Recombinant Human General transcription factor IIF subunit 1 (GTF2F1)

Code CSB-YP010004HU
MSDS
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Source Yeast
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Code CSB-EP010004HU
MSDS
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Source E.coli
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Code CSB-EP010004HU-B
MSDS
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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-BP010004HU
MSDS
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Source Baculovirus
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Code CSB-MP010004HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
GTF2F1
Uniprot No.
Alternative Names
2810405L04Rik; BTF4; C76800; General transcription factor IIF 74 kDa subunit; General transcription factor IIF subunit 1; General transcription factor IIF; polypeptide 1; 74kDa; Gtf2f1; MGC94148; OTTHUMP00000237859; RAP74; T2FA_HUMAN; TF2F1; TFIIF; TFIIF-alpha; Transcription initiation factor IIF subunit alpha; Transcription initiation factor RAP74
Species
Homo sapiens (Human)
Expression Region
2-517
Target Protein Sequence
AALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD LSNKKIYQEE EMPESGAGSE FNRKLREEAR RKKYGIVLKE FRPEDQPWLL RVNGKSGRKF KGIKKGGVTE NTSYYIFTQC PDGAFEAFPV HNWYNFTPLA RHRTLTAEEA EEEWERRNKV LNHFSIMQQR RLKDQDQDED EEEKEKRGRR KASELRIHDL EDDLEMSSDA SDASGEEGGR VPKAKKKAPL AKGGRKKKKK KGSDDEAFED SDDGDFEGQE VDYMSDGSSS SQEEPESKAK APQQEEGPKG VDEQSDSSEE SEEEKPPEED KEEEEEKKAP TPQEKKRRKD SSEESDSSEE SDIDSEASSA LFMAKKKTPP KRERKPSGGS SRGNSRPGTP SAEGGSTSST LRAAASKLEQ GKRVSEMPAA KRLRLDTGPQ SLSGKSTPQP PSGKTTPNSG DVQVTEDAVR RYLTRKPMTT KDLLKKFQTK KTGLSSEQTV NVLAQILKRL NPERKMINDK MHFSLKE
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.

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Target Background

Function
TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.
Gene References into Functions
  1. An AR motif of the transactivation domain has been identified that contributes to transcriptional activity by recruiting the C-terminal domain of subunit 1 of the general transcription regulator TFIIF. PMID: 29225078
  2. These results suggest that Mediator structural shifts induced by activator binding help stably orient pol II prior to transcription initiation within the human mediator-RNA polymerase II-TFIIF assembly. PMID: 22343046
  3. Gdown1 competes with TFIIF for binding to the RPB1 and RPB5 subunits of Pol II, thereby inhibiting an essential function of TFIIF in preinitiation complex assembly. PMID: 22244332
  4. role of associated carboxyl-terminal domain phosphatase in dephosphorylating phosphoserines 2 and 5 of RNA polymerase II PMID: 12351650
  5. The alpha 1 helix of human RAP74 has an important role in the initiation and elongation of RNA chains PMID: 12354769
  6. The NMR solution structure of the C-terminal domain of RAP74 has been determined, and NMR methods have been used to map the binding sites of the C-terminus of CTD phosphatase/FCP1 on the RAP74 C-terminal fragment. PMID: 12578358
  7. cocrystal structure of the winged-helix domain of human RNA polymerase II-associating protein 74 bound to the alpha-helical C terminus of human FCP1 PMID: 12591941
  8. NMR structure of a complex containing this TFIIF subunit and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1. PMID: 12732728
  9. Interaction of TFIIF subunit RAP74 with recombinant androgen receptor N-terminal activation domain AF1 leads to imposition of helical structure on the AF1 domain. PMID: 15023052
  10. TFIIF supports elongation and suppresses pausing by stabilizing the post-translocated elongation complex PMID: 15351637
  11. alpha1-Helix of RAP74 is important for supporting NTP-driven translocation by RNAP II. PMID: 15831464
  12. TFIIF and Rpb7 are involved in both early and late transcriptional stages PMID: 17848138
  13. Mutated hydrophobic residues in RAP74 C-terminal structure disrupt secondary structure elements, showing that binding of the androgen receptor N-terminal domain depends upon helix 3 in the winged-helix domain of the RAP74 C-terminal domain polypeptide. PMID: 18284209
  14. NMR and thermodynamic studies further elucidate the complex molecular mechanism by which TFIIF and FCP1 cooperate for RNAPII recycling. PMID: 19215094

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Subcellular Location
Nucleus.
Protein Families
TFIIF alpha subunit family
Database Links

HGNC: 4652

OMIM: 189968

KEGG: hsa:2962

STRING: 9606.ENSP00000377969

UniGene: Hs.68257

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