Recombinant Human Nucleolin (NCL) Protein (His)

Beta LifeScience SKU/CAT #: BLC-03362P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) NCL.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) NCL.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) NCL.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) NCL.

Recombinant Human Nucleolin (NCL) Protein (His)

Beta LifeScience SKU/CAT #: BLC-03362P
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Product Overview

Description Recombinant Human Nucleolin (NCL) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P19338
Target Symbol NCL
Synonyms C23; FLJ45706; MS1116 ; NCL; Nucl; NUCL_HUMAN; Nucleolin; Protein C23
Species Homo sapiens (Human)
Expression System Yeast
Tag N-6His
Target Protein Sequence VKLAKAGKNQGDPKKMAPPPKEVEEDSEDEEMSEDEEDDSSGEEVVIPQKKGKKAAATSAKKVVVSPTKKVAVATPAKKAAVTPGKKAAATPAKKTVTPAKAVTTPGKKGATPGKALVATPGKKGAAIPAKGAKNGKNAKKEDSDEEEDDDSEEDEEDDEDEDEDEDEIEPAAMKAAAAAPASEDEDDEDDEDDEDDDDDEEDDSEEEAMETTPAKGKKAAKVVPVKAKNVAEDEDEEEDDEDEDDDDDEDDEDDDDEDDEEEEEEEEEEPVKEAPGKRKKEMAKQKAAPEAKKQKVEGTEPTTAFNLFVGNLNFNKSAPELKTGISDVFAKNDLAVVDVRIGMTRKFGYVDFESAEDLEKALELTGLKVFGNEIKLEKPKGKDSKKERDARTLLAKNLPYKVTQDELKEVFEDAAEIRLVSKDGKSKGIAYIEFKTEADAEKTFEEKQGTEIDGRSISLYYTGEKGQNQDYRGGKNSTWS
Expression Range 2-482aa
Protein Length Partial
Mol. Weight 54.4kDa
Research Area Epigenetics And Nuclear Signaling
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats.
Subcellular Location Nucleus, nucleolus. Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Database References

