmin, Nucleolar phosphoprotein B23, Nucleolar protein NO38, Numatrin
- FuncS
Supplier Data
Functional Studies - Recombinant human GST-Nucleophosmin-ALK fusion protein (Active) (AB268820)
The specific activity of ab268820 was determined to be 32 nmol/min/mg in a kinase assay using IGF1Rtide synthetic peptide substrate.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human GST-Nucleophosmin-ALK fusion protein (Active) (AB268820)
SDS-PAGE analysis of ab268820.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The ALK-Nucleophosmin fusion protein disrupts normal cellular signaling processes. It acts by activating downstream signaling pathways that promote cellular proliferation and survival. NPM1 besides its role in ribosome biogenesis aids in the transport of proteins and ribonucleic acids. When fused with ALK the NPM1 segment facilitates the relocation of the ALK portion leading to aberrant activation of signaling cascades. The fusion protein forms part of oligomeric complexes that overshadow the regular cell regulatory mechanisms.
Pathways
ALK-Nucleophosmin fusion protein plays a significant role in the PI3K/AKT and RAS/MAPK pathways. The fusion's constitutively active kinase domain causes persistent activation of PI3K/AKT promoting cell growth and anti-apoptotic signals. Also its impact on RAS/MAPK engages proliferative responses. In doing so it interacts with proteins like GRB2 and SOS1 instrumental in mediating these signaling pathways. This integration into critical pathways highlights its pivotal role in pathogenesis.
Specifications
Form
Liquid
Additional notes
Affinity purified.
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
Target data
Additional targets
Product promise
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