Nucleolar transcription factor 1/UBTF Protein, Human (His-SUMO)

The nucleolar transcription factor 1/UBTF protein critically activates RNA polymerase I-mediated transcription by binding to the ribosomal RNA gene promoter and cooperating with the SL1/TIF-IB complex. Nucleolar transcription factor 1/UBTF Protein, Human (His-SUMO) is the recombinant human-derived Nucleolar transcription factor 1/UBTF protein, expressed by E. coli , with N-SUMO, N-6*His labeled tag.

The Nucleolar transcription factor 1/UBTF protein plays a crucial role in transcriptional activation mediated by RNA polymerase I by recognizing the ribosomal RNA gene promoter and engaging in cooperative interactions with the transcription factor SL1/TIF-IB complex. Specifically binding to the upstream control element, UBTF functions as a homodimer and interacts with various proteins, including TBP, TAF1A, RASL11A, IRS1, PIK3CA, DHX33, PHF6, CEBPA (isoform 1 and isoform 4), DDX11, NOP53, and ALKBH2. These interactions highlight the protein's involvement in diverse cellular processes, emphasizing its regulatory role in ribosomal RNA gene transcription and its association with key factors implicated in transcriptional control and nucleolar function.

Human

E. coli

N-SUMO;N-6*His

P17480 (M1-T670)

7343  [NCBI]

Partial

MNGEADCPTDLEMAAPKGQDRWSQEDMLTLLECMKNNLPSNDSSKFKTTESHMDWEKVAFKDFSGDMCKLKWVEISNEVRKFRTLTELILDAQEHVKNPYKGKKLKKHPDFPKKPLTPYFRFFMEKRAKYAKLHPEMSNLDLTKILSKKYKELPEKKKMKYIQDFQREKQEFERNLARFREDHPDLIQNAKKSDIPEKPKTPQQLWYTHEKKVYLKVRPDATTKEVKDSLGKQWSQLSDKKRLKWIHKALEQRKEYEEIMRDYIQKHPELNISEEGITKSTLTKAERQLKDKFDGRPTKPPPNSYSLYCAELMANMKDVPSTERMVLCSQQWKLLSQKEKDAYHKKCDQKKKDYEVELLRFLESLPEEEQQRVLGEEKMLNINKKQATSPASKKPAQEGGKGGSEKPKRPVSAMFIFSEEKRRQLQEERPELSESELTRLLARMWNDLSEKKKAKYKAREAALKAQSERKPGGEREERGKLPESPKRAEEIWQQSVIGDYLARFKNDRVKALKAMEMTWNNMEKKEKLMWIKKAAEDQKRYERELSEMRAPPAATNSSKKMKFQGEPKKPPMNGYQKFSQELLSNGELNHLPLKERMVEIGSRWQRISQSQKEHYKKLAEEQQKQYKVHLDLWVKSLSPQDRAAYKEYISNKRKSMTKLRGPNPKSSRTT

Approximately 95 kDa, based on SDS-PAGE under reducing conditions.

• 
  ≥ 90%, as determined by reducing SDS-PAGE.

<1.0 EU/μg, determined by LAL method.