Recombinant Human Transcription Initiation Factor Iib (GTF2B) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-10237P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Transcription Initiation Factor Iib (GTF2B) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-10237P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Human Transcription Initiation Factor Iib (GTF2B) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q00403
Target Symbol GTF2B
Synonyms General transcription factor IIB; General transcription factor TFIIB; gtf2b; RNA polymerase II transcription factor IIB; S300 II; S300-II; TF IIB; TF2B; TF2B_HUMAN; TFIIB; Transcription initiation factor IIB
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence MASTSRLDALPRVTCPNHPDAILVEDYRAGDMICPECGLVVGDRVIDVGSEWRTFSNDKATKDPSRVGDSQNPLLSDGDLSTMIGKGTGAASFDEFGNSKYQNRRTMSSSDRAMMNAFKEITTMADRINLPRNIVDRTNNLFKQVYEQKSLKGRANDAIASACLYIACRQEGVPRTFKEICAVSRISKKEIGRCFKLILKALETSVDLITTGDFMSRFCSNLCLPKQVQMAATHIARKAVELDLVPGRSPISVAAAAIYMASQASAEKRTQKEIGDIAGVADVTIRQSYRLIYPRAPDLFPTDFKFDTPVDKLPQL
Expression Range 1-316aa
Protein Length Full Length
Mol. Weight 50.8kDa
Research Area Immunology
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 General transcription factor that plays a role in transcription initiation by RNA polymerase II (Pol II). Involved in the pre-initiation complex (PIC) formation and Pol II recruitment at promoter DNA. Together with the TATA box-bound TBP forms the core initiation complex and provides a bridge between TBP and the Pol II-TFIIF complex. Released from the PIC early following the onset of transcription during the initiation and elongation transition and reassociates with TBP during the next transcription cycle. Associates with chromatin to core promoter-specific regions. Binds to two distinct DNA core promoter consensus sequence elements in a TBP-independent manner; these IIB-recognition elements (BREs) are localized immediately upstream (BREu), 5'-[GC][GC][GA]CGCC-3', and downstream (BREd), 5'-[GA]T[TGA][TG][GT][TG][TG]-3', of the TATA box element. Modulates transcription start site selection. Exhibits also autoacetyltransferase activity that contributes to the activated transcription.
Subcellular Location Nucleus. Chromosome.
Protein Families TFIIB family
Database References
Tissue Specificity Expressed in the inner cell mass forming the embryoblast. Not detected in cells from the outer thin layer trophoblast (at protein level).

Gene Functions References

  1. a hand-off model in which Ssu72 mediates a conformational transition in TFIIB, accounting for the role of Ssu72 in transcription reinitiation, gene looping, and promoter-terminator cross-talk. PMID: 29158257
  2. binding of specific DNA sequences changes the protein structure and dynamics, and TFIIB may exist in two conformational states PMID: 26284261
  3. The role of zinc at Cys3His1 binding site in the absence of TFIIB protein folding PMID: 26016528
  4. these results establish a new paradigm for TFIIB functionality in human gene expression, which when downregulated has potent anti-viral effects. PMID: 24441171
  5. Association of the winged helix motif of the TFIIEalpha subunit of TFIIE with either the TFIIEbeta subunit or TFIIB distinguishes its functions in transcription. PMID: 25492609
  6. TFIIB was involved in the proliferation and growth of HCC cells. PMID: 23055019
  7. a mode of phospho-TFIIB-independent transcriptional regulation that prioritizes the transcription of p53-target genes during cellular stress. PMID: 23115335
  8. Data show that TFIIF has an important role in stabilizing TFIIB within the PIC and after transcription initiates. PMID: 21896726
  9. a six-amino acid human TFIIB tip region is needed for appropriate levels of serine 5 C-terminal domain phosphorylation and mRNA capping and for retention of the required elongation factor TFIIF. PMID: 20880846
  10. phosphorylation of TFIIB at serine 65 is a critical event in transcription that links the gene promoter and terminator and triggers initiation by RNA pol II PMID: 20226668
  11. interaction with vitamin D receptor helix H10 residues PMID: 12529369
  12. Data show that human TATA box binding protein (TBP) can use a shared surface to interact with two different transcription factor IIB (TFIIB) family members to initiate transcription by different RNA polymerases. PMID: 12535529
  13. The groove in the first cyclin repeat of TFIIB is identified as the FCP1-binding site of TFIIB core domain (TFIIBc), consisting of several hydrophobic and several basic amino acids. PMID: 12578358
  14. lack of role in bending of TATA-binding protein simultaneously with promotoer DNA PMID: 12791683
  15. TFIIB interacts with SP1/SP3 at the SP1 site, besides its association with EAR3 and the TATA-less core promoter region. PMID: 12972613
  16. in addition to its role in regulating TBP binding to a TATA box, the TBP surface is unexpectedly involved in TBP association with all three TFIIB family members PMID: 14585974
  17. The structural role of Zn2+ binding to the the zinc-ribbon domain of TFIIB was analysed. PMID: 14641108
  18. Results identify a small nonconserved surface of the transcription factor TFIIB zinc ribbon that is required for RNA polymerase II (pol II) transcription in vivo and for different types of basal pol II transcription in vitro. PMID: 15024075
  19. A TFIIB conformational change is critical for the formation of activator-dependent transcription complexes. PMID: 15037660
  20. Collapse of the transcription bubble defines the RNA polymerase II promoter clearance transition. PMID: 15989968
  21. high level of TFIIB can bypass the Mediator requirement for basal transcription and pol II recruitment in nuclear extract PMID: 16595664
  22. Together, our results support a mode of preinitiation complex assembly in which TFIIB/RNA polymerase II recruitment to the promoter occurs in vivo. PMID: 16878124
  23. TFIIB binding is required for the interferon antagonist effect exerted by Thogoto virus M protein. PMID: 18768974
  24. slipping at juncture is induced by TATA-binding protein and transcription factor IIB and requires a TATA box but not a transcription factor IIB recognition sequence PMID: 19193635
  25. TFIIF in HeLa cell nuclear extract helps to rescue the inactive mutations by interacting with either the B-finger or another component of the initiation complex that is influenced by the B-finger PMID: 19590095

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

Recently viewed