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Homo sapiens


Characteristics: The use of recombinant protein expression vectors containing the EBV oriP in cell lines stably expressing EBV's EBNA1 protein significantly increases recombinant protein yield. Transfected with: UniProtKB; P03211; EBV EBNA1. Transformant: NCBI_TaxID; 28285; Adenovirus 5. DT Created: 04-04-12; Last updated: 05-07-19; Version: 17

Proper Citation

ATCC Cat# CRL-10852, RRID:CVCL_6974




Transformed cell line DT Created: 04-04-12; Last updated: 05-07-19; Version: 17


DT Created: 04-04-12; Last updated: 05-07-19; Version: 17


293 c18, 293c18, HEK 293 c18, HEK-293 c18, HEK293-EBNA1, HEK-293-EBNA, HEK 293-EBNA, HEK 293 EBNA, HEK293EBNA, 293 EBNA, 293-EBNA1, 293-EBNA, 293/EBNA, 293EBNA, EBNA-293, EBNA293, 293E, HEK293E, HEK/EBNA, HEK-EBNA, HEK.EBNA, 293/EBNA-1 DT Created: 04-04-12, Last updated: 05-07-19, Version: 17



Cat Num


Cross References

BTO; BTO:0002974 CLO; CLO_0001231 ATCC; CRL-10852 CCRID; 3111C0001CCC000152 FCS-free; 6-2-513-1-16-12 TOKU-E; 242 TOKU-E; 3609 TOKU-E; 3672 Wikidata; Q54882445 DT Created: 04-04-12; Last updated: 05-07-19; Version: 17


DT Created: 04-04-12; Last updated: 05-07-19; Version: 17

Originate from Same Individual

DT Created: 04-04-12; Last updated: 05-07-19; Version: 17

Publications that use this research resource

IGF2 mRNA binding protein-2 is a tumor promoter that drives cancer proliferation through its client mRNAs IGF2 and HMGA1.

  • Dai N
  • Elife
  • 2017 Jul 28

Literature context:


The gene encoding the Insulin-like Growth Factor 2 mRNA binding protein 2/IMP2 is amplified and overexpressed in many human cancers, accompanied by a poorer prognosis. Mice lacking IMP2 exhibit a longer lifespan and a reduced tumor burden at old age. Herein we show in a diverse array of human cancer cells that IMP2 overexpression stimulates and IMP2 elimination diminishes proliferation by 50-80%. In addition to its known ability to promote the abundance of Insulin-like Growth Factor 2/IGF2, we find that IMP2 strongly promotes IGF action, by binding and stabilizing the mRNA encoding the DNA binding protein HMGA1, a known oncogene. HMGA1 suppresses the abundance of IGF binding protein 2/IGFBP2 and Grb14, inhibitors of IGF action. IMP2 stabilization of HMGA1 mRNA plus IMP2 stimulated IGF2 production synergistically drive cancer cell proliferation and account for IMP2's tumor promoting action. IMP2's ability to promote proliferation and IGF action requires IMP2 phosphorylation by mTOR.

Funding information:
  • NHLBI NIH HHS - 01HL118386(United States)
  • NIDDK NIH HHS - P30 DK040561()
  • NIDDK NIH HHS - P30 DK043351()
  • NIDDK NIH HHS - P30 DK057521()
  • NIDDK NIH HHS - R37 DK017776()

Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity.

  • Krotee P
  • Elife
  • 2017 Jan 3

Literature context:


hIAPP fibrils are associated with Type-II Diabetes, but the link of hIAPP structure to islet cell death remains elusive. Here we observe that hIAPP fibrils are cytotoxic to cultured pancreatic β-cells, leading us to determine the structure and cytotoxicity of protein segments composing the amyloid spine of hIAPP. Using the cryoEM method MicroED, we discover that one segment, 19-29 S20G, forms pairs of β-sheets mated by a dry interface that share structural features with and are similarly cytotoxic to full-length hIAPP fibrils. In contrast, a second segment, 15-25 WT, forms non-toxic labile β-sheets. These segments possess different structures and cytotoxic effects, however, both can seed full-length hIAPP, and cause hIAPP to take on the cytotoxic and structural features of that segment. These results suggest that protein segment structures represent polymorphs of their parent protein and that segment 19-29 S20G may serve as a model for the toxic spine of hIAPP.