Recombinant Human Nucleophosmin (NPM1)

Recombinant Human Nucleophosmin (NPM1) — Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 a… Purity >90%.

SKU: BCRECP-001258 Category:

Product Specifications

Product SkuBCRECP-001258
Product DescriptionRecombinant Human Nucleophosmin (NPM1) Protein is expressed from E.coli with N-terminal 6xHis-tagged. It contains 1-294aa. [Accession | P06748].
Uniprot No.P06748
Gene NamesNPM1
PurityGreater than 90% as determined by SDS-PAGE.
Expression SystemE.coli
Expression Region1-294aa
SpeciesHomo sapiens (Human)
Tag InfoN-terminal 6xHis-tagged
Molecular weight36.7kDa
ActivityPlease contact us to obtain bioactivity data.
BufferIf the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Research AreasEpigenetics and Nuclear Signaling

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.

Product Specifications

Recombinant Human Nucleophosmin (NPM1) — Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 a… Purity >90%. Suitable for ELISA and Western Blot applications.

SDS-PAGE: Single band at expected molecular weight confirming purity.

ELISA: Suitable as coating antigen or detection standard.

Western Blot: Compatible with standard Western Blot protocols.

Protein Interaction: Validated for SPR (Surface Plasmon Resonance) and BLI (Bio-Layer Interferometry) studies.

Shipping: Shipped at ambient temperature. Lyophilized protein is stable during transit.

Storage: Store lyophilized protein at -20°C to -80°C. Reconstituted protein should be aliquoted and stored at -80°C. Avoid repeated freeze-thaw cycles.

Shelf Life: 12 months from date of receipt when stored as recommended.

Shipping Time: Orders placed before 2 PM EST ship same day. International orders typically deliver within 5-10 business days.

Protein Biology

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)

Subcellular Location

Nucleus, nucleolus; Nucleus, nucleoplasm; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome

Disease Association

[A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated] | [A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA] | [A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1] | [Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location]

Subunit

(Microbial infection) Interacts with HTLV1 Rex protein (via N-terminal nuclear localization signal)

Gene: NPM1  |  Organism: Homo sapiens  |  Synonyms: Nucleolar phosphoprotein B23; Nucleolar protein NO38; Numatrin
Key Publications

Frequently Asked Questions

How do I order or inquire about this product?

Fill out the Online Inquiry form with your required quantity and specifications. You can also email sales@biocrestsci.com. Our team typically responds within 4 business hours with a quote and availability confirmation.

What is the shipping and delivery time?

Orders placed before 2 PM EST ship the same day. Domestic (US) delivery typically takes 2-3 business days. International orders deliver within 5-10 business days. All products are shipped at ambient temperature with appropriate packaging to ensure stability.

How should I store this recombinant protein?

Lyophilized proteins should be stored at -20°C to -80°C upon receipt. After reconstitution, aliquot and store at -80°C. Avoid repeated freeze-thaw cycles. Shelf life is 12 months from date of receipt when stored as recommended.

What quality controls are performed on your products?

Each product undergoes SDS-PAGE purity analysis (typically >85-95%), endotoxin testing, and bioactivity validation. Products are validated for ELISA, Western Blot, and SPR/BLI applications as specified on this product page. A Certificate of Analysis (CoA) is available upon request.

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