Recombinant Human Nucleolar Transcription Factor 1 (UBTF) Protein (His-SUMO)

Name: Recombinant Human Nucleolar Transcription Factor 1 (UBTF) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-02125P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Nucleolar Transcription Factor 1 (UBTF) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P17480
Target Symbol	UBTF
Synonyms	UBTF; UBF; UBF1; Nucleolar transcription factor 1; Autoantigen NOR-90; Upstream-binding factor 1; UBF-1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MNGEADCPTDLEMAAPKGQDRWSQEDMLTLLECMKNNLPSNDSSKFKTTESHMDWEKVAFKDFSGDMCKLKWVEISNEVRKFRTLTELILDAQEHVKNPYKGKKLKKHPDFPKKPLTPYFRFFMEKRAKYAKLHPEMSNLDLTKILSKKYKELPEKKKMKYIQDFQREKQEFERNLARFREDHPDLIQNAKKSDIPEKPKTPQQLWYTHEKKVYLKVRPDATTKEVKDSLGKQWSQLSDKKRLKWIHKALEQRKEYEEIMRDYIQKHPELNISEEGITKSTLTKAERQLKDKFDGRPTKPPPNSYSLYCAELMANMKDVPSTERMVLCSQQWKLLSQKEKDAYHKKCDQKKKDYEVELLRFLESLPEEEQQRVLGEEKMLNINKKQATSPASKKPAQEGGKGGSEKPKRPVSAMFIFSEEKRRQLQEERPELSESELTRLLARMWNDLSEKKKAKYKAREAALKAQSERKPGGEREERGKLPESPKRAEEIWQQSVIGDYLARFKNDRVKALKAMEMTWNNMEKKEKLMWIKKAAEDQKRYERELSEMRAPPAATNSSKKMKFQGEPKKPPMNGYQKFSQELLSNGELNHLPLKERMVEIGSRWQRISQSQKEHYKKLAEEQQKQYKVHLDLWVKSLSPQDRAAYKEYISNKRKSMTKLRGPNPKSSRTT
Expression Range	1-670aa
Protein Length	Partial
Mol. Weight	95.2 kDa
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.
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	Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element.
Subcellular Location	Nucleus, nucleolus.
Database References	HGNC: 12511 OMIM: 600673 KEGG: hsa:7343 STRING: 9606.ENSP00000302640 UniGene: PMID: 27172002 Study demonstrated that HMG box 1, the linker region between the HMG boxes and C-terminal acidic region (AR), and the AR cooperatively regulate the nucleolar localization of UBF. PMID: 28874518 In seven unrelated affected individuals, all suffering from developmental regression starting at 2.5-7 years, the authors identified a heterozygous variant, c.628G>A in UBTF, encoding p.Glu210Lys in UBF, which occurred de novo in all cases. PMID: 28777933 RINT-1 interacts with MSP58 and UBF within nucleoli and plays a role in ribosomal gene transcription. PMID: 27530925 This study provides some compelling evidences in support of HBx-elicited and c-Myc-mediated increase in UBF levels that abets oncogenic onslaught in hepatic cells by increasing rDNA transcription and ribosome biogenesis. PMID: 25890091 These results suggest that UBF can inhibit gene expression from viral DNA prior to its replication. PMID: 25965800 we have uncovered a novel role for UBTF1 and UBTF2 in maintaining genome stability through coordinating the expression of highly transcribed Pol I (UBTF1 activity) and Pol II genes (UBTF2 activity). PMID: 25452314 p14ARF fails to prevent E7-mediated UBF1 phosphorylation, but could facilitate nucleolar pRb inactivation by targeting E7 to the nucleolus. PMID: 24798431 PIP2 depletion reduces Pol I transcription. PMID: 23591814 UBF is expressed widely by human multiple fetal tissue,s and the expression level is very high in HL-60 cells. PMID: 21162312 Downregulation of RUNX2 expression reduces the localization of HDAC1 to the nucleolar periphery and also decreases the association between HDAC1 and UBF. PMID: 22393235 hALP binds the upstream binding factor (UBF) in vivo and in vitro PMID: 21177859 depletion of upstream binding factor (UBF; an rRNA transcription factor) decreased the chromatin binding affinity of B23, which in turn led to an increase in histone density at the r-chromatin PMID: 20713446 The three-dimensional solution structure of the first high mobility group (HMG) box domain in upstream binding factor has been determined by multidimensional NMR. PMID: 11969401 we have identified an interaction between UBF and TAF1, a factor involved in the transcription of cell cycle and growth regulatory genes. Coimmunoprecipitation and protein-protein interaction assays confirmed that TAF1 binds to UBF. PMID: 12498690 The DNA binding affinity of UBF's fifth box domain (HMG box 5) is found to be much weaker than that of the first HMG box domain (HMG box 1). PMID: 12590579 Data show that both UBF1 and UBF2 activate RNA polymerase II-regulated, beta-catenin-responsive promoters. PMID: 12748295 Proto-Oncogene Proteins c-myc activated transcription from the UBF promoter PMID: 15282543 results suggest that extensive binding of UBF is responsible for formation and maintenance of the secondary constriction at active NORs, and that UBF mediates recruitment of the pol I machinery to nucleoli independently of promoter elements PMID: 15598984 Data suggest that the A state of human upstream binding factor HMG Box1 could represent a potential folding intermediate on protein folding pathway. PMID: 15752694 A potential protein-folding pathway is proposed for upstream binding factor HMG box 1 domain based on the early stages of its pH 2.1 unfolded state characterized by multidimensional heteronuclear magnetic resonance spectroscopy. PMID: 15924431 SL1 directs preinitiation complex formation, functioning in core promoter binding, RNA polymerase I recruitment, and UBF stabilization. PMID: 15970593 model for CAST/hPAF49 function in which the network of interactions of Pol I-specific subunits with UBF facilitates conformational changes of the polymerase, leading to stabilization of the Pol I-template complex and, thereby, activation of transcription PMID: 16809778 UBF activates transcription in the transition between initiation and elongation, at promoter escape by RNA polymerase I (Pol I). PMID: 16858408 Upon p14ARF overexpression, UBF was found hypophosphorylated, thus unable to efficiently recruit the transcription complex, these data define a new p53-independent pathway that could regulate cell cycle through the negative control of rRNA transcription. PMID: 16924243 GdmCl-induced equilibrium unfolding transition of HMG box 5 of hUBF was monitored by both circular dichroism and fluorescence spectra. A cooperative two-state unfolding process was observed PMID: 17260958 possible sites in hUBF HMG box 5 that may interact with the first bromodomain of TAF1 were proposed PMID: 17505112 transcription factor UBF binds extensively across rDNA throughout the cell cycle, resulting in a specialized form of chromatin that is the hallmark of active nucleolar organizer regions PMID: 17699751 found a small but significant difference between the emerging daughter cells in the number of UBF-loaded NORs PMID: 18502146 The authors propose that UBF is recruited to the replication compartments to aid replication of HSV-1 DNA. PMID: 19088274 The established differential localization of UBF in nucleoli of HeLa cells has a functional meaning. It reflects both the level of rRNA synthesis activities and the architectural role of UBF in nucleoli of these cells. PMID: 19393134 these results implicate a fluid helix-turn-helix folding model of hUBF Box-5. PMID: 19452555 central repeated domain of treacle binds with RNA polymerase I, while that the treacle C-terminus is involved in rDNA promoter recognition and UBF recruitment. PMID: 19527688

FAQs

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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.