TAF II p100 Polyclonal Antibody
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- 实验流程
- 背景知识
Application
| WB, IHC-P, IF, ICC, E |
|---|---|
| Primary Accession | Q15542 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 86830 Da |
| Gene ID | 6877 |
|---|---|
| Other Names | TAF5; TAF2D; Transcription initiation factor TFIID subunit 5; Transcription initiation factor TFIID 100 kDa subunit; TAF(II)100; TAFII-100; TAFII100 |
| Dilution | WB~~Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/100 - 1/300. ELISA: 1/5000. Not yet tested in other applications. IHC-P~~1:50~200 IF~~1:50~200 ICC~~N/A E~~N/A |
| Format | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.09% (W/V) sodium azide. |
| Storage Conditions | -20℃ |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | TAF5 |
|---|---|
| Synonyms | TAF2D |
| Function | The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473, PubMed:8758937, PubMed:8942982, PubMed:9045704). The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (PubMed:33795473). TAF5 is involved in two modules of TFIID, in TFIID-A together with TAF3 and TBP, and in TFIID-B with TAF8 (PubMed:33795473). Involved in contacts between TFIID and TFIIF in the PIC (PubMed:33795473). |
| Cellular Location | Nucleus. |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription. TAF5/TAFII100 interacts strongly with the histone H4-related TAF6/TAFII80 and the histone H3-related TAF9/TAFII31, as well as a stable complex comprised of both TAF5/TAFII80 and TAF6/TAFII31. Apparently weaker interactions of TAF5/TAFII100 with TBP, TAF1/TAFII250, TAF11/TAFII28, and TAF12/TAFII20, but not TAF7/TAFII55, also have been observed.
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