|Application ||WB, E|
|Calculated MW||23307 Da|
|Antigen Region||1-30 aa|
|Other Names||Transcription initiation factor TFIID subunit 11, TFIID subunit p30-beta, Transcription initiation factor TFIID 28 kDa subunit, TAF(II)28, TAFII-28, TAFII28, TAF11, TAF2I|
|Target/Specificity||This TAF11 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human TAF11.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||TAF11 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Core TAFII present in both of the previously described TFIID species which either lack or contain TAFII30 (TFIID alpha and TFIID beta respectively).|
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Provided below are standard protocols that you may find useful for product applications.
Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes a small subunit of TFIID that is present in all TFIID complexes and interacts with TBP. This subunit also interacts with another small subunit, TAF13, to form a heterodimer with a structure similar to the histone core structure.
Matsuoka, S., et al. Science 316(5828):1160-1166(2007)
Mungall, A.J., et al. Nature 425(6960):805-811(2003)
Guermah, M., et al. Mol. Cell 12(4):991-1001(2003)
Mengus, G., et al. J. Biol. Chem. 275(14):10064-10071(2000)
Birck, C., et al. Cell 94(2):239-249(1998)
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