Recombinant Human Far upstream element-binding protein 1 (FUBP1)

Code CSB-YP846584HU
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Source Yeast
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Code CSB-EP846584HU
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Source E.coli
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Code CSB-EP846584HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP846584HU
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Source Baculovirus
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Code CSB-MP846584HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
FUBP1
Uniprot No.
Alternative Names
DNA helicase V; far upstream element (FUSE) binding protein 1; Far upstream element (FUSE) binding protein 4; Far upstream element binding protein 1; far upstream element binding protein; Far upstream element-binding protein 1; FBP; FUBP; Fubp1; FUBP1_HUMAN; Fubp4; FUSE binding protein 1; FUSE-binding protein 1; HDH V
Species
Homo sapiens (Human)
Expression Region
2-644
Target Protein Sequence
ADYSTVPPP SSGSAGGGGG GGGGGGVNDA FKDALQRARQ IAAKIGGDAG TSLNSNDYGY GGQKRPLEDG DQPDAKKVAP QNDSFGTQLP PMHQQQSRSV MTEEYKVPDG MVGFIIGRGG EQISRIQQES GCKIQIAPDS GGLPERSCML TGTPESVQSA KRLLDQIVEK GRPAPGFHHG DGPGNAVQEI MIPASKAGLV IGKGGETIKQ LQERAGVKMV MIQDGPQNTG ADKPLRITGD PYKVQQAKEM VLELIRDQGG FREVRNEYGS RIGGNEGIDV PIPRFAVGIV IGRNGEMIKK IQNDAGVRIQ FKPDDGTTPE RIAQITGPPD RCQHAAEIIT DLLRSVQAGN PGGPGPGGRG RGRGQGNWNM GPPGGLQEFN FIVPTGKTGL IIGKGGETIK SISQQSGARI ELQRNPPPNA DPNMKLFTIR GTPQQIDYAR QLIEEKIGGP VNPLGPPVPH GPHGVPGPHG PPGPPGPGTP MGPYNPAPYN PGPPGPAPHG PPAPYAPQGW GNAYPHWQQQ APPDPAKAGT DPNSAAWAAY YAHYYQQQAQ PPPAAPAGAP TTTQTNGQGD QQNPAPAGQV DYTKAWEEYY KKMGQAVPAP TGAPPGGQPD YSAAWAEYYR QQAAYYAQTS PQGMPQHPPA PQGQ
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription.
Gene References into Functions
  1. High FUBP1 expression is associated with low Chemosensitivity to Adriamycin in Gastric Cancer. PMID: 28667493
  2. Low FUBP1 expression is associated with adenovirus infection. PMID: 29743362
  3. These results suggest that the interference with the FUBP1/FUSE interaction as a further molecular mechanism that, in addition to the inactivation of TOP1, may contribute to the therapeutic potential of camptothecin/SN-38. PMID: 29031818
  4. The findings demonstrate an association between FUBP1 levels and chordoma progression and prognosis, suggesting that FUBP1 can be used as a biomarker and a potential therapeutic target. PMID: 28780352
  5. we identified cyclin J and far upstream element-binding protein 1 (FUBP1) as novel miR-16 targets, which mediate miR-16 antiproliferative effects. PMID: 27157613
  6. FUBP1 acts as a potential oncogene in clear cell renal cell carcinoma (ccRCC) and may be considered as a novel biomarker or an attractive treatment target of ccRCC. PMID: 28076379
  7. FBP1 expression in Bcell lymphoma was also associated with poor survival outcomes. Functionally, small interfering RNAmediated silencing of FBP1 was able to inhibit the proliferation of Bcell lymphoma cells, resulting in G0/G1 phase cell cycle arrest. PMID: 27599538
  8. FUBP1 may potentially stimulate c-Myc expression in ESCC and its expression may promote esophageal squamous cell carcinoma progression. PMID: 26490982
  9. With the advent of large-scale genome sequencing technology, molecular genetic alterations in FUBP1 promoter have now been identified in the majority of oligodendrogliomas PMID: 26545048
  10. direct connection between the cellular PI3K/AKT/mTOR signaling pathway, frequently activated in human hepatocarcinogenesis, and the enrichment of oncogenic transcription factors of the FBP family PMID: 26901106
  11. Concomitant overexpression of far upstream element (FUSE) binding protein (FBP) interacting repressor (FIR) and its splice variants induce migration and invasion of non-small cell lung cancer cells. PMID: 26177862
  12. FBP1 promotes hepatitis C virus eplication by inhibiting p53 expression. PMID: 25995247
  13. High FBP1 expression was observed in glioma. PMID: 24347226