Gene Functions References

  1. Data show that NCL phosphorylation offers specificity to its protein-protein, protein-RNA interactions, resulting in the PARN deadenylase regulation, and hence gene expression, during cellular stress responses. PMID: 29168431
  2. Depletion of endogenous NCL in cells by siRNA targeting during H5N1 infection resulted in significantly increased viral polymerase activity. PMID: 29974255
  3. nucleolin interacts with the viral nucleoprotein PMID: 27373907
  4. This review focus on the contribution of nucleolin for cancer disease and on the development of therapeutic strategies targeting this protein. [review] PMID: 29650282
  5. Results found that prostate circulating tumor cells (CTCs) as a population have an increased level of total nucleolin expression compared to white blood cells. Additionally, there was a distinct nucleolin staining pattern and localization in CTCs. PMID: 28153390
  6. this results show that nucleolin increases colony formation and anchorage-independent growth of ErbB2-overexpressing cells, and that nucleolin overexpression in ErbB2-positive breast cancer patients is associated with reduced patient survival rates and increased disease-risk PMID: 27542246
  7. C23 has a role in promoting tumorigenesis via suppressing p53 activity PMID: 27506938
  8. NCL was associated with bipolar disorder. PMID: 28195573
  9. Nucleolin both forms an mRNP complex with the eIF4G and CSF-1 mRNA, and is co-localized with the eIF4G in the cytoplasm further supporting nucleolin's role in translational regulation. PMID: 28131007
  10. Identified the regulator of ribosome production nucleolin (NCL) as over-expressed in AML blasts. Moreover, we found in two series that high NCL mRNA expression level was associated with a poor overall survival, particular in elderly patients. PMID: 28103300
  11. Data suggest a 216-nucleotide proximal cis-element in LIF mRNA exhibits mRNA destabilizing potential; on exposure to carcinogen PMA (phorbol-12-myristate-13-acetate), this cis-element exhibits mRNA stabilizing activity. PMA induces nucleo-cytoplasmic translocation of both nucleolin and PCBP1, 2 trans-acting factors that bind to and stabilize LIF mRNA. [LIF = leukemia inhibitory factor; PCBP1 = poly(rC) binding protein 1] PMID: 28512205
  12. Data suggest that C11orf98 microprotein, NPM1, and nucleolin interact and colocalize in the cell nucleolus. (C11orf98 = chromosome 11 open reading frame 98 protein; NPM1 = nucleophosmin 1) PMID: 28589727
  13. nucleolin inhibition is a new anti-pancreatic cancer therapeutic strategy that dually blocks tumor progression and normalizes tumor vasculature in pancreatic ductal adenocarcinoma PMID: 27754848
  14. It has been found that during microtubule growth phases, nucleolin affects both the speed and life time of microtubule polymerization. PMID: 27309529
  15. Interaction of Host Nucleolin with Influenza A Virus Nucleoprotein in the Early Phase of Infection Limits the Late Viral Gene Expression PMID: 27711134
  16. A yeast display library based on an engineered IgG1 CH2 scaffold with diversified loop regions was constructed, and CH2 binders were isolated by panning against nucleolin. PMID: 28202413
  17. A portion of HS-anMan colocalized with nucleolin at small discrete sites, while most of the nucleolin and nascent RNA was dispersed. In U87 cells, HS-anMan, nucleolin and nascent RNA reassembled after prolonged hypoxia. PMID: 28300561
  18. our findings identified a novel role of NCL in influenza virus life cycle and established NCL as one of the host cell surface proteins for the entry of influenza A virus. PMID: 27085069
  19. C23 on the cell surface may be a kind of indispensable component in activation of EGFR signaling, by which C23 can participate in the growth and invasion of cervical tumors PMID: 26254615
  20. These data suggest that nucleolin could be an effective treatment target and prognostic factor for patients with non-small cell lung cancer PMID: 26846099
  21. These findings demonstrate that nucleolin expression is down-regulated by miR-194 and miR-206 and upregulated by HuR. PMID: 27221739
  22. Nucleolin overexpression is associated with ependymoma. PMID: 26615563
  23. Nucleolin stabilizes oncostatin-M mRNA by binding to a GC-rich element in its 3'UTR. PMID: 26399567
  24. Data show that nucleolin (NCL) antagonist N6L inhibits cell growth with different sensitivity depending to NCL localization. PMID: 26540346
  25. HAUSP-nucleolin interaction is regulated by p53-Mdm2 complex in response to DNA damage. PMID: 26238070
  26. These results suggested a clear link between nucleolin expression (including cell membrane nucleolin) and the stem cell-like phenotype in breast cancer, namely in the triple negative molecular subtype. PMID: 26283155
  27. Identification of NCL as a prominent host factor capable of binding with high affinity to the G4 structures present in the LTR promoter of HIV-1. PMID: 26354862
  28. NCL overexpression is involved in liver carcinogenesis. PMID: 25938538
  29. NCL is implicated in the initiation and transduction of EGFR and CXCR4 signaling in the esophageal squamous cell carcinomas.NCL is expressed in the esophageal squamous cell carcinoma tissues with metastasis in the cell membrane, cytoplasm and nucleus. PMID: 25631630
  30. Data suggest that NCL (nucleolin) is re-localized during lytic KSHV (Kaposi sarcoma-associated herpesvirus) infection and protects IL6 (interleukin-6) mRNA from SOX (KSHV cytoplasmic mRNA-specific endonuclease) degradation in cytoplasm. PMID: 25965334
  31. The involvement of cell surface nucleolin in the initiation of CCR6 signaling in human hepatocellular carcinoma.Expression of nucleolin and CCR6 correlates with overall survival in hepatocellular carcinoma patients. PMID: 25698534
  32. C23 protein meditates bone morphogenetic protein-2-mediated epithelial-to-mesenchymal transition via up-regulation of Erk1/Erk2 and Akt in gastric cancer.Correlations between C23, BMPRII expression and prognosis of gastric cancer patients. PMID: 25698539
  33. study dissects nucleolin-mediated activation of surface AC133 and its cognate gene CD133, via specific interaction of nucleolin with the tissue-dependent CD133 promoter P1 PMID: 26183533
  34. Inhibition of C23 expression was shown to increase the radiosensitivity of NSCLC cells, as implied by the relevance to the notably decreased DNA-PKcs phosphorylation activity at the S2056 and T2609 clusters. PMID: 25921135
  35. the multiple functions of NCL that are associated to its multiple cellular localization can participate to the development of cancer. PMID: 25866190
  36. Nucleolin down-regulation is involved in ADP-induced cell cycle arrest in S phase and cell apoptosis in vascular endothelial cells. PMID: 25290311
  37. This study uncovered a new role for nucleolin in restricting microtubule nucleation and anchoring at centrosomes in interphase cells. PMID: 25590348
  38. C1q exists as the C1 complex (C1qC1r2C1s2), and C1q binding to ligands activates the C1r/C1s proteases. Incubation of nucleoli with C1 caused degradation of the nucleolar proteins nucleolin and nucleophosmin 1. T PMID: 26231209
  39. Increasing expression of nucleolin may be associated with aggressive characteristics of human hepatocellular carcinoma. PMID: 25230759
  40. Lrrc34, a novel nucleolar protein, interacts with npm1 and ncl and has an impact on pluripotent stem cells PMID: 24991885
  41. Data show that nucleolin and endogenous galectin-3 exist in the same complexes in the nucleolus, the cytoplasm, and on the cell surface of melanoma cells. PMID: 25169435
  42. Induced expression of NCL with mutated CK2 phosphorylation sites stabilizes p53, results in higher expression of Bcl2 (B-cell lymphoma 2) homology 3 (BH3)-only apoptotic markers and causes a dominant-negative effect on cell viability. PMID: 25313645
  43. Combined inhibition of nucleolin and ras prevents EGFR activation in glioblastoma cells, additively reducing tumorigenicity. PMID: 25261371
  44. nucleolin may interact with more G protein-coupled receptors, at least chemokine receptor. Our study will lay a new foundation for cancer therapy by antagonizing nucleolin and CXCR4. PMID: 25326811
  45. Studies identify nucleolin as an unconventional epigenetic regulator in leukemia cells and demonstrate nucleolin-NFkappaB-DNMT1 axis as a new molecular pathway underlying AML leukemogenesis. PMID: 25015109
  46. Nucleolin was overexpressed in HCCLM9 cells at the protein and mRNA level. So nucleolin is a novel potential biomarker for the metastasis of hepatocellular carcinoma and a possible therapeutic target for the treatment of hepatocellular carcinoma patients. PMID: 24927373
  47. results for the first time demonstrate that nucleolin-SUMO at K294R plays a critical role in its nucleus sequestration and gadd45alpha mRNA binding activity. PMID: 25561743
  48. this study identified a novel role of the cleavage form of NCL generated by MMP7 in stabilizing MMP9 mRNA. PMID: 24632608
  49. Authors show that the largely nuclear P-protein isoform P3 can localize to nucleoli and forms specific interactions with nucleolin. PMID: 25428867
  50. Transient nucleolar localization of FMRP underlies a strong nucleocytoplasmic translocation, in a complex with nucleolin in order to regulate translation of its target mRNAs. PMID: 24658146

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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