  14. Apoptosis-mediated cleavage of FBP1 and its decreased expression in epithelial cells induces cell cycle arrest, which may play an important role in colonic epithelial disruption in colitis. PMID: 24966911
  15. We conclude that absent CIC and FUBP1 expressions are potential markers of shorter time to recurrence in oligodendroglial tumors. PMID: 24030748
  16. These findings are the first report describing the regulation of alternative splicing of MDM2 mediated by the oncogenic factor FUBP1. PMID: 24798327
  17. The data indicates an association between FUBP1 expression and proliferation in gliomas. PMID: 24117486
  18. FUBP1 expression differs among gastric tissues; there is a correlation between overall survival rates and age, sex, lymph node metastasis, and distant metastasis. PMID: 24192769
  19. Far upstream element-binding protein 1 and RNA secondary structure both mediate second-step splicing repression. PMID: 23818605
  20. biochemical features of FBP1 PMID: 22926519
  21. Analysis allowed us to define two highly recurrent genetic signatures in gliomas: IDH1/ATRX (I-A) and IDH1/CIC/FUBP1 (I-CF). PMID: 22869205
  22. Found CIC and FUBP1 mutations in oligodendrogliomas and demonstrate the presence of these mutations in oligoastrocytomas. PMID: 22588899
  23. increased polyubiquitination of FBP1 does not alter its protein stability, but instead modulates the stable recruitment of FBP1 to target loci PMID: 21779003
  24. The central domain of FBP1, containing four K homology motifs, was required for p27 5'-UTR RNA binding and the N terminal domain was important for translational activation. PMID: 21855647
  25. CIC gene was mutated in 6 oligodendrogliomas and FUBP1 gene was mutated in 2; 27 additional oligodendrogliomas showed 12 and 3 more tumors with mutations of CIC and FUBP1; results suggest role of these genes in biology and pathology of oligodendrocytes PMID: 21817013
  26. The authors suggest that FUSE binding protein 1 binds with the Japanese encephalitis virus untranslated RNA and functions as a host anti-virus defense molecule by repressing viral protein expression. PMID: 21367899
  27. Authors propose that FBP1 is a key regulator of cell growth and proliferation through its ability to selectively bind the NPM 3' UTR and repress NPM translation. PMID: 20802533
  28. The noncoding strand FUSE recruits an activator FUSE-binding protein (FBP) and a repressor FBP-interacting repressor (FIR) to fine-tune c-myc transcription. PMID: 20420426
  29. Results describe the roles of the FarUpStream Element (FUSE), FUSE Binding Protein (FBP), FBP Interacting Repressor (FIR), and TFIIH in the regulation of c-myc expression. PMID: 16628215
  30. FUBP1 is an authentic substrate of Parkin that might play an important role in development of Parkinson disease pathology along with aminoacyl-tRNA synthetase interacting multifunctional protein type 2 PMID: 16672220
  31. investigate the contributions of FBP's 4 K Homology (KH) domains to sequence selectivity. EMSA and missing contact point analysis revealed that FBP contacts 4 separate patches spanning a large segment of FUSE PMID: 19015535
  32. study found that FBP1 as well as FBP3 are more frequently expressed in prostate and bladder cancer than in renal cancer; in addition, a positive correlation between levels of FBP1, FBP3 and c-Myc was exclusively detectable in renal cell carcinomas PMID: 19087307
  33. oncogenic potential of c-Myc is 'switched off' after apoptosis induction as a consequence of the caspase-mediated cleavage of FBP-1. PMID: 19219071
  34. FBP1 is an important oncoprotein overexpressed in hepatocellular carcinoma that induces tumor propagation through direct or indirect repression of cell cycle inhibitors and proapoptotic target genes. PMID: 19637194

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Subcellular Location
Nucleus.
Database Links

HGNC: 4004

OMIM: 603444

KEGG: hsa:8880

STRING: 9606.ENSP00000359804

UniGene: Hs.567380

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